UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 5
15.6k
| Functional Description
stringlengths 6
12.4k
|
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B9HBA8
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MEATLPVCKSVTSTPGLFMGKTSGIRSSQCSFMMGNKVNFPRQRAQTAHVHCAKNGGALGVTCRAEKILVANRGEIAVRVIRTAHEMGIPCVAVYSTIDKDALHVKLADESVCIGEAPSSQSYLVIPNVLSAAISRRCTMLHPGYGFLAENAVFVEMCREHGINFIGPNPDSIRVMGDKSTARETMKKAGVPTVPGSDGLLQSTEEGVRLANEIGYPVMIKATAGGGGRGMRLAKEPDEFVKLLQQAKSEAAAAFGNDGVYLEKYVQNPRHIEFQVLADKFGNVVHFGERDCSIQRRNQKLLEEAPSPALTPELRKAMGDAAVSAAASIGYIGVGTVEFLLDERGSFYFMEMNTRIQVEHPVTEMISSVDLIEEQIRVAMGEKLRYKQEDIVLRGHSIECRINAEDAFKGFRPGPGRITAYLPSGGPFVRMDSHVYPDYVVPPSYDSLLGKLIVWAPTREKAIERMKRALDDTIITGVPTTIDYHKLILEIEDFKNGNVDTAFIPKHEKELAAPQQIIPAKQLTNSAA
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This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate Binds 2 magnesium or manganese ions per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and two subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
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Q5UPP6
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MNHLNNIINRIFSQDKNKAEKISRYLTTMIDQDYITDDDENILYQFSQEFNNMSDNLFEFIGNVVNQNIVFNVPQLSIYLSEDKIDVPCSRLNTYLKCYWHKITYKSGLLREKVWVPIKDFSGNIIIERANVISYQKEDLPYLLIYISRYLKTIDYRTS
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Belongs to the mimivirus L761/L899 family.
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B8CKI4
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MSDLKKAAQQAINLMDLTTLNDDDTDQKVIDLCHKAKTPAGDTAAICIYPRFIPIARKTLNEIGGDDIKIATVTNFPHGNDDIAIAVLETRAAVAYGADEVDVVFPYRALMAGNETVGFELVKACKEACGDEAILKVIIESGVLADPALIRKASELSIDAGADFIKTSTGKVAVNATLEAAEIMMTVISEKNTKVGFKPAGGVKDAAAAAEFLGVAARLLGDDWATPATFRFGASSLLTNLLHTLELGDAPKGPQGY
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Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. Belongs to the DeoC/FbaB aldolase family. DeoC type 2 subfamily.
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Q1RGG3
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MSYYAFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANIQDGCIMHGYCDTDTIVGENGHIGHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFRGEKRQLLMGTPARAVRSVSDDELHWKRLNTKEYQDLVGRCHAALHETQPLRQMEENRPRLQGTTDVTPKR
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Overproduction of CaiE stimulates the activity of CaiB and CaiD. Amine and polyamine metabolism; carnitine metabolism. Belongs to the transferase hexapeptide repeat family.
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B6DCZ4
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MKLMIFTGLVLFAIVRLIEAQAENEKPCLPEYKVCTHAPGNCCSDLVCDCYGRYKSGAQIGRNCFCLQKGVIYKREN
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Expressed by the venom gland. Contains 4 disulfide bonds. Belongs to the neurotoxin 19 (CSTX) family. 08 (U8-Lctx) subfamily.
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P59600
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MKNKLPPFIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASYGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTALRPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGINAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLNLGHIHGGDASNRICACCELHMDIRPQPGMTLNELNGLLNDALAPVSERWPGRLTVDELHPPIPGYECPPNHQLVEVVEKLLGAKTEVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELIIQVIHHFCWH
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Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines. H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine Binds 2 Zn(2+) or Co(2+) ions per subunit. Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine from N(2)-acetyl-L-ornithine (linear): step 1/1. Homodimer. Belongs to the peptidase M20A family. ArgE subfamily.
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A9KBI4
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MLQTYKDQLPDYAKDLKLNLTQVLSESPSSELSNQQITGVALAVAYATRNRQLIELIFQKAEAELDESTLQAIKAAASIMAMNNIYYRFVHLVKDSEYQRLPANLRMNIIANPGIDKKDFELYSLAVSAINGCGLCIDAHANTLIKAGFSKHSIQHVIRIAAVLNGLAQVSIIENKT
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Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity. (R)-N(6)-dihydrolipoyl-L-lysyl-[lipoyl-carrier protein] + a hydroperoxide = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + an alcohol + H2O Belongs to the AhpD family. Extended N-terminus.
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A8F0L8
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MSEVVVKEQLEQYISKIERLEQEKADLSQEVKDIFQDASSHGFDVKAMKSILKLKKLDKDKLAEQDAMLELYRDTLGI
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Belongs to the UPF0335 family.
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Q1XDD1
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MTKVFALGWLLKINLMKTLYSLRRFYHVETPFNTTVGVGGRDIESTGFAWWSGNARLINVSGKLLGAHVAHAGIMVFWTGAMTLFEVAHFVPEKPLYEQGFILIPHLATLGWGVGPGGEIFNTYPYFVVGVVHLISSAVLGFGGLYHSLIGPDTLEESFPFFGYDWRDKNKMTTILGIHLVLLGIGAFLLVIKALFIGGVYDTWAPGGGDVRFVSNPTLNPLVIFGYVLKSPFGGDGWIVSVNNMEDLVGGHVWIGIICIAGGIWHILTKPFAWARRAFVWSGEAYLSYSLGALSIMGLTASNFVWYNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVASSQGPTGLGKYLMRSPSGEIIFGGETMRFWDLRAPWVEPLRGPNGLDLNKIKNDIQPWQERRAAEYMTHAPLGSLNSVGGVATEINSVNYVSPRSWLTTSHSFLGFFLFIGHLWHAGRARAAAAGFEKGINRENEPVLSMRPLD
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One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes. Belongs to the PsbB/PsbC family. PsbC subfamily.
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O74835
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MAGNKRKRSNASEGSDSQGNERISSLSANEATQDFPRGGASSLTPLEYKEAVLEAKKDFMESASGTAELSKKTRPKKKGSKKSSKSELDNEENLKVHIQSLRYKNITPGSLILGQIAQINTLDLAVSLPNCLTGYVPITNISDKLSDRLDSIDNHAEDNAATEEEDGLNQIPDLMDLYKVGQWVRVSVTALGSENTTKTGKRHIELSLKPQDANGSAPEAADFVAGSMIQAVVSSIEDHGIVFDIGINNYTGFLSKKHINDFPFVEGQSLLCSVISKEDRIFHLSLTATSTKALEVMPSVQAILPGDYINVLVTDIKESGVIAKYMGVVDVTSDIYHSSPVKGEDLEDKFQLAKSVPARVLFVIPGDPPKIAVSFLPHVLTFNFATPNTPHPDQLDIGFIVNAAKVTYVSSSLGVFCDVGVPEISGFAHISRLSDKKVAGISPNSGPYKVDSTHEARIINYSYVDNLYILSFQQSVLNQQFLRIEDIEVGQFVDGTIAKLIPQGIVVTISEGINGLVPSTHMADIALQFPERRFKVGSSVKCRVLSTNVLRKRVLLTLKKSLLNTDLPLIYDYEQATPGTQTVGTLARIFEDGAIVEFYNSVRAFLPVSEMSEAYIRDAREHFKVGQTLSVTIVSCDPENRKMRVGCREQSWDAKRLERFENIKAGSVLSGIVLQKTEDSVIVDLGDKVTGVITLGQLCDGDLNKCSKVMNKLRASTKLAEVLVLRKDTSKKLISLSLKKSLVEAAKENRMPINITDLKEGIKYFGFVRNATTFGVFVEFCDGLVALVPKAYISEEYVPVPSAVYKPQQSVTCVCLSVELSQEKAFMSFKPLAQKQEKAVEFMESKYDIDNPVDETIKKTYDYVAGKITWAVVTSAKASQLNVDLAANVHGRVDVSEVFDNFGEIVDPNKPLKRFHKGDKIRVRVLGIHDSRNHKFLPISHRVSPKQFLELSVRPSILNMEPFSMKEPQFKKGDEVTGFVNNVSKECVWVSLTPSVNGRIPILDLTTDVKELNSLQKHFFLGKAIKCYVVNAEDSITLSAIGPLQGFENLTPGSRLVGKVTNVNEAGAILQLPGHMSGRVSRIDMFDDYDILPETKFTRNNLVGVCVLSVDVPNRKVALSARNSRTQSQPVEIKDKEINSVDDLKIGDICRGFVCNVANQGLFVTIGHNLIARVKIGELFDTFIKDWKPHFHVNQLVKGSIVGIDNDSKRIEMSLKQSKIKDSSEITKTFADIAVGSNLDGTVVKVGDYGVLIRIDGTDNIVGLCHKSEIADAVVLNISKLYSSGDKVRAHVLDVDSEKRRIALGLKSSYFDSDSDISMSDNEEDVEMRSEDQSDTSESEVGSKDDVQSEEVENLESAGDEDEEEEPSALQANGFDWTDGSTVFDKLADDTEDSEDEEDEEPKRKKSKSDRFDDEEKDLDEIPSTAADFERQLLSSPNSSLLWISYMAYHLNLNELQEAREVGKRALSTINYREEDEKLNVWMALLNLEVAYGTEDSLKEVFKEACAYCDALIVYEKLCGILIKGGKVDLADEYMQLMLKNFKQVPSVWIQYATFLLNNDKAEKAHGLLERSLQSLPKSEHVGIIEKFAILEFKNGDPERGRTIFEGLLSSYPKRLDLWNVLIDMEMKQDDPSIVRRLFQRLLALNLSTKKAKFAFKKWLAYEKNIGDDEGAEQVKRRAIEYVSESHSEN
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Involved in the biogenesis of rRNA. Required for the formation of 18S and 5.8S rRNA (By similarity). Component of the ribosomal small subunit (SSU) processome.
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Q0WKD9
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MNNSNRIRLTWISYLSYALTGALVIVTGIVMGNIAEYFNLPIASMSNTFTFLNAGILISIFLNAWLMEIIPLKRQLVFGFILMLIAIAGLMVGHNLMIFSISMFIFGVVSGITMSIGTFLVTHMYEGRQRGSRLLFTDSFFSMAGMIFPIAAAMLLARHIEWYWVYACIGLLYVGIFVLTLCSEFPVLGHKATDQSKPVVKEKWGVGVLFLAIAALCYILGQLGFIQWVPEYATKTFNMNISQAGQLVSNFWISYMIGMWIFSFILRFFDLQRIVTVLAAMATLAMYLFVSTDNPAYLSYYILALGFVSSAIYTTLITLGSLQTKVSSPKLVNFILTCGTVGTMLTFVVTGPIVANNGVHAALETANGLYLAVFILCLALGFFTKHRSHGHVTH
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Belongs to the major facilitator superfamily. TsgA family.
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O42179
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MEPLDQTPGFPLSPEPNYWYETTPSLLLVSYPHLLDISSNQSTQSVPFQGSSALLTAVIYITVFVVGLTGNTLAIYVVLRYAGMKTVTNIYILNLAVADELYIVGLPFLATQNVLSYWPFGSFLCRVVMTADSMNQFTSIFCLTVMSIDRYLAVVHPIRSTKWRHPRVAKVVSAAVWAVSFVVVLPVVIFSDVQVRPSRPLQVGTSSKCLVKRVQETFNSCNMIWPEPKNVWSTAFILYTAMVGFFGPLLIICLCYLLIVIKVRHRMSAAQVGAVVSTCPLNICCLSRR
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Belongs to the G-protein coupled receptor 1 family. Seems to lack the C-terminal part (TM6 and TM7).
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A2S4R9
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MKSTRPFHPTPVITIDGPTASGKGTVAALVAAHLGFHLLDSGALYRLAALASIRYQVEPDDADALASLVDGLHITFREGCAQLDGVDVSDEIRAEAVGNRASAIAVHASVRAALVARQRAFRKTPGLVADGRDMGTLIFPDAVLKVFLTASVEARAARRHKQLMQKGFSANIDNLLQDLRERDARDSNRAAAPLKPAADAKPLDTSALTIEQSVEQVLAWYRELGQPA
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ATP + CMP = ADP + CDP ATP + dCMP = ADP + dCDP Belongs to the cytidylate kinase family. Type 1 subfamily.
