ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P81528 | VAVKATTTEEETEIPAK | Function: Hydrolyzes the cell walls of mycobacteria. May play an important role in cell wall growth and cell separation.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 1817
Sequence Length: 17
EC: 3.2.1.-
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P06653 | MEINVSKLRTDLPQVGVQPYRQVHAHSTGNPHSTVQNEADYHWRKDPELGFFSHIVGNGCIMQVGPVDNGAWDVGGGWNAETYAAVELIESHSTKEEFMTDYRLYIELLRNLADEAGLPKTLDTGSLAGIKTHEYCTNNQPNNHSDHVDPYPYLAKWGISREQFKHDIENGLTIETGWQKNDTGYWYVHSDGSYPKDKFEKINGTWYYFDSSGYMLADRWRKHTDGNWYWFDNSGEMATGWKKIADKWYYFNEEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADKPEFTVEPDGLITVK | Function: Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Autolysin strictly depends on the presence of choline-containing cell walls for activity.
Catalytic Activity: Hydrolyzes... |
P36548 | MSTFKPLKTLTSRRQVLKAGLAALTLSGMSQAIAKDELLKTSNGHSKPKAKKSGGKRVVVLDPGHGGIDTGAIGRNGSKEKHVVLAIAKNVRSILRNHGIDARLTRSGDTFIPLYDRVEIAHKHGADLFMSIHADGFTNPKAAGASVFALSNRGASSAMAKYLSERENRADEVAGKKATDKDHLLQQVLFDLVQTDTIKNSLTLGSHILKKIKPVHKLHSRNTEQAAFVVLKSPSVPSVLVETSFITNPEEERLLGTAAFRQKIATAIAEGVISYFHWFDNQKAHSKKR | Function: Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors.
PTM: Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Can also be exported by the Sec system.
Cata... |
P57638 | MSKKITILIDAGHGGYDPGAIGIRGLKEKNINIEIALKLEKLLNHDKMFCTILTRHNDSYLSLKKRKQLLKKNQVNFLISIHADSSRKQNVSGASIWIVSKTRINREINNYLKNKSTLLFSKKIENIFKQNKNDFFLKKTILDLQSNNFQKIELDLSKEILKQLEKNTKLNKKYPNYASLGILSSINTPSILIETGFITNILEGKKLKTTNYQNKIANSIYLGLKNYFTKSSYILKK | Function: Cell-wall hydrolase involved in septum cleavage during cell division.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 27240
Sequence Length: 237
Subcellular Location: Secreted
EC: 3.5.1.28
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Q8K908 | MIDPGHGGQDPGAINSLGLQEKKITLKIGIKLKNLLQNSDLFYPVLTRNDDSYVSLKKRRDFLKNNHVSFLISIHADSSKKRYVSGASIWITTNDRMHREINNFIKNREENIYFPKNIQNLIQKNKHDFFLKKTVLDLQFNNFQKMEINLSRYIFQQLKKIIKLDKINLNYASLGILSSINTPSMLIETGFITNFLEEKKLRTNKYQNKIANAIYIALKNYFQDRLLSNLRNT | Function: Cell-wall hydrolase involved in septum cleavage during cell division.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 27259
Sequence Length: 233
Subcellular Location: Secreted
EC: 3.5.1.28