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Q1JU72
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MFEGFERRLVDVGDVTINCVVGGSGPALLLLHGFPQNLHMWARVAPLLANEYTVVCADLRGYGGSSKPVGAPDHANYSFRAMASDQRELMRTLGFERFHLVGHDRGGRTGHRMALDHPDSVLSLAVLDIIPTYVMFEEVDRFVARAYWHWYFLQQPAPYPEKVIGADPDTFYEGCLFGWGATGADGFDPEQLEEYRKQWRDPAAIHGSCCDYRAGGTIDFELDHGDLGRQVQCPALVFSGSAGLMHSLFEMQVVWAPRLANMRFASLPGGHFFVDRFPDDTARILREFLSDARSGIHQTERRES
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Catalyzes the hydrolytic defluorination of fluoroacetate to produce glycolate. Has only very low activity towards chloroacetate. a haloacetate + H2O = a halide anion + glycolate + H(+) Optimum pH is 8.5-9.5. Homodimer. Up-regulated by fluoroacetate. Not detectable in the absence of fluoroacetate, or when cells are grown on Luria broth. Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
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Q6D4A8
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MSTLVSLNNISVTFGSRKILSDISLTLQAGRILTLLGPNGAGKSTLVRVVLGLLAPTSGSLVRDPALRIGYVPQKLHLDTTLPLTVSRFMQLRPGVKKQDILPALKRVQAAHLLEQPMQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQMALYDLINQLRQEFHCGVLMVSHDLHLVMAKTDEVLCLNQHVCCSGTPEVVSLHPEFLAMFGHRGAEQLAIYRHHHNHRHDLQGRIILKRQGGNDA
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Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family.
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Q5E586
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MNVTQQSEKEAVIKLTGISKSFDGKEVISNFDLDVNHGEFLTILGPSGCGKTTVLRMIAGFETADAGTILLDSTDVTSVPAEQRHVNTVFQSYALFPHMTVFENVAFGLRMQKVAESEIEPRVTEALQMVRLAQMANRKPHQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQIELKQLQRQLGITFIFVTHDQEEALSMSDRIIVMRDGVIEQDGTPREIYEEPKNLFVARFIGEINVFAATVQERLDEKRIKAEIEDTSAIVYCDLDVAPGDKVKVLLRPEDLRLEEIKESDNKGITGYVRERTYKGMTLDSVLELDSGMRVMISEFFNEDDPDVDHSLGQKVAITWVESWEVVLADEQEV
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Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1. The complex is composed of two ATP-binding proteins (PotA), two transmembrane proteins (PotB and PotC) and a solute-binding protein (PotD). Belongs to the ABC transporter superfamily. Spermidine/putrescine importer (TC 3.A.1.11.1) family.
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A5G7Y9
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MAGLAMNTELLRRILVGFIREEVRKIGLQKAVLGLSGGIDSALVAYLAAEALGPENVYACTMPYRTSNPESEAHARLVAERLGINYRVIEITPMVDAYFQMVPDADNMRRGNKMARERMTILYDHSAAYSALVLGTSNKTELLLGYGTLFGDMASALNPIGDIYKTQVWQLSEAMGVPREVIEKKPSADLWAGQTDEQELGFTYREVDELLYQMVDLRCNRQELIAQGFSADFIDKIYGKVQNSHFKRRLPVIAKVSTRTIDRDFRYSRDWGK
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Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+) Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. Homodimer. Belongs to the NAD synthetase family.
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A8F0N9
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MSRRHAAEKRVILPDMKYNSIVLSRFINNIMKEGKKALAEKIVYSAFNKIEKKYRVDPYQTFNNAMHNVKPHLEVTSVRVGGANYQVPTHVDERRGYALASRWIINAASKRSEKMMIDKLAEELFEASNNRGVAIKKKEDTHKMAEANKAFSHFSPKKMK
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One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. Part of the 30S ribosomal subunit. Contacts proteins S9 and S11. Belongs to the universal ribosomal protein uS7 family.
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B3STU4
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MVTKAKIPLFLFLSALFLALVCSSLALETEDLSNELNPHHDPESHRWEFQQCQERCQHEERGQRQAQQCQRRCEEQLREREREREREEIVDPREPRKQYEQCRETCEKQDPRQQPQCERRCERQFQEQQERERRERRRGRDDDDKENPRDPREQYRQCEEHCRRQGQGQRQQQQCQSRCEERFEEEQRRQEERERRRGRDNDDEENPRDPREQYRQCQEHCRRQGQGQRQQQQCQSRCEERLEEEQRKQEERERRRGRDEDDQNPRDPEQRYEQCQQQCERQRRGQEQQLCRRRCEQQRQQEERERQRGRDRQDPQQQYHRCQRRCQTQEQSPERQRQCQQRCERQYKEQQGREWGPDQASPRRESRGREEEQQRHNPYYFHSQGLRSRHESGEGEVKYLERFTERTELLRGIENYRVVILEANPNTFVLPYHKDAESVIVVTRGRATLTFVSQERRESFNLEYGDVIRVPAGATEYVINQDSNERLEMVKLLQPVNNPGQFREYYAAGAQSTESYLRVFSNDILVAALNTPRDRLERFFDQQEQREGVIIRASQEKLRALSQHAMSAGQRPWGRRSSGGPISLKSQRSSYSNQFGQFFEACPEEHRQLQEMDVLVNYAEIKRGAMMVPHYNSKATVVVYVVEGTGRFEMACPHDVSSQSYEYKGRREQEEEESSTGQFQKVTARLARGDIFVIPAGHPIAITASQNENLRLVGFGINGKNNQRNFLAGQNNIINQLEREAKELSFNMPREEIEEIFERQVESYFVPMERQSRRGQGRDHPLASILDFAGFF
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Seed storage protein. Homotrimer. Expressed in seed (at protein level) (PubMed:27128197). Expressed in seed (PubMed:25084379). Expressed during nut development. Expressed in gel stage of the seed kernel. Causes an allergic reaction in human. Binds to IgE of patients allergic to pecan nuts and walnuts. Binds to IgE in 30% of the 27 patients tested by Western blot and in 24% of the 25 patients tested by double-blind, placebo-controlled oral food challenge. Belongs to the 7S seed storage protein family.
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L0GCW2
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MQTQCTVLQLLVLVALCSCGGILKEKYFQKGVDYLTSHIPIPVVKDVVKSAAKQLVHKISKNQQLCLIVDTVQWCNKSCLAAENKEGYCHGTKCKCGIKVSY
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Has antimicrobial activity against yeasts and bacteria. Expressed by the venom gland. Belongs to the long chain scorpion toxin family. Class 3 subfamily.
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Q927L9
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MNRLKDQYLKEIVPALMSKFNYDSVMEVPKIDKIVINTGVGDATANAKVLDSAVEELALITGQKPVITKAKNSIAGFRLREGMPIGAKVTLRGERMYDFLDKLVTVSLPRVRDFRGVSKKAFDGRGNYTLGVREQLIFPEIDYDQVSKVRGMDVVIVTTAKSDEESHELLTQLGMPFQK
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This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome. Belongs to the universal ribosomal protein uL5 family.
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P13380
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MKKINIIKIVFIITVILISTISPIIKSDSKKDISNVKSDLLYAYTITPYDYKDCRVNFSTTHTLNIDTQKYRGKDYYISSEMSYEASQKFKRDDHVDVFGLFYILNSHTGEYIYGGITPAQNNKVNHKLLGNLFISGESQQNLNNKIILEKDIVTFQEIDFKIRKYLMDNYKIYDATSPYVSGRIEIGTKDGKHEQIDLFDSPNEGTRSDIFAKYKDNRIINMKNFSHFDIYLEK
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Causative agent of the symptoms associated with scarlet fever, have been associated with streptococcal toxic shock-like disease and may play a role in the early events of rheumatic fever. Superantigen that binds to major histocompatibility complex class II beta chain in a zinc-dependent manner, it may activate up to 20% of all T-cells. Superantigens bind simultaneously TCRs and MHC class II molecules resulting in a massive release of pyrogenic and inflammatory cytokines. This toxin seems to be coded by a bacteriophage. Belongs to the staphylococcal/streptococcal toxin family.
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P50978
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MSKTLPKDFIFGGATAAYQAEGATHADGKGPVAWDKYLEDNYWYTAEPASDFYHQYPVDLKLAEEFGVNGIRISIAWSRIFPKGYGAVNPKGLAFYHNLFAECHKRHVEPFVTLHHFDTPEALHSNGDFLNRENIEHFVNYAEFCFKEFPEVNYWTTFNEIGPIGDGQYLVGKFPPGIQYDLAKVFQSHHNMMVAHSKAVKLFKDGGYSGEIGVVHALPTKYPYDPNNPADIRAAELEDIIHNKFILDATYLGKYSEKTMEGVNHILAVNGGQLDLREEDFAALEAAKDLNDFLGINYYMSDWMRAFDGETEITHNAKGEKGSSKYQIKGVGRREAPVNVPKTDWDWIIYPQGLYDQIMRVKQDYPNYKKIYITENGLGYKDEFVNHTVYDDARIDYVKKHLEVLSDAIADGANVKGYFIWSLMDVFSWSNGYEKRYGLFYVDFDTQERYPKKSAYWYKKLAETQIID
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a 6-phospho-beta-D-galactoside + H2O = an alcohol + D-galactose 6-phosphate Carbohydrate metabolism; lactose degradation; D-galactose 6-phosphate and beta-D-glucose from lactose 6-phosphate: step 1/1. Belongs to the glycosyl hydrolase 1 family.
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B9KL51
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MDSILVKGNGELRGQIPIAGAKNACLALMPATLLSDEPLTLTNAPRLSDIRTMTQLLQSLGAEVASLQGGQVLALSSHALTDHRADYDIVRKMRASILVLGPMLARDGHAVVSLPGGCAIGARPVDLHLKALEAMGAELDLRDGYIHAKAPAGGLKGARVVFPLVSVGATENALMAATLAKGTTVLENAAREPEIVDLARCLRRMGAQIEGEGSSTITIEGVDRLGGATHPVVTDRIELGTYMLAPAICGGEVELLGGRIELVGAFCEKLDAAGISVEETERGLRVARKNGRVKAVDVMTEPFPGFPTDLQAQMMALLCTAEGTSVLEERIFENRFMHAPELIRMGARIEVHGGTATVTGVEKLRGAPVMATDLRASVSLILAGLAAEGETIVSRVYHLDRGYERVEEKLSACGAQIRRIPG
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Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the EPSP synthase family. MurA subfamily.
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B8EES8
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MPKMKTDKGVAKRFKKTANGFKRKQAHLRHILTKKSTKRKRHLRAKCLVSKADVPAIARQLPYA
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Belongs to the bacterial ribosomal protein bL35 family.
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Q6P7Y3
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MAGSQQQQQQQAVSKPTGGKHGNNLPLWGNEKTMNLNPMILTNVLSSPYFKVQLYELKTYHEVVDEIYFKVNHVEPWEKGSRKTAGQTGMCGGVRGVGTGGIVSTAFCLLYKLFTLKLTRKQVMGLITHSDSPDIRALGFMYIRYTQPPPDLVDWYDEFLDDEEELDVKAGGGCVMTVGEMLRSFLTKLEWFSTLFPRIPVPVQKAIDQHMKSRPRKPPQKDEQEEEEEEATAAPAADTGRHGDKRRSRTPRRSPSPRKSQNRSRSRSHHRERHGASFDYELERERDRQRKEREGKDRDRDRDRDRERDRERDRDRRRSRTPDRNAERRRSRSRERRRSRSTSRDKRTERKDRDKDREAESERERSRKKDREHHKDRERSKDKRSKGEGEERRHKDDKEEKKHREEKRSKRSRSRSRDRKHKAERSSKKRSRSGSRSRQEAGEEKNRKRERSHSKDRQHKRSRSKERSHRRESSNERIHARQERPSSESGERTNSVRADSP
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May be required for pre-mRNA splicing. Belongs to the PRP38 family.
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Q36362
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MPQLLPTPWFTIFIYAWMVLLAVIPLKILSYVYPNHNYLRGLQKPSEHSWFWPWS
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Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family.
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A0RB27
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MQNKIQVKSVEKRENALIFCAENSEIEVKGLSARNHVLVDSDNLSFLYILENESSFIYVSIPHTCWEAMHEAMNNDVVMFVRVNDIEMELEGLKEEVEYLVENIEGNANYGEELVTAVEKVFL
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Belongs to the UPF0738 family.
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Q6KV95
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MGKRLLDKLWERHVVTTNENGLDLLYIDLHLVHEVTSPQAFEGLRLTNRTVRRPDLTFATMDHNIPTKDVWNITDRIAKQQLDTLRENCKQFQVPLADIGDEEQGIVHVIGPELGLTQPGKTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLWQRKPKAMGIELKGKLQKGVYAKDIILHLLSKYGVAVGTGYVMEFYGETIGTMEMEERMTLCNMAIEGGAKAGIIAPDEKTFAYVKGRKYAPRDYETFEKKWFELYTDADAIYDLHISIDVTDLAPYVTWGTNPSMGVRIDEKLPEKHDVNDERAFSYMGLIPGQSTYDIPVQHVFIGSCTNSRLSDLEIAASVVKGRKVKEGVRALVVPGSKRVRDAAMQKGLHHIFEEAGFEWREPGCSMCLGMNPDQVPEGEHCASTSNRNFEGRQGKGARTHLVSPAMAAAAALYGHFVDIRKESYDGAISYS
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Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate Binds 1 [4Fe-4S] cluster per subunit. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. Heterodimer of LeuC and LeuD. Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.