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Q89A33 | MIIAIDAGHGGQDPGAIGKNKFQEKNITLSIAKKLTKLLNHTNFFKAVMIRRGNYFLSVFKRTQIAEKYHANLLISIHANSSKNRKISGVSIWVLPKNVHNTRIQKHKLNKKTKNIHKKINTKTSKFKNFYEIEYDLAKIIIQELRKVSTLNQKKPKYAKFGILKFSQFPSILVETGFISNPIEEQHLNKKFYQNLISKSISIALKKYFLKRIKQYN | Function: Cell-wall hydrolase involved in septum cleavage during cell division.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 25202
Sequence Length: 217
Subcellular Location: Secreted
EC: 3.5.1.28
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P26365 | MMYRIRNWLVATLLLLCTPVGAATLSDIQVSNGNQQARITLSFIGDPDYAFSHQSKRTVALDIKQTGVIQGLPLLFSGNNLVKAIRSGTPKDAQTLRLVVDLTENGKTEAVKRQNGSNYTVVFTINADVPPPPPPPPVVAKRVETPAVVAPRVSEPARNPFKTESNRTTGVISSNTVTRPAARATANTGDKIIIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLLNDDPMFKGVLTRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMASWLEQHEKQSELLGGAGDVLANSQ... | Function: Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 4... |
P44493 | MKTKILFFLFFSTFSFSIFAAPITIAIDPGHGGKDPGAISRNLGIYEKNVTLSIAKELKALLDKDPHFRGVLTRKSDYYISVPERSEIARKFKANYLISIHADSSKSPDRRGASVWVLSNRRANDEMGQWLEDDEKRSELLGGAGKVLSHNNDKYLDQTVLDLQFGHSQRTGYVLGEHILHHFAKVTTLSRSTPQHASLGVLRSPDIPSVLVETGFLSNSEEEKKLNSQTYRRRIAYMIYEGLVAFHSGKTNTLVKDNLVQNIKQNDIKKSGKNNRTSEQNINEDNIKDSGIRHIVKKGESLGSLSNKYHVKVSDIIKLN... | Function: Cell-wall hydrolase involved in septum cleavage during cell division.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 49109
Sequence Length: 432
Domain: LysM domains are thought to be involved in peptid... |
P26366 | MIYRIKNAVIAALILLCAQAGAASLSDIQVSNGEQQARITLSFIGEPEYAYSQDGKRTVALDIRQTGVIQGLPLQFSGNNLVKTIRAGTPKDAQSLRLLVDLTENGKTEAVKRQNGGNYTVIFTINADVPPPPPPVVAKRVESAPRPTEPARNPFKSSDDRLTGVTSSNTVTRPAARASAGAGDKVVIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLLNNDPMFKGVLTRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNRDATGASVWVLSNRRANSEMANWLEQHEKQSELLGGAGDVLANSQSDPYLS... | Function: Cell-wall hydrolase involved in septum cleavage during cell division.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 46790
Sequence Length: 439
Subcellular Location: Periplasm
EC: 3.5.1.28
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P63884 | MSGSNTAISRRRLLQGAGAMWLLSVSQVSLAAVSQVVAVRVWPASSYTRVTVESNRQLKYKQFALSNPERVVVDIEDVNLNSVLKGMAAQIRADDPFIKSARVGQFDPQTVRMVFELKQNVKPQLFALAPVAGFKERLVMDLYPANAQDMQDPLLALLEDYNKGDLEKQVPPAQSGPQPGKAGRDRPIVIMLDPGHGGEDSGAVGKYKTREKDVVLQIARRLRSLIEKEGNMKVYMTRNEDIFIPLQVRVAKAQKQRADLFVSIHADAFTSRQPSGSSVFALSTKGATSTAAKYLAQTQNASDLIGGVSKSGDRYVDHTM... | Function: Cell-wall hydrolase involved in septum cleavage during cell division.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain ... |