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Q84LA1
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MAQAWAFLLPVLVLGSYVTSLFFPSYISNPLCGGDGGRSLFLCAQAPKDQDPSPAVSTMYKTAFHFQPAKNWMNDPSGPMYFNGIYHEFYQYNLNGPIFGDIVWGHSVSTDLVNWIGLEPALVRDTPSDIDGCWTGSVTILPGGKPIIIYTGGDIDQHQAQNIAFPKNRSDPYLREWIKAPNNPVLRPDEPGMNSIEFRDPTTGWIGPDGLWRMAVGGELNGYSAALLYKSEDFLNWTKVDHPLYSHNGSNMWECPDFFAVLPGNNAGLDLSAAIPQGAKHALKMSVDSVDKYMIGVYDLQRDAFVPDNVVDDRRLWLRIDYGTFYASKSFFDSNKNRRIIWGWSRETDSPSDDLEKGWAGLHTIPRTIWLAGDGKQLLQWPVEEIESLRTNEISHQGIELNKGDLFEIKEVDAFQADVEIDFELASIDDADPFDPSWLLDPEKHCGEAGASVPGGIGPFGLVILASDNMDEHTEVYFRVYKSQEKYMVLMCSDLRRSSLRPDLEKPAYGGFFEFDLEKERKISLRTLIDRSAVESFGGGGRVCITSRVYPAVLADVGRAHIYAFNNGSATVRVPQLSAWTMRKAQVNVEKGWSAI
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Hydrolyzes inulin-type beta-(2,1)-fructans, but not beta-(2,1)-linkages in branched fructans. Has low activity against beta-(2,6)-linked fructans. May play a role as a beta-(2,1)-trimmer during graminan biosynthesis. Hydrolysis of terminal, non-reducing (2->1)-linked beta-D-fructofuranose residues in fructans. Inhibited by sucrose. Optimum pH is 4.5-5.5. Inactive above pH 7.5. Optimum temperature is 30-40 degrees Celsius. Belongs to the glycosyl hydrolase 32 family.
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A5J273
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MVKNSFSSVISQEEKKENGGSVEFQVVSFTNKIRRLTSHLELHKKDYLSQRGLRKILGKRQRLLSYLSKKNKMRYKELINQLDIRESKTQ
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Part of the 30S ribosomal subunit. Belongs to the universal ribosomal protein uS15 family.
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Q5ZW87
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MLTIKNWQLLSENDKKLCLSRPRQSSAIKENVLEIINQVQLSGDKALYDLTKQFDRVNLQYLQVPQEKIEQANIPKNALNAITQAIGTISSYHQSLLPENTEISTASGITIRNVYRPIQKVGLYVPGGNKTPLVSSLLMQAIPAKVAGCPIKVLCTPPDAEGEINEHILVAARLCGIDTIYAIGGAQAIAAMAYGTESVIKVDKIFGPGNSYVTQAKTLVAIDADGAAIDMPAGPSEVMILADTEANPEFIAADLLAQAEHGPDSQVILICDECELANQVNQQLEIQMSYLSRIEFIKRSLANSRIIICSNQSEQLDIINSYAPEHLIINRKNPEPWVEKIVAAGTVFLGSWAAETMGDYVTGSNHVLPTSGFARNHSGLSTLDFMTRFTVQAINQEAIRNLGPAAMTLAELEGLDAHANAVQIRLNTLGD
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Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH Binds 1 zinc ion per subunit. Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. Belongs to the histidinol dehydrogenase family.
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B4EX44
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MVLMIVSGRSGSGKSVALRALEDMGFYCVDNLPVDLLPELAKTLAERDAAAAAVSIDVRNMPESPEIFEKALESLPAEYSPQLLFLDADRNTLIRRYSDTRRLHPLSTKNLSLEMAIDTESDLLEPLRSRADLIIDTSEMSVHELAEMLRTRLLGKRERELTMVFESFGFKHGIPIDADYVFDVRFLPNPHWDPKLRPMTGLDRPVAAFLDRHTEVHNFIYQTRSYLELWLPMLETNNRSYLTVAIGCTGGKHRSVYVAEQLADYFRSRGKNVQSRHRTLEKRK
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Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6-phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis. Under low GlcN6P concentrations, RapZ is sequestered and inactivated by an other regulatory small RNA, GlmY, preventing GlmZ degradation and leading to synthesis of GlmS. Homotrimer. Belongs to the RapZ-like family. RapZ subfamily.
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A8MQX3
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MKSQTVLISIFIFSFFALHQCMQMDVGEIEGSNKISIGKCVPAQCSVSFFKRDCWCCFRDQSMCSKTQKECESNPRCPPLKF
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Maternally-contributed central cell peptide regulating suspensor development and correct auxin distribution in early developing embryos. Expressed exclusively in ovule embryo sacs and in early developing endosperms. Primarily expressed in the central cell gamete of nonfrtilized ovules, which upon fertilization gives rise to the endosperm, and later in the micropylar endosperm, which surrounds the embryo. No visible phenotype, due to redundancy with ESF1.1 and ESF1.3. Simultaneous down-regulation of all 3 genes by RNAi induces embryo abnormalities. Belongs to the MEG family.
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P89477
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MTSRPADQDSVRSSASVPLYPAASPVPAEAYYSESEDEAANDFLVRMGRQQSVLRRRRRRTRCVGLVIACLVVALLSGGFGALLVWLLR
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Essential for the anterograde spread of the infection throughout the host nervous system. Together with the gE/gI heterodimer, US9 is involved in the sorting and transport of viral structural components toward axon tips. During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN), maybe through an interaction with PACS-1 sorting protein. Phosphorylated on serines within the acidic cluster, possibly by host CK2. Phosphorylation determines whether endocytosed viral US9 traffics to the trans-Golgi network or recycles to the cell membrane. Belongs to the alphaherpesvirinae envelope protein US9 family.
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P22073
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MTIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHTPGKVFNGDNGNVACDSYHRYEEDIRLMKELGIRTYRFSVSWPRIFPNGDGEVNQEGLDYYHRVVDLLNDNGIEPFCTLYHWDLPQALQDAGGWGNRRTIQAFVQFAETMFREFHGKIQHWLTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAHGLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACARTISLHSDWFLQPIYQGSYPQFLVDWFAEQGATVPIQDGDMDIIGEPIDMIGINYYSMSVNRFNPEAGFLQSEEINMGLPVTDIGWPVESRGLYEVLHYLQKYGNIDIYITENGACINDEVVNGKVQDDRRISYMQQHLVQVHRTIHDGLHVKGYMAWSLLDNFEWAEGYNMRFGMIHVDFRTQVRTPKESYYWYRNVVSNNWLETRR
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BglA is intracellular and cleaves cellobiose probably through inorganic phosphate mediated hydrolysis. Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Homooctamer. Belongs to the glycosyl hydrolase 1 family.
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A4VNA4
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MIGRLRGTLAEKQPPHMILDVNGIGYEVEVPMTTLYRLPAVGEPVTLHTHLVVREDAQLLYGFAEKRERELFRELIRLNGVGPKLALALMSGLEVDELVRCVQAQDTSVLVRIPGVGKKTAERLLVELKDRFKAWESMPAIATLVVEPGSKTAVTSAENDAVSALISLGFKPQEASRAVSAIQEENLSSEEMIRRALKGMV
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The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. ATP + H2O = ADP + H(+) + phosphate Forms a complex with RuvB. Belongs to the RuvA family.
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Q8Y5X4
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MEQTYVMVKPDGVERGLIGEIVTRIEKKGLKIVAGKLMQIDRELAEKHYAEHIGKSFFEDLIGFITSGPVFAMVLEGDDAIATARRMMGKTNPLEADPGTIRADYAIHTNRNVIHGSDSPESAQREIQLFFAPDEILSYQKAVDTWI
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Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP Homotetramer. Belongs to the NDK family.
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A6UQJ4
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MARQKFSGKGGKGKSKKGQQSTAPRRRVEFKYKGFTLPELQEMPIKKFIEIVPARQRRTMSRGITPNQRKLVMKIKKARRLVNRGKEPRVIRTHCRDFVITPEMIGLTISIYTGKQFKEIKLVEETLGRFLGEMAPTRGIVQHGSPGMGATRGSMFVPIK
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Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. Belongs to the universal ribosomal protein uS19 family.
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C1B2S6
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MTSWPPRIVIRRSSGLRTMESALVRSGLGPVAGVDEAGRGACAGPLVVAACVLAPKPYPALARLDDSKKLTERTREELFPAITRLAVAWSVVSFPADEVDRMGVHVANIEGMRRAVAGLTTTPGYVLTDGFRVPGLPAPSLPVIGGDAAAACIAAASVLAKVSRDRVMVAMDETHPGYGFAIHKGYNTPAHLAALEVLGPCPEHRRSWSNVAALLHRVDNSSGSAR
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Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytic cleavage to 5'-phosphomonoester. Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. Belongs to the RNase HII family.
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Q92AD2
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MSNKVKSDIEIASVAEILPVTTIAEHLGLDADALELYGKYKAKLSYDTIHSLKDKEQGKLVLVTAINPTPAGEGKSTVTVGLGDALSKKDKKTVIALREPSLGPTMGIKGGATGGGYAQVIPMEDINLHFTGDFHAITAANNALSAFIDNHMQQGNDLGIDGRRIVWKRVVDLNDRALRKVVVGLGGPIQGVPREDGFDITVASEIMAIICLASDLKDLKKRLSEIVIGYNYKKEPITVGEMGYEGALTLLLKDALKPNLVQTLEHTPAIVHGGPFANIAHGCNSVSATSTALKLGEYVVTEAGFGADLGAEKFLDIKVPALGKAPDCVVIVATIRALKMHGGALKTELSEENVDALAKGFTNLQKHTESIQTFGIPYVVAINKFITDSDAEVAKLEQLCEEHGIPFSLTEVWEKGGDGGLELADKVIAAVESGEEDYKRIYDDAWSIEEKLEAIVTKVYGGIGVELSSKAQKQIVEFKKYGWDRYPICMAKTQYSLSDDPTLLGRPTDFVIHIREFIPKLGAGFVVALTGDVMTMPGLPKKPAALNMDVDENGNAQGLF
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(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate One-carbon metabolism; tetrahydrofolate interconversion. Belongs to the formate--tetrahydrofolate ligase family.
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C3M699
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MFQDNPRLAQLKQKIQETLPKKEGTIKASDKGFGFLEVDSKTSYFVPPPYMKKCMHGDKVVAFIRTENEREVAEPSELIEQSLTRFIGRVKLFKGKLNVAPDHPQLKKLSLKAKTKKGLNEADFQEGDWVVAHLVRHPLKGDDGFFVQISHKITDANDKIAPWWVTLAENDLPNSEPAGIDDWQLKDDADLVREDLTALPFVTIDGESTKDMDDALYAQQLPNGDFALTIAIADPTAYITPEDEMDKVARERGFTIYLPGRNIPMLPRDLADELCSLMENQVRPALCCSVTIRKDGVIGDDIRFFAANIKSHARLVYDHVSDWLETGSSEQWQPSEEIAQVVRDLYAFSQARANWCETHAVVFPDRPDYRFELSADNDVVAIHADMRRTANRLVEESMITANICAGKTLQTTFGFGVFNTHAGFKAEKMADVVELMAVNGAPNADAETLATVEGFAALRRWLATQETSYLDNRIRKYQSYSEIGNQPLPHFAMGLDVYATWTSPIRKYGDMINHRLLKAHILGKAPVQTPDETVGEELALHRKHHKIAERNVADWLYARTLADEPAKETRFQAEIFDINRPGMRVRLLENGAMAFIPGALILDNKERIECNGEDGTILIDKEVVYKLGDVLEIVLTEVNQENRSLVGKPTQVFADLVSETQTSTEQPAEGAENNEPQA
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Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction. Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. Belongs to the RNR ribonuclease family. RNase II subfamily.
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Q7MK60
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MSKHFFLHNEFHWQGRHDAEDGAAGSRVHHVVQQIDYTHIGENPYGVALLGFACDAGVARNKGRIGAKKSPDLIRRALANLAWHSPHPLYDLGTVVCDDDLLESSQQHCAKIIAEVLPCVPVITLGGGHEVAWASFSGLARYFEQHHPEKAPKIGIINFDAHFDLRAFSSSQADVKPSSGTPFNQIQHYCQQQGWDFHYACLGVSKASNTRALFERAEQLNVWFVEDKDLGSVNHDYHLTQLQHFIDDCDYLYLTIDLDVFPAATAPGVSAPAARGVSYDNLAPFLDRILAHRDKLMLADIAEYNPTYDVDSQTARLAARLCWDIANAMNDKLEHQ
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Catalyzes the conversion of N-formimidoyl-L-glutamate to L-glutamate and formamide. H2O + N-formimidoyl-L-glutamate = formamide + L-glutamate Binds 2 manganese ions per subunit. Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (hydrolase route): step 1/1. Belongs to the arginase family.
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E9LVH9
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MANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF
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Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.1). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.1, PubMed:23592055). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.1, PubMed:23592055). Capable of degrading the bioplastic poly(lactic acid) (PLLA) (PubMed:28671263). a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+) an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+) (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+) cutin + H2O = cutin monomers. kcat is 2.4 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 17 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 5.3 sec(-1) with pNP-butanoate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 16 sec(-1) with pNP-butanoate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). Shows promising applications in ethyl alcohol distillery processes as it may be utilized for treatment of molasses wastewater (PubMed:33387709). Has potential for application in biological recycling of plastic waste products (PubMed:23592055, Ref.1, PubMed:28671263). Belongs to the AB hydrolase superfamily.
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Q0SHX9
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MTAANVPGSSIGVDALPIRENLRGKSAYGAPQLTVPVQLNTNENPHPPTKALVDDVAESVREAARELHRYPDRDAVALRTDLAAYLVRQTGVPVTVDNVWAANGSNEILQQLLQAFGGPGRSAMGFVPSYSMHPIIADGTETEWLPIFRRADFALDVDAATAAITERRPDVVFVTSPNNPTGHSVGIAELRRVLDAAPGIVIVDEAYAEFSDAPSALTLIDEYPSKLVVSRTMSKAFAFAGGRLGYLAAAPAFIEALLLVRLPYHLSVVTQAAARAALRHANETLASVHALATERVRVSKALDDTGFRVIPSDANFILFGEFTDSAHAWRAYLDRGVLIRDVGIPGYLRATVGLASENDAFIVASDEIAATELTSSGDRG
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2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. Homodimer. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
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B7ZWG3
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MGQELCAKRLQPGCSCYHRSEGGEAHSCQRSQPGSTEPAVFELTEASSSTASFHPRGLEAASAQKLKSKRPRSNSDSFQEENLRQGLPWKKSLPFGAASSYLNLEKLGEGSYAKVYKGISRINGQLVALKVISMNAEEGVPFTAIREASLLKGLKHANIVLLHDIVHTKETLTFVFEYMHTDLAQYMSQHPGGLHPHNVRLFMFQLLRGLAYIHHQRVLHRDLKPQNLLLSHLGELKLADFGLARAKSIPSQTYSSEVVTLWYRPPDALLGATEYSSELDIWGAGCIFIEMFQGQPLFPGVSNILEQLEKIWEVLGVPTEDTWPGVSKLPNYNPEWFPPPKPQSLQIVWDRLGGVPEAEDLASQMLKGFPRDRVSAQEALVHDYFSVLPSQLYQLPDEESLFAVSGVKLKPEMCDLSASYRKRHHLVGVNKCW
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Serine/threonine-protein kinase that acts like an antiapoptotic protein that counters TRAIL/TNFSF10-induced apoptosis by inducing phosphorylation of BIRC5 at 'Thr-34'. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
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Q0AMW4
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MLYLLFAPLADDFQLANLFRYITFRTGGALMTAMLIAFVFGKPMIGWLRRKQGKGQPIRAEGIERHVVEKAGTPTMGGFLILLGVMVGTLLWADLTNAYVWIVIFVTAGFGVIGFIDDYLKVTKQTTAGFGGRFKLVGEFAIALIAVVWATHTARSLGVEPGIETSIAVPFFKDLMINIGPLFFVFGCVVIVGSGNAVNMTDGLDGLAIVPVMIAAATFGVIAYVVGRVDFAEYLQVHYTAGAGEILIFCGALIGAGIGFLWWNAPPAMVFMGDTGSLSLGGALGTIAVAIKHELVLAIVGGLFVLELVSVMVQVASFKLFGKRVFRMAPIHHHFEKKGWAEPTIVIRFWIIAVILALIGLATLKLR
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Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the glycosyltransferase 4 family. MraY subfamily.
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Q8PNR7
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MDIEQLREKSADELKAHLTDLRKEQFSLRMQQVTGQLPKTHETRRVRREIARVKHLLGSTK
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Belongs to the universal ribosomal protein uL29 family.
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Q1KKV1
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MSCPNNSGNFLMDPLMGGSSSFRDEGYSSNSGMYIHTAAECGYSVMKVEPSPLSKSRDVPAGSVLLSSFQDAPYLSAQPSTWTPGTKSSRDQQLVAQCLQPCSFPAGNVKEEAFCCFYQDGSKRKQTTESATYIRLRDNRCGPEQTTTQARGCFQMYNREEPQQDDQLFAPACSLLHLGTSVESQSKISCSKFATETGKDERKEEKARSDGCSETSDNEELKGRNLQSQRTLFLCLNVSAILLRNSRVLVFGNSHDASSEKTTGNWLKAKSGRKKRCPYTKHQTLELEKEFLFNMYLSRERRLEISRSINLTDRQVKIWFQNRRMKLKKLNRESREREQGVVYNYC
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Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Belongs to the Abd-B homeobox family.
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Q3V089
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MQATAALETDSDKNYPKNGGHFQNDKLYNPKKENMFFSNGCNGVILAFPDGKEDSLATEERASDKENSIVDQRDLSELSFSENQDSNRGNIFSQSSEFEDSNDYAFLNETYSIHYSESKLKDENLLHLYSGLHPEVHKRVEMIFDTLDNNSIGLGRSAEASGADCGDVQKSDVDEDSQQEYHSAELECISAHLAKTVSRSSLDVSELKTSSYDFKCGGNFEDNHGKLESGPSPSLESLNGFAQECSLQVSTSQSSDMLQEYHEPKYEKCKEQEVDLTYHKAFDGILQRSSSPLNHQKVPETQVYTKEVKSQTTESKDFYGNRIFQNKALQRPENATMFPQDRALETHLKANDAHQPSGPCALDDSVISLCGSSQYKSLPEPGFFSPVIPRVAVTDYQAEVEGSCLHHVQGSATNKACSLMKEVCLTSVPDAAACIAAVQQTLHVSSRVNASSSIVSASSITETKMVRQSQAEEWQSDKRSVACNTAWSCGQQCRDAQRAAPGSDSGRPLSTGCLKPSGNSLNENSLELRKVFDTTDRQKHCNRAFQLCEEKAVPSRCCQKTTERAIKAEMHLLDVCYQMCHRHCHHIYKLVMESRAGLNRNLQTDSAKKELGAALLSVLEDLKLRYMNLKGKVHKGIPLEELPPLSVESKLLSAFSDFVSRLMKDEACSLSGANSELDNQSLPDVDVSPGLLKTLSQMSFIPDSSQPEQGKSPMSDVCKNGDTDIGFNCLKLNDKECKTVQEASEDWFDATERLIGADFSETQDSTAECEEWQPRNPLELKNSELHGKGQGFLIHVGGLCPSVSEADLRSHFQKYQVSEISIYDSTNYRYASLAFAKNSNAKMAVKEMNGVKINGKSVTVRLVKIPGEYTPPPLSTTGNSTSMNHLEKNTNKDATSASSICRLPRAKSRQLESEQDSEFPPLDQGVKKNCNQMKSGQLLPETPFQFIPPNTLNLRSFTKIMKRLAELHPDISRDHIIEALQEVRINHKGFLNGLSINTIVKMASSFLRNSALK
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Component of intercellular bridges during meiosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells. Not required for fertility. Homodimer. Interacts with TEX14. Detected in the intercellular bridges. Localization to intercellular bridges is identified in all stages of tubules but dynamically increases from stage I pachytene spermatocytes to stage XII secondary spermatocytes and disappears after the formation of step 1 round spermatids (stage I). In addition, it is localized in the cytoplasm in pachytene spermatocytes to secondary spermatocytes. The cytoplasmic signals also increases dramatically in stages X-XII, decreases from step 1 to step 3 spermatids, and disappears in step 4 spermatids. Highly expressed in testis. Also expressed in other tissues at lower level. Present in testes beginning at postnatal day 5 (at protein level). No visible phenotype. Null male mice produce an increased number of sperm and show enhanced fertility.
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Q7UP21
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MKALNANISTMSEVSRSATPQSDSPAQAEVTPEVCIRIANFNAWYGSFQAIHNLSLDVPRNQVTAFIGPSGCGKSTLLRWINRMNDIVPSANSRGTLMIDELDVLAQTTDVVNLRRRVGMVFQKPNPFPKSIYDNVAFGPKLHLYLSRAELDELVEWSLRKAAVWDEVKDRLHAPALGLSGGQQQRLCIARAIAVGPEVLLMDEPCSALDPASTLAIEDLIYELREQYTIVMVTHNMQQASRCSDRTAFFFEGKLVESGPTQDVFTKPQEKRTDDYVRGRFG
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Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in) The complex is composed of two ATP-binding proteins (PstB), two transmembrane proteins (PstC and PstA) and a solute-binding protein (PstS). Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family.
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A1K7J8
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MSDVKKVVLAYSGGLDTSVILKWLQDTYQCEVVTFTADLGQGEELEPARQKALKFGIKPENIFIDDLREEFVRDFVFPMFRANTIYEGEYLLGTSIARPLIAKRQIEIARATGADAVSHGATGKGNDQVRFELGYYALMPGVKVIAPWREWDLLSREKLLAYAEKHGIPIEMKHKQGGSPYSMDANLLHISFEGRHLENPAAEAEESMWRWTVSPEAAPDAAEYVDLEFEKGDLVAINGQRLKAHELLAKLNELGGKHGIGRLDLVENRYVGMKSRGCYETPGGTILLRAHRAIESITLDREVAHLKDDLMPRYASMIYNGYWWSPERQALQALVDHTQQTVNGWVRIKLYKGNVIVVARDSKTDSLFDPTIATFEDDQGAYNQKDAHGFIRLNALRMRIAANAKTKRG
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ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Homotetramer. Belongs to the argininosuccinate synthase family. Type 1 subfamily.
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A1S7C2
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MARKVFYISDGTAITAEVFGHAVLSQFPMEFEAITIPFVETNAKAEAVKKQINDSFITTGERPLVFHSIVKPEIRDVIYSSEGLDYDFLNTFVAPLEQQLGVSAAPVLHRTHGKANHSYEARIDAINFAMENDDGQTLKHMDKADIILLGVSRCGKTPSSLYLSMQFGIKAANYPFTEDDMDSLKLPEALKRNKHKLFGLTIDPVRLQEIRQSRMENSRYSSLRQCRMEVKEVEMMFKKERIPYIDTTNHSVEEIATKILDMTGMERHMF
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Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation. [pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-phosphate + AMP + H(+) [pyruvate, water dikinase]-phosphate + H(+) + phosphate = [pyruvate, water dikinase] + diphosphate Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PSRP subfamily.
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Q31NU0
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MDGLKRYLSSAPILATIWFAITAGILIEFNRFFPDLLFHPL
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May help in the organization of the PsaE and PsaF subunits. Belongs to the PsaJ family.
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A0LDB0
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MAKIKRALISVSDKTGLVPFCQGLAEHGVSFLSTGGTARLLRESGLDVMDVSEFTGFPEMLDGRVKTLHPKVHGGLLGLRDNASHQQQMGEHGIEPIDMVVVNLYPFEATVAKEGCTLEEAIENIDIGGPSMLRSAAKNYRSVTVVTDPADYARVLESLRAHDGQCDAGLNAQLARKVYARTAAYDAAISNWLSALDNEGRPGAFPETYTVQFKKVQGMRYGENPHQSAAFYAESPPSEEASLATATQLQGKELSFNNIHDANGALELVKEFSKPAAVVVKHANPCGVAVHDGDLLAAYRMARDTDPVSAFGGIIALNRCVDVAVAKEIAQLFVEVIIAPEYDEQALELFATKKNLRLLRVPNIGVATAVSTMDLKRVTGGLLLQDRDLKQLPEGSLKVVTERAPSEAEMRDLLFAWKVVKHVKSNAIVYAKEQRTLGVGAGQMSRVDASRIAVWKAQDTAHTAGLRENPLLGAAMASDAFFPFRDGVDAAAKAGAKAVIQPGGSVRDEEVIAAANEHGMAMVFTGMRHFKH
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(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1. The IMP cyclohydrolase activity resides in the N-terminal region. Belongs to the PurH family.