Q9K0V3 | MIKLTRRQIIRRTAGTLFALSPIASAVAKTVRAPQFTAARIWPSHTYTRLTLESTAALKYQHFTLDNPGRLVVDIQNANINTVLHGLSQKVMADDPFIRSIRAGQNTPTTVRLVIDLKQPTHAQVFALPPVGGFKNRLVVDLYPHGMDADDPMMALLNGSLNKTLRGSPEADLAQNTTPQPGRGRNGRRPVIMLDPGHGGEDPGAISPGGLQEKHVVLSIARETKNQLEALGYNVFMTRNEDVFIPLGVRVAKGRARRADVFVSIHADAFTSPSARGTGVYMLNTKGATSSAAKFLEQTQNNADAVGGVPTSGNRNVDTA... | Function: Cell-wall hydrolase involved in septum cleavage during cell division.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 45190
Sequence Length: 416
Subcellular Location: Periplasm
EC: 3.5.1.28
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P0A4M7 | MKKYIFMRVLRSLVSIFLVTTLTYTIIYTLVPRKLIFKQDPNYNKIATTADKRDNYENTVFERMGYIEYYDTKELQEKASSMDSSVTVEANATNKAIYEKYINQLGHGWTLGEFTESGQFYATREIPIFERVFHFYANLIDIDHTNKIQDPENPDLKRYLRFENDPAIGWSLVGSGTKHKYLLYFNSQFPFVHQNFVNLNLGDSYPTYANTPVLQVITQGQGQTKTAQVQFPTGKKTSSVNIYSRTYKSPSQADSREVASYGKDDPYTATESNYQYPSMIVSSAITGLIGLVLAYALAVPLGSAMARFKNTWIDSLSTGA... | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55623
Sequence Length: 498
Subcellular Location: Cell membrane
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Q8EI85 | MALACLNSLNANAEIFSFDTRNSLNSDTLVLFHSADSTTYSLDFLPQSTQDQLNLAVADNSFSGKRGEVLEILVPSEIDAKRVLLVGIGDAKTLTPGEINALGGNIAAKLETVPQATVRVLTQGLNNAPLFGSELAHGIELRSYRYTQFKASNRVEKNYQIGVDDLSLNQKHHKNLQAVEAGVFLARDLTNAPAGNMYPESFANEARKLKSLGVKVTVLEAKDIERLNLGALAAVGKGSERPPKLVVAHWPGSKEAPIALVGKGITFDSGGYNIKATGTSIARMKSDMAGAATVLGTVKAMAIQKAPVNLVAIMPMAENM... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which... |
Q6FFD8 | MKFTLQSTAPQSAQHEYLLVLVTEQQLKNTADTYKINTLDTITHTSQFKSGFNEVLTLIGQAETCSYLNLVGLGDLKDLQPAKIAKLAQTIIKLVQTKFKQIHLDISALPIELHYLFALNLTQANYVFDEFKSKKSEAQLEQIHLITAQTGLTTQQLDLIQAIASGQDLARDLGNRPGNICFPEYLADQAKALAHEFPELLKVTILDEQQMADLGMNAFLAVSQGSDRPGRIITLEYNAQLEQAPVVLVGKGVTFDTGGISIKPAQGMDEMKFDMCGAASVLGTIRTLCEARLPIHVVGAVAAAENMPSGQATRPGDIVT... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
B0VMG3 | MKFTTYTTFPEQTSNESLWILVDSEQLQSNLNTYQINNLESILTATQFKANFNETLPLFGQLSTQPHSQLLGLGKAAELQAAKLAKLAQTIIKSAQNKFKHIAIDIAALPVEYHYLFALSLTQAAYGYDEFKSTKNEFVLQQVDLISSQTSLDENQLALVHAVQSGQSYARDLGNRPGNICFPEYLAEQALALAAEFPDLLKVTVLNEQQMADLGMYAFLAVSKGSERPGRIVTLEYQAQLEQAPVVLVGKGVTFDTGGISLKPGLGMDEMKFDMCGAASVLGTIRALCEARLPIHVVGAIAAAENMPSGKATRPGDIVT... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