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O26901
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MKSLPPEMRQILGDCYPHIRELNPAQRSAIEAGYLESEDNYIIAIPTASGKTLLGIIAALKTVMEGGRVIYTVPLLSIQNEKIKEFRKLEEHGIRVGKDPRTSDIAVMVFESFDSLTRFSWNILREVDLLIVDEFHMIGEYTRGPVIESAITRARTLNPSVRIVALSATLSNMDEIAGWLDARVVEHDYRPVPLHREVLDTEMFGVREKNDVVLKVLERSLEDGSQTLAFVSTRRFTESLASHLADKISGKIPDDMVESFREVAGKVLEVPKSRGSPPTSTCLKLAECLEAGIAFHHAGLFNRQREIIEDEFRDGNILMITATPSLMYGVNLPSRTVVIRDYTRWTSQGPRRIPVFDYEQMSGRAGRPQYDDAGYSYLIARSHDEAMDLEEYYIRGEVERTTSRIIENRDALYRQIIAQVASGLSGTTEELADFFRNTFYGYQMVEGPFSDSFGMDSIQYEVENATEYLMRNRILYPGPEGFSATEFGLLIAKSNYSVETAIKLHQFASEMDEMDIYRLIYEITRTPDMPLISFKGRKSRDPVRDKLMEHGLFLMDVGNEEATAAALIEWINERTEYEIENAFHVYAASTRRSAYEASKIVKFFGKICEIMGVYRHSSQLEILSARLYYGVKEDAIPLVVGVRGLGRVRARKIIKTFGEDLRHVREDELKRIDGIGPKMAGAIRRYCERF
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DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Helicase with 3'-to 5'- polarity; able to unwind over 100 bp of DNA at 50 degrees Celsius. Unwinds forked DNA, preferentially on lagging strand forks; has weaker activity on Holliday junctions. Displaces the invading strand in DNA D-loops. Unwinds short oligonucleotides from dsDNA with 3'- but not blunt ends or 5'-ssDNA tails in an ATP-dependent manner. ATPase activity is stimulated by ssDNA but not dsDNA, protein binds ssDNA, dsDNA with 5'- or 3'-overhangs but not blunt ended dsDNA and replication forks. Replication forks bind both this protein and RPA. RPA does not stimulate the helicase activity of this protein. ATP + H2O = ADP + H(+) + phosphate Monomer (By similarity). Binds replication protein A (RPA), in presence and absence of DNA. The C-terminal region (about 633-690) acts as a brake for ATP hydrolysis (PubMed:17991488) and interacts with RPA (PubMed:21195035). Belongs to the helicase family. Hel308 subfamily.
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Q7U8U2
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MDQSSGKGSGRDVGVAPVVLTILDGWGHRNDSEHNAIRQGDTPVMEALWHAYPHALIQASGSHVGLPDHQMGNSEVGHLTIGAGRIIRQELVRISDTVRDDQLNNTPALVELAEHLQNDTGTLHLLGLCSDGGVHSHVNHLCGLIHWAAAAGIKKVAVHAITDGRDTPTQSAMGSITLVQRAMEEAGVGHLASLCGRYWAMDRDKRWDRTEKAYDLYTDPTRSISDQSPQQLLAESYAAGITDEFLKPVRLSDDVMQDGDSVLVFNFRPDRARQIVQTLCLDDFDGFERRTTPKLDVVTFTQVEQDLPVSVAFPPEPLDDLLGQVVAEAGLRQYRTAETEKYPHVTYFMNGGIEQPLPGEERHLVPSPRVATYDLSPAMSADQLTDSCIDAIDQGTYSLIVINYANPDMVGHTGVMDAATEAIATVDRCIGRLLDAVGRRGGTMLITADHGNAELMQGPDGQAWTAHTTNPVPCILVEGEQRKLPGHGNDISLREDGGLADIAPTLLQILNLEQPAAMTGRSLIEPVSNVDPSPLSARLPLPV
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Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Binds 2 manganese ions per subunit. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Monomer. Belongs to the BPG-independent phosphoglycerate mutase family.
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Q8NAU9
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MGSGRVPGLCLLVLLVHARAAQYSKAAQDVDECVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHCKDVDECEREDNAGCVHDCVNIPGNYRCTCYDGFHLAHDGHNCLDVDECAEGNGGCQQSCVNMMGSYECHCREGFFLSDNQHTCIQRPEEGMNCMNKNHGCAHICRETPKGGIACECRPGFELTKNQRDCKLTCNYGNGGCQHTCDDTEQGPRCGCHIKFVLHTDGKTCIETCAVNNGGCDSKCHDAATGVHCTCPVGFMLQPDRKTCKDIDECRLNNGGCDHICRNTVGSFECSCKKGYKLLINERNCQDIDECSFDRTCDHICVNTPGSFQCLCHRGYLLYGITHCGDVDECSINRGGCRFGCINTPGSYQCTCPAGQGRLHWNGKDCTEPLKCQGSPGASKAMLSCNRSGKKDTCALTCPSRARFLPESENGFTVSCGTPSPRAAPARAGHNGNSTNSNHCHEAAVLSIKQRASFKIKDAKCRLHLRNKGKTEEAGRITGPGGAPCSECQVTFIHLKCDSSRKGKGRRARTPPGKEVTRLTLELEAEVRAEETTASCGLPCLRQRMERRLKGSLKMLRKSINQDRFLLRLAGLDYELAHKPGLVAGERAEPMESCRPGQHRAGTKCVSCPQGTYYHGQTEQCVPCPAGTFQEREGQLSCDLCPGSDAHGPLGATNVTTCAGQCPPGQHSVDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAISFQDCDTKVQCSPGHYYNTSIHRCIRCAMGSYQPDFRQNFCSRCPGNTSTDFDGSTSVAQCKNRQCGGELGEFTGYIESPNYPGNYPAGVECIWNINPPPKRKILIVVPEIFLPSEDECGDVLVMRKNSSPSSITTYETCQTYERPIAFTARSRKLWINFKTSEANSARGFQIPYVTYDEDYEQLVEDIVRDGRLYASENHQEILKDKKLIKAFFEVLAHPQNYFKYTEKHKEMLPKSFIKLLRSKVSSFLRPYK
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Is a positive regulator of the BMP signaling pathway, required for proper chondrogenesis, osteogenesis and skeletal development. It acts as coreceptor for BMP ligands, particularly BMP2 and BMP4, facilitating their interactions with BMP type I receptors (PubMed:33308444). It is required for ligand-induced recruitment of BMP receptors to lipid rafts (By similarity). Binds to TGFBR2 and activates TGFB signaling. In lung cancer cells, could serve as an endogenous autocrine and paracrine ligand of TGFBR2, which could regulate TGFBR2 signaling and hence modulate epithelial-mesenchymal transition and cancer progression. Forms homooligomers (PubMed:33308444). Forms heterooligomers with SCUBE1 and SCUBE2 (PubMed:33308444). Interacts with TGFBR2 through the CUB domain; this interaction does not affect TGFB1-binding to TGFBR2. Interacts with BMP2, BMP4 and BMP7; the interaction is mediated by the CUB domain (PubMed:33308444). Interacts with BMPR1A, BMPR1B and BMPR2; the interaction with BMPR1A and BMPR1B is BMP2- and BMP4-dependent (PubMed:33308444). Highly expressed in osteoblasts. In normal lung, mainly expressed in bronchial epithelial cells. Tends to be up-regulated in lung cancer cells. N-glycosylated. Proteolytic cleavage produces a CUB-containing C-terminal fragment that retains the ability to bind to TGFBR2. This reaction is catalyzed in vitro by MMP2 and, to a lesser extent, by MMP9. The disease is caused by variants affecting the gene represented in this entry. Truncated N-terminus.
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A9M2P1
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MYTGRFAPSPTGLLHIGSLLTAAASYADARSNGGKWLVRMEDLDPPREMPGAASHILHTLEAFGFEWDGEVAYQSRRYALYEETLCRLKTAGLVYPCHCSRKDWQAAARRGADGFVYNGRCRHPGQRPAPQGKQPAWRIRVPDRDIGFSDGIVGGYAQNLARDIGDFVLLRADGYWAYQLAVVADDAEQGVTHIVRGQDLLVSTPRQIYLQQCLGVPTPQYAHLPLLTNAQGQKWSKQTLAPALDLNRREQLLRQVFRYLNLPEAPETDRPAELLDWAVAHWDMDKVPKHAVTPP
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Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon. Binds 1 zinc ion per subunit. Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.
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A9ESS9
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MPKMKTNRAAAKRFKVTGSGRIRRSKGGLNHCMQEKSKKRLRRLRKNDMVDSAMEKRVKLLLPYG
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Belongs to the bacterial ribosomal protein bL35 family.
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Q9ESR9
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MGFLHQLQLLLWKNVTLKRRSPWVLAFEIFIPLVLFFILLGLRQKKPTISVKEAFYTAAPLTSAGILPVMQSLCPDGQRDEFGFLQYANSTVTQLLERLNRVVEESNLFDPERPSLGSELEALHQRLEALSSGPGTWESHSARPAVSSFSLDSVARDKRELWRFLMQNLSLPNSTAQALLAARVDPSEVYRLLFGPLPDLDGKLGFLRKQEPWSHLGSNPLFQMEELLLAPALLEQLTCAPGSGELGRILTMPEGHQVDLQGYRDAVCSGQATARAQHFSDLATELRNQLDIAKIAQQLGFNVPNGSDPQPQAPSPQSLQALLGDLLDVQKVLQDVDVLSALALLLPQGACAGRAPAPQAGSPSGPANSTGVGANTGPNTTVEEGTQSPVTPASPDTLQGQCSAFVQLWAGLQPILCGNNRTIEPEALRRGNMSSLGFTSKEQRNLGLLVHLMTSNPKILYAPAGSEADHVILKANETFAFVGNVTHYAQVWLNISAEIRSFLEQGRLQQHLHWLQQYVADLRLHPEAMNLSLDELPPALRLDYFSLPNGTALLQQLDTIDNAACGWIQFMSKVSVDIFKGFPDEESIVNYTLNQAYQDNVTVFASVIFQTRKDGSLPPHVHYKIRQNSSFTEKTNEIRRAYWRPGPNTGGRFYFLYGFVWIQDMIERAIINTFVGHDVVEPGNYVQMFPYPCYTRDDFLFVIEHMMPLCMVISWVYSVAMTIQHIVAEKEHRLKEVMKTMGLNNAVHWVAWFITGFVQLSISVTALTAILKYGQVLMHSHVLIIWLFLAVYAVATIMFCFLVSVLYSKAKLASACGGIIYFLSYVPYMYVAIREEVAHDKITAFEKCIASLMSTTAFGLGSKYFALYEVAGVGIQWHTFSQSPVEGDDFNLLLAVTMLMVDTVVYGVLTWYIEAVHPGMYGLPRPWYFPLQKSYWLGSGRTETWEWSWPWAHAPRLSVMEEDQACAMESRHFEETRGMEEEPTHLPLVVCVDKLTKVYKNDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDQLTVEEHLWFYSRLKSMAQEEIRKEMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGAYGDGYRLTLVKRPAEPGTSQEPGMASSPSGRPQLSNCSEMQVSQFIRKHVASSLLVSDTSTELSYILPSEAVKKGAFERLFQQLEHSLDALHLSSFGLMDTTLEEVFLKVSEEDQSLENSEADVKESRKDALPGAEGLTAVESQAGNLARCSELAQSQASLQSASSVGSARGDEGAGYTDGYGDYRPLFDNLQDPDSVSLQEAEMEALARVGQGSRKLEGWWLKMRQFHGLLVKRFHCARRNSKALCSQILLPAFFVCVAMTVALSVPEIGDLPPLVLSPSQYHNYTQPRGNFIPYANEERREYRLRLSPDASPQQLVSTFRLPSGVGATCVLKSPANGSLGPMLNLSSGESRLLAARFFDSMCLESFTQGLPLSNFVPPPPSPAPSDSPLSPDEDSLLAWNTSLPPTAGPETWTWAPSLPRLVHEPVRCTCSAQGTGFSCPSSVGGHPPQMRVVTGDILTDITGHNVSEYLLFTSDRFRLHRYGAITFGNIQKSIPAPIGTRTPLMVRKIAVRRVAQVLYNNKGYHSMPTYLNSLNNAILRANLPKSKGNPAAYGITVTNHPMNKTSASLSLDYLLQGTDVVIAIFIIVAMSFVPASFVVFLVAEKSTKAKHLQFVSGCNPVIYWLANYVWDMLNYLVPATCCIIILFVFDLPAYTSPTNFPAVLSLFLLYGWSITPIMYPASFWFEVPSSAYVFLIVINLFIGITATVATFLLQLFEHDKDLKVVNSYLKSCFLIFPNYNLGHGLMEIAYNEYINEYYAKIGQFDKMKSPFEWDIVTRGLVAMTVEGFVGFFLTIMCQYNFLRQPQRLPVSTKPVEDDVDVASERQRVLRGDADNDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKDLLQVQQSLGYCPQFDALFDELTAREHLQLYTRLRGIPWKDEAQVVRWALEKLELTKCADKPAGSYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAVCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQNVKDVVRFFNRNFPEAMLKERHHTKVQYQLKSEHISLAQVFSKMEHVVGVLGIEDYSVSQTTLDNVFVNFAKKQSDNVEQQEAEPSTLPSPLGLLSLLRPRPAPTELRALVADEPEDLDTEDEGLISFEEERAQLSFNTDTLC
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Probable transporter, its natural substrate has not been found yet. May have a role in macrophage lipid metabolism and neural development. May play a role in myelination, perhaps as a transporter for certain kinds of myelin chemical components (PubMed:12210128). May play an important role in gamma-secretase processing of APP and thus in amyloid-beta peptide generation (PubMed:22086926). Regulates esterification of plasma membrane cholesterol by modulation of sphingolipid metabolism (PubMed:24201375). Probable lipid transporter that modulates cholesterol sequestration in the late endosome/lysosome by regulating the intracellular sphingolipid metabolism, in turn participates in cholesterol homeostasis (PubMed:24201375). May alter the transbilayer distribution of ceramide in the intraluminal membrane lipid bilayer, favoring its retention in the outer leaflet that results in increased acid ceramidase activity in the late endosome/lysosome, facilitating ceramide deacylation to sphingosine leading to the sequestration of free cholesterol in lysosomes (By similarity). In addition regulates amyloid-beta production either by activating a signaling pathway that regulates amyloid precursor protein transcription through the modulation of sphingolipid metabolism or through its role in gamma-secretase processing of APP (PubMed:22086926). May play a role in myelin formation (PubMed:12210128). Forms discrete, punctate intracellular vesicles. Expressed at high levels in brain, at moderate levels in heart, kidney and lung, and at low levels in skeletal muscle, stomach, spleen, colon and pancreas (PubMed:10970803). Not detected in the liver or small intestine (PubMed:10970803). In brain, highly expressed in white matter and detected in oligodendrocytes (PubMed:10970803, PubMed:11157071). Expressed in cerebellum as well as the anterior commissure (PubMed:11157071). Expressed mainly in the white matter but is also scattered in gray matter throughout the whole brain (PubMed:11157071). Expressed in myelinating cells of both ventral and dorsal restricted regions in newborn spinal cord (PubMed:12210128). Expressed in non-myelin-forming as well as in myelin-forming Schwann cells in the sciatic nerve (PubMed:17240058). N-glycosylated. Methylated at Gln-271 by N6AMT1. Belongs to the ABC transporter superfamily. ABCA family.
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A9WP53
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MRTKIELGKLGENLAADFLERRGFRIVDTNWRCPSGEIDLVAFDGEFLVIAEVKARRSLRYGHPFEAITDAKLRRLRTLAVLWARHHGFFSSPIRIDAVAVLIPQGEEPRLEHLRGLG
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Belongs to the UPF0102 family.
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A0A1Y0AWT3
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MNATDAESRKPENKPSSESSSSGSTSGSSDGEVSSKTYFKNNKSKVLSGQREVVLEVVRDLSYTICKEAEEKLVERFPRKDGSNEMLPKEDSINTNHNYTTDSDEHPVELTTKTEECKNTEKTKKKSFVRALSKDKQLSAYRSRSRSTRLSYSGHISRTHSVEKSLSRYKKSVLRNRRTSFGHGRDSSTTKRSVSRDKDNRLRRRIGSSRSHTRSHSRFRRSEKKLPSRSPRRIRSQERRHERRRSMSSDYERIALRRSEPIKRRDKDEFFKNNKKVSGDIKKGKGNDNGTVAELEAKITERQRKSLDILTSRTGGACLTPDKLRMIQAEITDKSSAAYQSIAREALKKYIHGYINKVNVDSVAVITRKLLKDNIVRGRGVLCHSIIQAQATSPKFTHVYAAMVAIINSKFPNIGELLLKRLVIQFKRAFGCNDKTVCLTSSHFIAHLVNQRVAHEILALEILTLLIESPTDDNVEVAITFLKECGMKLTEVSSDRVGGIFELLKNILHQGKLDKRVQYMIKVLFQVRRDGFKDHQSIIESLELVEEYAQFTHLLLLEDVTYPKDILNEFKFDDQYETNEEKYKALSKNILGSHASDSDGSFGSGSNSETALSDCDKGKNEVNDKYTSGDIIDETKPNLIALRRTIYLTLNSCLDYEECAQKLMKMQLKTCQQNEFCQILLDCCAEQRTYEKFYGLLTHRICKMNKSFIEPFKEIFKDICQTTHCLDTNRLRNISKFFAHLLFTDAISWDVLDCIKLTEDEAITSRCIFIKSFFQELVEYMGLYHFNKKLKTEVLAGTLAGLFPKDNPRNIRFSINFFTSIGLGGITNELCQLLKIAPKSAPSSSSSSSLSSELSAPSDDDSSSDSENKKKHKGKNKKMTKKKNPSKKKEETKKIVGKNKIAAKNKTIKRRTDKDNSSSKDNFLKSESSSNESISLDSLSSELFAPSSYSSSESSNDSESKEKHKGKNKKMTKKKNPSNKREKTKKKLSKNKKAPNKNTKKRMTEKDISSSESSISESKSLNCSASNQNENEKRKKRVTSKSRTKRVKMFKQCQWVDADNQRDIKRKKRAEYRYEPLVYRKRNEEYLKKGGPNCRKDNYGNRQNHEISQRHDSEIKRRREERKKRHHEKNHSREYKRSKLGPCQREYFLYMCCQFYYPCTFQCLCQNCHFTFYS
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Male determiner protein (M-factor) that controls male somatic sexual differentiation. Acts as a dominant factor that regulates the mRNA splicing of transformer (tra) and doublesex (dsx) transcripts and promotes expression of male splice forms of tra and dsx (By similarity). Probably acts as a component of the spliceosome C complex required for mRNA splicing factor and exon-junction complex (EJC) assembly (By similarity). Hinders eIF4AIII from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs (By similarity). Component of the spliceosome C complex. Specifically expressed in early male embryos. Zygotic expression first appears in 2- to 3-hour-old embryos (cellularized blastoderm stage). Expression is then maintained throughout male development until adulthood. The M.domestica genome only codes for one male determiner Mdmd protein, which is encoded in the M region, and can be located at different loci on the genome (chromosomes II, III, V or Y). The M region contains a cluster of tandemly repeated Mdmd copies with only one intact copy: other copies are degenerate with large truncations and frameshifts and are assumed to be non-functional. The presence of multiple copies in the M region may preserve its integrity in a hostile non-recombining environment. This protein is encoded on chromosome Y. Belongs to the CWC22 family.
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A4XP32
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MSTSSSPYAAFAALLSSAGHSVSPAELHGLLLGRSCAGAGFDADAWLLDAADLLGGEPQDSVRQALIGLQEMVKGELCSEDMAVVLLLPDDETPLAQRAVALGQWCQGFLGGFGLTARDGALSAEAMEVLQDLSAIAQVQSALEESEDGENDYMEVMEYLRVAPLLLFTECAKPAAPAAKPSLH
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Belongs to the UPF0149 family.
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Q711P4
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MKLCVTVLSLLVLVAAFCSPALSAPMGSDPPTSCCFTYTVRKLPRNFVTDYYETSSLCSQPAVVFQTKKGRQVCANPSDDWVQEYMDDLELN
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Monokine with inflammatory and chemokinetic properties. Homodimer. Interacts with CCR5 (By similarity). Belongs to the intercrine beta (chemokine CC) family.
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P31372
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GALDGSWKEATLPQVKAMLQKDTGKASGDTVTYSGKTVHVVAAAVLPGFPFPSFEVHDKKNPTLDIPAGATVDVTFINTNKGFGHSFDITKKGPPFAVMPNIKPIVAGTGFSPVPKDGKFGYSEFTWHPTAGTYYYVCQIPGHAATGMFGKIIVK
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Electron carrier from cytochrome c552 to the A-type oxidase. Binds 1 copper ion per subunit. E(0) is +680 mV. Monomer. The two different versions of rusticyanins are most probably due to strain variations.
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Q6LIL7
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MQLTTQALMVQGTTSDAGKSVLVTGLCRVLVRKGIKVAPFKSQNMALNSAVTKDGGEIGRAQAVQAQAACIEPTVHMNPVLLKPNTDVGAQIIVQGKAIADMDAIGYNGYKKVVMGPIMESFGILQDEYQTVIIEGAGSPAEINLRENDVANMGFAEKADVPVIIIADIDRGGVFAHLYGTLALLSESEQARVIGFVINRFRGDIKLLESGLDWLEEKTGKPVLGVLPYLHGLMLEAEDAINVQQVEAADEQLNVVVPVLTRVSNHTDFDPLRMHPQVNLQFVGKGQPIPPTDLIIIPGTKSVRSDLAFLREQGWDKQIERHLRLGGKVMGICGGYQMLGESIADPDGIEGDAGESQGLGYLQTSTILAPEKQLKQTVGTLQLPEQPAVPVRGYEIHAGITSGIQTNAPVQLQDGPDGQLGIDNQVFGTYLHGIFEQTEACNAILSWAGLEATQTPDFDLIREQGIDRVADTLEEYMKLDKLWPEWADKFAK
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Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Cofactor biosynthesis; adenosylcobalamin biosynthesis. Belongs to the CobB/CobQ family. CobQ subfamily.
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O20215
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RFKKIRRLGALPGLTSKRPRSGSDLKNQLRSGKRSQYRIRLEEKQKLRFHYGLTERQLLKYVHIAGKAKGSTGQILLQLLEMRLDNILFRLGMASTIPGARQLVNHRHILVNGRIVDIPSYRCKPRDIITTNNKQRSKALIQNFIASSPRQEELPNHLTIDPFQYKGLVNQIIDSKWIGLKIN
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One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. With S5 and S12 plays an important role in translational accuracy. Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity (By similarity). Belongs to the universal ribosomal protein uS4 family.
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A0A0E4BZH1
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METAGLSFSRYFVVMNLLQMTIPSSEQFTVNSLERPVLAALGGNVELSCQLSPPQSAEHMEIRWFRSHYTRPVYLYKEGKDLYGETISKYVERTKLLKEAIGEGKVTLRILNVSADDDGQYHCFFKDGDVYEEAIAEVKVTATSLEIQILIHPPNTKGLLVECNSEGWFPQPQMEWRDSRGGIIPPSSKSHSQNGNKLFNMKMSLLLRDSSHGNITCYLRNPITGQEERTSIVLSDKLFSWDSVWILILVAILAVLLFFIMMPSVELQQREQRRCCDWNSPCLIGIGIVFSSMCVIIGLTITLHHRNRVPVSDRKFQLVSMYLEDMTVMVWVLMVFITMLISLVYFRLRGFFQI
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May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. Expressed in the thymus and skin. All hominoid species have a common inactivating mutation, but that Old World monkeys such as olive baboons, green monkeys, cynomolgus macaques and rhesus macaques have apparently functional SKINT1L sequences, indicating that SKINT1L is inactivated in a common ancestor of hominoids. Belongs to the SKINT family.
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P62667
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MARRRRAEVRQLQPDLVYGDVLVTAFINKIMRDGKKNLAARIFYDACKIIQEKTGQEPLKVFKQAVENVKPRMEVRSRRVGGANYQVPMEVSPRRQQSLALRWLVQAANQRPERRAAVRIAHELMDAAEGKGGAVKKKEDVERMAEANRAYAHYRW
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One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA (By similarity). Part of the 30S ribosomal subunit. Contacts proteins S9 and S11 (By similarity). Belongs to the universal ribosomal protein uS7 family.
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Q83982
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MNPNQKIICISATGMTLSVVSLLVGIANLGLNIGLHYKVGDTPNVNIPNVNGTNSTTTIINNNTQNNFTNITNIIQSKGGERTFLNLTKPLCEVNSWHILSKDNAIRIGEDAHILVTREPYLSCDPQGCRMFALSQGTTLRGRHANGTIHDRSPFRALISWEMGQAPSPYNTRVECIGWSSTSCHDGMSRMSICMSGPNNNASAVVWYGGRPITEIPSWAGNILRTQESECVCHKGVCPVVMTDGPANNRAATKIIYFKEGKIQKIEELAGNAQHIEECSCYGAGGVIKCICRDNWKGANRPVITIDPEMMTHTSKYLCSKVLTDTSRPNDPTNGNCDAPITGGSPDPGVKGFAFLDGENSWLGRTISKDSRSGYEMLKVPNAETDIQSGPISNQVIVNNQNWSGYSGAFIDYWANKECFNPCFYVELIRGRPKESSVLWTSNSIVALCGSKKRLGSWSWHDGAEIIYFE
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Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. Binds 1 Ca(2+) ion per subunit. Inhibited by the neuraminidase inhibitors zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere with the release of progeny virus from infected cells and are effective against all influenza strains. Resistance to neuraminidase inhibitors is quite rare. Homotetramer. Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. Intact N-terminus is essential for virion morphogenesis. Possesses two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain. The transmembrane domain also plays a role in lipid raft association. N-glycosylated. The influenza A genome consist of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains. Belongs to the glycosyl hydrolase 34 family.