C1F4B7 | MKTTLVSTPLAQLETELLAVFATDTAPAADMANGTQASPQVQLLTRDAALDAAVKTILASGDFKAEANETLLIHAPQGMAARRLLLVGAGKQARFTVHALRKAAGSAVRAARAKNIREATLAIPQSQGLDVTATARALGHGAAVADFDPDFYRSDRKDKSLQSLTLALPEATDANAAEAGLREGIALGESQNLTRTLVNEPGNRLTPTLLGEQAKKMCAEQGLRCQVYSSEKLHELKMGSFWSVTQGSDEPPALIVMEYTPEGAAEGPVLGLVGKGITFDSGGLSLKPADSMEKMKYDMAGAAAMIGAMRAIALLKPRIK... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
P45334 | MKYQAKNTALSQATDCIVLGVYENNKFSKSFNEIDQLTQGYLNDLVKSGELTGKLAQTVLLRDLQGLSAKRLLIVGCGKKGELTERQYKQIIQAVLKTLKETNTREVISYLTEIELKDRDLYWNIRFAIETIEHTNYQFDHFKSQKAETSVLESFIFNTDCAQAQQAISHANAISSGIKAARDIANMPPNICNPAYLAEQAKNLAENSTALSLKVVDEEEMAKLGMNAYLAVSKGSENRAYMSVLTFNNAPDKNAKPIVLVGKGLTFDAGGISLKPAADMDEMKYDMCGAASVFGTMKTIAQLNLPLNVIGVLAGCENLP... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which... |
A1WUV1 | MELKTKSGDPARQRTACVVVGVYERRRMSEAARAVDAASDGYLSHLLRRGDLEGEAGQTLLLPDCPGVRTDRVLLVGCGRERDFNERTYRKAVTAAARALEQAGTGEAILFLPELPVRGRDVAWRVAATAEILETTLYRFDTYKSDPRPPRRPLRQATLAVPRRADLRRAQPALTLGQAAGRGANFSRDLGNTPANICTPGYLGEQAEALAQRFDGVRAEILGPAELEEQGLAALLAVARGAEAPPRLVVLHYRGADDDQAPVALVGKGITFDSGGISIKPSASMDEMKYDMSGAAAVFGAVHAAAEAQLPLNLVAVIPA... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q7VGF0 | MKVSISHKNNFKGVSYQAQALLMSKSVFAKSPYAKLCKSFGFEGEGKFFLQEQALLLVCVEELGLDSIREAGASIARHFRTLPYKNVNVALNGKLDDSKAYALLLGALLGVYECVSYKTKTPPLHLKEIILLDEKNEVASESVLKKVHIVAQSVNEVREIINTIPQVATPKYLAKYAKELSKEVGNLECKILDEEALQKEKMGAFLAVNRASCNPPRLIHLSYKPKGAKKRIVLVGKGLTYDCGGLSLKPADFMVTMKADKSGGCAVMGIIKAIAQLGANIEVHSIIGAAENMIGGNAYKPDDVLYSREGKSIEVRNTDA... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
O25294 | MLKIKLEKTTFENAKAECSLVFIINKDFSHAWVKNKELLETFKYEGEGVFLDQENKILYAGVKEDDVHLLRESACLAVRTLKKLAFKSVKVGVYTCGAHSKDNALLENLKALFLGLKLGLYEYDTFKSNKKESVLKEAIVALELHKPCEKTCANSLEKSAKEALKYAEIMTESLNIVKDLVNTPPMIGTPVYMAEVAQKVAKENHLEIHVHDEKFLEEKKMNAFLAVNKASLSVNPPRLIHLVYKPKKAKKKIALVGKGLTYDCGGLSLKPADYMVTMKADKGGGSAVIGLLNALAKLGVEAEVHGIIGATENMIGPAAY... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which... |
Q9H4A4 | MASGEHSPGSGAARRPLHSAQAVDVASASNFRAFELLHLHLDLRAEFGPPGPGAGSRGLSGTAVLDLRCLEPEGAAELRLDSHPCLEVTAAALRRERPGSEEPPAEPVSFYTQPFSHYGQALCVSFPQPCRAAERLQVLLTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKYKYSALIEVPDGFTAVMSASTWEKRGPNKFFFQMCQPIPSYLIALAIGDLVSAEVGPRSRVWAEPCLIDAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (... |
O09175 | MESSGPSSCHSAARRPLHSAQAVDVASASSFRAFEILHLHLDLRAEFGPPGPGPGSRGLNGKATLELRCLLPEGASELRLDSHSCLEVMAATLLRGQPGDQQQLTEPVPFHTQPFSHYGQALCVVFPKPCCAAERFRLELTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKCTYSALVEVPDGFTAVMSASTWERRGPNKFFFQMSQPIPSYLIALAIGDLASAEVGPRSRVWAEPCLIEAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (... |