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Q8R1B6
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MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEDDDDDEDDVVDLAANSLLNKLIRQSLIESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYELALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTEVTKQIIIGTPGTVLDWCFKRKLIDLTKIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNVIKLRKEELTLNNIRQYYVLCENRKGKYQALCNIYGGITIGQAIIFCQTRRNAKWLTVEMMQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVNQSEEPDYETYLHRIGRTGRFGKKGLAFNMIEVDKLPLLMKIQDHFNSNIKQLDPEDMDEIEKIEY
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ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development. ATP + H2O = ADP + H(+) + phosphate Detected in both cytoplasm and nucleus of testicular cells. Also detected in chromatoid bodies of round spermatids. Isoform 1 is expressed in germ cells. Isoform 2 is expressed in Leydig cells and in round spermatids of adult testis upon gonadotropin stimulation. Phosphorylated on threonine residues. The phosphorylated form is found in the cytoplasm but not in the nucleus. Male mice display normal sexual behavior but are sterile with testes that are 25% smaller than the wild-type. Round spermatids arrest at step 8 and fail to elongate. Chromatoid bodies are unusually condensed, greatly reduced in size and lack the typical amorphous texture throughout all steps of spermiogenesis. Belongs to the DEAD box helicase family.
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A2VD12
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MASCPDSDNSWVLAGSETLPVETLGPESRVDPESEEAPQALQDSSKADGKESAGTLNGEEMLFQTESSQGEGAALPEESEAKGALGGDDGHGTKRPGDTAVQEDLQETPMVTSLGPDTQDLERNIHPQNLPSSPRAVWKEHGCSSSDDDTDVDVEGLRRRRGREPSPPQPTAAVDGEDQAKGEGIGELGISLNMCFLGALVLLGLGILLFSGALLEPETEPVEEAELQVFPETELVQTVGNRQDEVEQLQASVPPDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRGVDGVCLNWGGSPQGGKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQWQLLGSVHRNLQRGLQDAGQGAPAHAGLAELGHMLAQTLQGLESQGINTGRSSNDSEAWHQKKPRFQHPREWSGREKWRGGQRDQKAEHWKLKKEESGQDRKKSWRDEGREFTGHWKENRPRAEESGSRKDSKRQDPKVHPRKSGNSHSGERQKHSWGKDNSPDSVSWEELLRRKYRPPQGCSGVADCARQEGLALFGVELAPVRQQELASVLREYLARLPWAGQLTKELPLSPAYFGEDGIFRHDRLRFRDFVDALEDSLEEVALKQTGDDDEVDDFEDFIFSHFFGDKALKRRSKKKEKQPWNHRAVGPREEHSRHPHHYHQG
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Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling (By similarity). Interacts with ESR1, PBX1, PBX2 and PBX3. Interacts with TEX11 (By similarity). Shuttles between the nucleus and the cytosol. Mainly localized in the cytoplasm, associated with microtubules. Detected in small amounts in the nucleus. The C-terminal domain (AA 443-731) contains a nuclear export signal. Association to the cytoskeleton through a N-terminal leucine rich-domain (between AA 190-218).
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A8A1Z0
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MRIAKIGVIALFLFMALGGIGGVMLAGYTFILRAG
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Belongs to the UPF0387 family.
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B0TAK8
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MTSQFASLWQQSLEILKQELKPASFDTWLKNTQLVTIQNGEAHIGVPNDLARDWLENRYATLVKNALSVVLGESVEVRFFTPSADSRRSEPSRRPVATEESSPPLLNPKYTFDTFVVGNSNRFAHAAALAVAEAPAKAYNPLFVYGGVGLGKTHLMQAIGHFVIEQHPQSRVVYVSSEKFTNELINAIRDDKTVEFRNRYRNIDVLLIDDIQFLAGKERTQEEFFHTFNALHESSKQIIISSDRPPKEIPTLEDRLRSRFEWGLITDINPPDLETRIAILRKKAILENLDVPNEVMVFIANIIQSNIRELEGALNRVIAYANLSGKSLTSEVAEEALKNIIPSHRAKVITIALIQEIVAEHYNMRVEDFKAKKRTRDVAFPRQIAMYLSREMLDVSLPKIGEEFGGRDHTTVIHAHEKITKDIEKDPQLEMTIQVLKEKIQRA
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Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family.
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Q5E8V2
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MGGISIWQLLIIAVIIVLLFGTKKLRGVGSDLGSAVKGFKKAISEDEPAKEAKKDADFVPQNLEKKEAETVEKQKQNDKEQA
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Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. The Tat system comprises two distinct complexes: a TatABC complex, containing multiple copies of TatA, TatB and TatC subunits, and a separate TatA complex, containing only TatA subunits. Substrates initially bind to the TatABC complex, which probably triggers association of the separate TatA complex to form the active translocon. Belongs to the TatA/E family.
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C1DLQ2
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MSKGHSLQDPYLNTLRKERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVRLPTASEGEQPEPGNA
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RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Homohexamer. Belongs to the Hfq family.
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Q9Y2F8
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MLRPQGLLWLPLLFTSVCVMLNSNVLLWITALAIKFTLIDSQAQYPVVNTNYGKIQGLRTPLPSEILGPVEQYLGVPYASPPTGERRFQPPESPSSWTGIRNATQFSAVCPQHLDERFLLHDMLPIWFTTSLDTLMTYVQDQNEDCLYLNIYVPMEDDIHEQNSKKPVMVYIHGGSYMEGTGNMIDGSILASYGNVIVITINYRLGILGFLSTGDQAAKGNYGLLDQIQALRWIEENVGAFGGDPKRVTIFGSGAGASCVSLLTLSHYSEGLFQKAIIQSGTALSSWAVNYQPAKYTRILADKVGCNMLDTTDMVECLKNKNYKELIQQTITPATYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVDGIVDNEDGVTPNDFDFSVSNFVDNLYGYPEGKDTLRETIKFMYTDWADKENPETRRKTLVALFTDHQWVAPAVATADLHAQYGSPTYFYAFYHHCQSEMKPSWADSAHGDEVPYVFGIPMIGPTELFSCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWSKYNPKDQLYLHIGLKPRVRDHYRATKVAFWLELVPHLHNLNEIFQYVSTTTKVPPPDMTSFPYGTRRSPAKIWPTTKRPAITPANNPKHSKDPHKTGPEDTTVLIETKRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHETHRHPSPQRNTTNDITHIQNEEIMSLQMKQLEHDHECESLQAHDTLRLTCPPDYTLTLRRSPDDIPFMTPNTITMIPNTLMGMQPLHTFKTFSGGQNSTNLPHGHSTTRV
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Putative neuronal cell surface protein involved in cell-cell-interactions. Homodimer. Interacts with NRXN1 in a calcium-dependent manner. Interacts through its C-terminus with DLG4/PSD-95 third PDZ domain (By similarity). Expressed in fetal and adult brain, prostate and testis. Belongs to the type-B carboxylesterase/lipase family.
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Q44015
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MPRFAANLSMMYNEHAFLDRFAAAAADGFRAVEFLFPYEHAAAELRARLDANGLTQALFNAAPGDWAAGERGLAALPGREADFRGTIGRALEYAGVIGNDRIHVMAGLIPADADRARCRATYLENLAFAANAAAAQGVTVLIEPINTRDMPGYFLNRQDDGQAICKEVGAANLKVQFDCYHCQIVEGDVAMKLKRDIAGIGHIQIAGVPERHEPDVGELNYPYLFEVMDTLGYDGWIGCEYRPRAGTSAGLGWLKPYLGR
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Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). 3-hydroxypyruvate = 2-hydroxy-3-oxopropanoate Belongs to the hyi family.
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Q1BH71
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MSHDSDDKTFPYQKDDAELRRRLTPMQYEVTQHAATERAFTGEYTDTEDAGIYKCVVCSTPLFESGAKFHSGCGWPSYFKPLNGEVIDEKVDYSHGMVRVEVRCNNCGAHLGHVFEDGPRDKTGLRYCINSAALNFESRPENE
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[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein] Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein. Belongs to the MsrB Met sulfoxide reductase family.
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P30163
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MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITVGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGSTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
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Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family.
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Q3Z611
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MVKVYAPASSANMSVGFDVLGAAVTPVDGALLGDVVTVEAAETFSLNNLGRFADKLPSEPRENIVYQCWERFCLELGKQIPVAMTLEKNMPIGSGLGSSACSVVAALMAMNEHCGKPLNDTRLLALMGELEGRISGSIHYDNVAPCFLGGMQLMIEENDIISQQVPGFDEWLWVLAYPGIKVSTAEARAILPAQYRRQDCIAHGRHLAGFIHACYSRQPELAAKLMKDVIAEPYRERLLPGFRQARQAVAEIGAVASGISGSGPTLFALCDKPDTAQRVADWLGKNYLQNQEGFVHICRLDTAGARVLEN
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Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5. Belongs to the GHMP kinase family. Homoserine kinase subfamily.
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Q3IR98
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MRDIFERRDGDAAGRIGELSVPRAGTTVETPALLPVVNPHIRTIAPAELESTFGAQILITNGYILYGSDEYRERALADGLHDLFDFSGAIMTDSGSFQLSEYGEISVTNEEILRFQRDIGSDIGTPVDIPTPPEASREQTAADLETTKARLEAAETVDTGEMLVNAPVQGGTYPDLREEAAEHAYGTTLDVFPVGAVVPLMNSYRYGDMIEAILGAKRGLGADAPVHLFGAGHPMMFALAVAAGCDLFDSAAYALYARDDRYLTVAGTDHLDDLEYLPCSCPVCADHTPAELQAEDDTERERLLARHNLHVSFQELRTIKQAIKKGNLLELVERRARGHPAMVDGYRALLEAADQLERDDPVSKGSFFYLSGESARRPEVKRHHDRLSRLSVDGDRVLLSEGGDNSRFDETWRLQPPFGPFPPALSDSYPLTAELPERLDDRAYEAAAKGVRRLVDDHPETEFAVAHWGWPDAALDSLPDGVELLRLGADSDHPERDSAQSDMDGDEPKEDYPPGEDENA
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Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. 7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine Binds 1 zinc ion per subunit. tRNA modification; archaeosine-tRNA biosynthesis. Belongs to the archaeosine tRNA-ribosyltransferase family.
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Q44315
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MRTPVSTYRLQIRKGFTLFDAAKTVPYLHSLGVDWVYLSPVLTAEQGSDHGYDVTDPSAVDPERGGPEGLAAVSKAARAAGMGVLIDIVPNHVGVATPAQNPWWWSLLKEGRQSRYAEAFDVDWDLAGGRIRLPVLGSDDDLDQLEIRDGELRYYDHRFPLAEGTYAEGDAPRDVHARQHYELIGWRRADNELNYRRFFAVNTLAGVRVEIPAVFDEAHQEVVRWFREDLADGLRIDHPDGLADPEGYLKRLREVTGGAYLLIEKILEPGEQLPASFECEGTTGYDALADVDRVLVDPRGQEPLDRLDASLRGGEPADYQDMIRGTKRRITDGILHSEILRLARLVPGDANVSIDAGADALAEIIAAFPVYRTYLPEGAEVLKEACELAARRRPELDQAIQALQPLLLDTDLELARRFQQTSGMVMAKGVEDTAFFRYNRLGTLTEVGADPTEFAVEPDEFHARLARRQAELPLSMTTLSTHDTKRSEDTRARISVISEVAGDWEKALNRLRDLAPLPDGPLSALLWQAIAGAWPASRERLQYYALKAAREAGNSTNWTDPAPAFEEKLKAAVDAVFDNPAVQAEVEALVELLEPYGASNSLAAKLVQLTMPGVPDVYQGTEFWDRSLTDPDNRRPFSFDDRRAALEQLDAGDLPASFTDERTKLLVTSRALRLRRDRPELFTGYRPVLASGPAAGHLLAFDRGTAAAPGALTLATRLPYGLEQSGGWRDTAVELNTAMKDELTGAGFGPGAVKIADIFRSFPVALLVPQTGGES
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Catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation. 4-[(1->4)-alpha-D-glucosyl](n-1)-D-glucose = 1-[(1->4)-alpha-D-glucosyl](n-1)-alpha-D-glucose Monomer. Belongs to the glycosyl hydrolase 13 family.
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A5EVF4
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MSKSQSLQDPYLNALRKERVPVSIYLVNGIKLQGQIESFDAFVILLRNNISQMVYKHAVSTIVPSRNIHLSREEMGLEDEAGEEISAEYTPNAEGQAEATADPLYD
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RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Homohexamer. Belongs to the Hfq family.
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B5EKH1
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MRWAVLGGGHWGTALAVYLLRQRHMVQLWGRRAERLPCQPGRTDLFPVFPECARPEGLHCTVDLAAAVQGGEGIVLAVPSHALRGLLTHLLPCLPSTALFVLASKGLEVPSALRLDQVLREILPEAPLVVLSGPSFAHDLMLGKPLAMTAASTDPTYAQRVAEAFGSAQMRVYTSDDVAGVCLGGAIKNVLAIAAGISDGLGNGDSARAALITRGMAELHRLGTALGGRTETFMGLAGAGDLILTSCSDLSRNRRVGLGLGSGLSLEAVLRGIGEEAEGVRTAQALFQLAQSLGVDMPITEQVYRVLFEGAAPRAASDELMRRALRSELHVSDDGTPGGAARTE
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NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADPH Membrane lipid metabolism; glycerophospholipid metabolism. Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
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Q6DJD8
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MSWRPQYRCSKFRNVYGKVASRENCYDCIPITKNVHDNHFCAVNPKFLAIVTESAGGGSFFVIPLHQTGRIEPNYPKVCGHQGTVLDIKWNPFIENIIASCSEDTSVRIWEIPDGGLKRNMTEAVLELYGHSRRVGLIEWHPTAINILFSAGYDYKILIWNLDVGEAVKMIDCHTDVILCMSFNTDGSLMATTCKDKKLRVLEPRSGRVLQETTCKNHKVTRVVFFGDMKRLLTTGVSKWNTRQIALWDQEDLSMPVTEEEIDGLSGLLFPFYDVDTHMLYLAGKGDGNIRYYEITAEKPYLTYLMEFRSPAPQKGLGVMPKHGLDVSACEIFRFYKLVTLKNQIEPISMIVPRRSENYQEDIYPMTSGTEPALSPDEWLRGVNKGPVLMSLKEGYRKENKAIYKAPVKEKKSLVVNGIDLLENVPPRTENELLRMFFKQQEEIRRLKEQLSQRDLLVRQLELELKNLRNSPKDS
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May play a role in the reorganization of neuronal actin structure. Belongs to the WD repeat coronin family.
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Q5PM85
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MKSLQALFGGTFDPVHYGHLKPVETLANLIGLSRVIIMPNNVPPHRPQPEASSAQRKYMLELAIADKPLFTLDERELQRNAPSYTAQTLKAWREEQGPEAPLAFIIGQDSLLNFPTWHDYDTILDNTHLIVCRRPGYPLEMTQAQHQQWLEQHLTHTPDDLHQLPAGKIYLAETPWLNISATLIRERLEKGESCDDLLPENVLNYINQQGLYR
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Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. Belongs to the NadD family.
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Q0SRW4
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MEILKSMIDPKIVMAIVISFIVASILGPIIIPLLHKLKFGQNIRQEGPKSHLKKAGTPTIGGLIFIFATIITMFVMVGNPTDEAMIALYSFVGFGFVGFLDDLLKIIKKKNEGLTSGQKMILLLIISGFLTWYAYKYIGTSINIPFLNGQINLGLFYIPAAMFYFAGVTNAVNLTDGLDGLATSVTVLVTTFLGIISYNLGHISLAIFCVALAGALLAFLRFNAFPARVFMGDTGSLALGGAVAMVALILKMPLILVLIGIIYVIETLSVILQVASFKLTGKRIFKMAPIHHHFEQLGWSETKIVSVFSIITVVFCFIAFASL
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Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the glycosyltransferase 4 family. MraY subfamily.
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A7TRW3
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MSDFWDKNKGSIASGFKSAGKYTYQGAKYVGKSGYNASKNHYNKSKEQRDKRDKKKGKKKNGDDEYSGDDSYSDDDSSYSTASIPVSSMKDPNSFPPPPLKPQQVQATSSSHSVEQYPASAGVPQQQLRQLPPQPISATQQPAWPQQPAANQYDGQVSAPDQSQMQYGGQTQYQQPPAMQQPPAMQQHPAMQQPPDMQQPPDMQQPPAMQQPPAMQQPPAMQQPPAMQQPPAMQQPPAMQQPPAMQQPPNMVGQPSNQFQLPEPQQRQTPPLPPVTSQPYGEAQNQAQNQGQFQATPLSQLQNMQQEETTRSVPNAYDPQQTYSQPPSIPQRHTPQPVVNQVQYQESQSSIPQVNQDYYGQQPEVNQQNNLMNRSIPPPMQQQPPMQQQPPMQQQPPMQQQPPMQQQPPMPPRGPSLAAPAYGGTPNINANAQLPASSGITVKPYNPDEVQTREPLALKVDIGNLPPPPTHRDRGTETRPPSEPKPSPAIRNPISAVPAVSRASTLDSSSVPVNSIPAHQNQPIYMQDNSSSVESFPDEETSDFNNLPPPPPPNRRVTEQNLEKSAKSSTIGQEQRNDSKTEPPRAAIVGSFNSNPTINFEPPPKPFRPVVNSDRKSESPVQPQPLARSANGPPALPSRRGTQTSFESHPTPPSMESSTPSLPNRLNRNEPPIAEKPVSSFPPPPKPFRRVEAESPSHSQVNDSNKESSAPRTHNFGNDEDEDISAPVKWNPPAELLERKSEIDVKKGKKAPPPVVKPKPKNLSSVNKVNPEYEGHKPVGSMNQNQNQNQNQNSLNSITDELTHVHLRKTGISLEDEGKKFGGNDTSIDDIPPKFEKIETSRKPKAPPAVPKKKDSIRGAPPPVPAKKKNLNATPQPPPSRRNNNVNNDNDDDDSNPFEKYMRDAVPAEENRLRK
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Localizes within detergent-insoluble glycolipid-enriched membranes. Belongs to the AIM3 family.
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Q0SAG9
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MLPEPHRLRRHSDFSMTVRRGRRMGRRDLVVHAFDRAQADELVSSGGPRFGLVVSKAVGPAVIRHRVARRLRHICIDLVDVVPRGTDVVIRALPGAATASSRDLEKQLRAGLLRLDLLAPVSTSA
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RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit. Belongs to the RnpA family.
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A5PJA8
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MAATLWAFFSVLLLLLSRDAQSSEVSGSTSDGSGGSGVGTGDRFKIEGRAVVPGVKPQDWISAARVLVDGEEHVGFLKTDGSFVVHDIPSGSYVVEVISPAYRFDPVRVDITSKGKMRARYVNYIKTSEVVRLPYPLQMKSSGPPSYFIKRESWGWTDFLMNPMVMMMVLPLLIFVLLPKVVNTSDPDMRREMEQSMNMLNSNHELPDVSEFMTRLFSSKSSDKSSSGSSKTGKSGAGKRR
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Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. Component of the ER membrane protein complex (EMC). Belongs to the EMC7 family.
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Q6ZNU5
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MSDEGSRGSRLPLALPPASQGCSSGGGGGGSSAGGSGNSRPPRNLQGLLQMAITAGSEEPDPPPEPMSEERRQWLQEAMSAAFRGQREEVEQMKSCLRVLSQPMPPTAGEAEQAADQQEREGALELLADLCENMDNAADFCQLSGMHLLVGRYLEAGAAGLRWRAAQLIGTCSQNVAAIQEQVLGLGALRKLLRLLDRDACDTVRVKALFAISCLVREQEAGLLQFLRLDGFSVLMRAMQQQVQKLKVKSAFLLQNLLVGHPEHKGTLCSMGMVQQLVALVRTEHSPFHEHVLGALCSLVTDFPQGVRECREPELGLEELLRHRCQLLQQHEEYQEELEFCEKLLQTCFSSPADDSMDR
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Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR. Interacts with the ATP-binding domain of HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with PGLYRP1; this interaction blocks the cytotoxic activity of the PGLYRP1-HSPA1A complex (PubMed:21247889). Ubiquitous.
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P76015
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MKKLINDVQDVLDEQLAGLAKAHPSLTLHQDPVYVTRADAPVAGKVALLSGGGSGHEPMHCGYIGQGMLSGACPGEIFTSPTPDKIFECAMQVDGGEGVLLIIKNYTGDILNFETATELLHDSGVKVTTVVIDDDVAVKDSLYTAGRRGVANTVLIEKLVGAAAERGDSLDACAELGRKLNNQGHSIGIALGACTVPAAGKPSFTLADNEMEFGVGIHGEPGIDRRPFSSLDQTVDEMFDTLLVNGSYHRTLRFWDYQQGSWQEEQQTKQPLQSGDRVIALVNNLGATPLSELYGVYNRLTTRCQQAGLTIERNLIGAYCTSLDMTGFSITLLKVDDETLALWDAPVHTPALNWGK
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Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP (PubMed:15476397, PubMed:11350937). Binds covalently dihydroxyacetone in hemiaminal linkage (PubMed:15476397). DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR (PubMed:24440518). In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity (PubMed:24440518). In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR (PubMed:24440518). dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate Inhibited by chloro-3-hydroxyacetone and D,L-glyceraldehyde. kcat is 2.8 sec(-1) with dihydroxyacetone as substrate. Values measured with the DhaKLM complex (PubMed:11350937). kcat is 290 min(-1) with dihydroxyacetone as substrate. kcat is 12.5 min(-1) with D,L-glyceraldehyde as substrate (PubMed:15476397). Polyol metabolism; glycerol degradation. Homodimer (PubMed:12813127, PubMed:15476397, PubMed:24440518). The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL (PubMed:12813127, PubMed:15476397). DhaL also forms a complex with DhaR (PubMed:24440518). Activated by DhaR. Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKML has no transport activity.
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Q3SFR3
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MAKGGREKIKLESTAGTGHFYTTTKNKKTMPEKMEISKFDPKARKHVMYKETKLK
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Belongs to the bacterial ribosomal protein bL33 family.
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P47778
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MVPKLFTSQICLLLLLGLMGVEGSLHARPPQFTRAQWFAIQHISLNPPRCTIAMRVINNYRWRCKNQNTFLRTTFANVVNVCGNQSIRCLHNRTLNNCHRSRFRVPLLHCDLINPGAQNISNCRYADRPGRRFYVVACDNRDPQDSPRYPVVPVHLDTTI
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Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity (By similarity). Interacts with bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA). In vitro interacts with phospholipid bilayers. Located in the matrix of eosinophil large specific granule, which are released following activation by an immune stimulus. Belongs to the pancreatic ribonuclease family.
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Q6HMS8
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MLVISANEQRNLVNMNEVIAYAALALKEFSAERTITPIRGSLPFANEKNTALIMPSVAEGLEALGLKVVTVVPENKKIGKKTINGIVMLSDFQTGEPLALLEGSYLTMIRTGALSGVATKHLARHNAKTLCIIGTGEQAKGIAEAVFAVRDIEKVILYNRTEEKAYAFSQYIQEKFGKPAYVHTNANEAISEADIIVTTTNASTPVFSEKLQKGVHVNAVGSFKPSMQELPSHAIVGANKVVVESKEAALDETGDLQVPIKEGLFKANAIHAELGQIISGEKAGRENDEEITVFKSVGLAVVDIIVAKYLYEKAVESGVGNKIEF
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Catalyzes the reduction of Delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, using preferentially NADPH over NADH as the electron donor. Is likely involved in a degradation pathway that converts trans-3-hydroxy-L-proline (t3LHyp) to L-proline. L-proline + NAD(+) = 1-pyrroline-2-carboxylate + H(+) + NADH L-proline + NADP(+) = 1-pyrroline-2-carboxylate + H(+) + NADPH kcat is 11 sec(-1) for Pyr2C reduction using NADPH. kcat is 2.1 sec(-1) for Pyr2C reduction using NADH. Belongs to the ornithine cyclodeaminase/mu-crystallin family.
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Q8N853
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MPSQSACPVLSTAPGTPCDLRKHLLNMVSEEKRSPQLSAKTWRRGLRLQKRRNALFLPEGDICVVGSTSGARALIPETSKLERSGTVIAYCNLELLASSDPPVWASQSTGMTGMSYRSQPQLGFKSTPPAHSSVFHHSVKAPKEDQAQEAASRPLTSQDGWNPNIKK
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Product of a dubious CDS prediction. May be a non-coding RNA. No experimental confirmation available.
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B7L763
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MKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLDDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ
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This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. dUTP + H2O = diphosphate + dUMP + H(+) Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. Homotrimer. Belongs to the dUTPase family.
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B7LN63
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MSIYTRPVMLLLSGLLLLTLAIAVLNTLVPLWLAHEHLPTWQVGMVSSSYFTGNLVGTLLTGYLIKRLGFNRSYYLASLVFAAGCLGLGLMIGFWSWMAWRFVAGVGCAMIWVVVESALMCSGTSRNRGRLLAAYMMIYYVGTFLGQLLVSKVSTELMNVLPWVTALILAGILPLLFTRILSQQTESRKTTSITSMLKLRQARLGVNGCIISGIVLGSLYGLMPLYLNHQGISNSNIGFWMAVLVSAGIVGQWPIGRLADKFGRLLVLRVQIFVVILGSIAMLTHTAMAPALFILGAAGFTLYPVAMAWSCEKVSQDQLVAMNQALLLSYTIGSLLGPSFTAMLMQHYSDNLLFIMIASVSFIYLLMLLRNARHTSNPVAHV
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Belongs to the major facilitator superfamily. YcaD (TC 2.A.1.26) family.
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