P00811 | MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITPP... | Function: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 41556
Sequence Length: 377
Subcellular Location: Periplasm
EC: 3.5.2.6
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Q48743 | MKRLLAFCLLFFAALGQAKVPPPARSAADAEIQRAVAAFMQQYQVPGVAVGITVDGAERYYNYGVSSRKTQAKVGANTLFEVGSVSKTFTATLASYAQVNQQLSLADHPGKYLPEMKGHDFDKVTLLNLGTHTAGGFPMQVPTQVKTDQQLTAYFQSWHPQYPAGTKRTYANPGIGMLGVIAAKSMRMPFQKAMTGVLLPKLGLTNTYLTVPPAKMAFYAQGYDDKGQPVRMSPGALWEPTYGIKTTARDLLRFVEINLDQVKVEPKLKRAIDGTHVGYYRLGEMTQGLVWEQLPYPASETSLQANSSQKVIFESNAVAA... | Function: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 41878
Sequence Length: 385
Subcellular Location: Periplasm
EC: 3.5.2.6
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P94958 | MKKSLSATLISALLAFSAPGFSAADNVAAVVDSTIKPLMAQQDIPGMAVAVSVKGKPYYFNYGFADVQAKQPVTENTLFELGSVSKTFTGVLGAVSVAKKEMTLNDPAEKYQPELALPQWKGITLLDLATYTAGGLPLQVPDAVKSRADLLHFYQQWQPSRKPGDMRLYANSSIGLFGALTANAAGMPYEQLLTARILAPLGLSHTFITVPESAQSQYAYGYKNKKPVRVSPGQLDAESYGVKSASKDMLRWAEMNMEPSRAGNADLEMAMYLAQTRYYKTAAINQGLGWEMYDWPQQKDMIINGVTNEVALQPHPVTDN... | Function: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 41272
Sequence Length: 379
Subcellular Location: Periplasm
EC: 3.5.2.6
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O69773 | MDNSMKNIFRQGRLFIALSLAMTSISAFALTQQEVDDIIKPLMKQEQIPGMSVAISVNGKQAIYHYGVQSKQTQIPVSDRTLYEIGSLSKTFTATLATYAQIQGKLDFSQSVSHYLPELKGSAFDNVSVMNLATHTSGLSLFVPSDIKTNDQLMAYYQKWLPDNEVGQYRSYSNLGVGLLGIVTAKQLNMPFSQAMEKLMLPSLGLKHTYIHVPKSQEKYYAQGYNKQNQPVRLNLEILGPEAYGLKSNAKDLIRYLEINMQSIKVAKTWQEAIENTHTGVYLTDSFVQDMMWESYPWPVSLSQLLQGNRDDMALKPQKV... | Function: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 43366
Sequence Length: 384
Subcellular Location: Periplasm
EC: 3.5.2.6
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P24735 | MRDTRFPCLCGIAASTLLFATTPAIAGEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRVTPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMAL... | Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 43401
Sequence Length: 397
Subcellular Location: Periplasm
EC: 3.5.2.6
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P85302 | ATDIRQVVDSTVEPLMQQQDIAGLSVAVIQNGKAQYFNYGVANKDSKQPITENTLFEIGSVSKTFTATLAGYALANGKLKLSDPASQYLPALRGDKFDHISLLNLGTYTAGGLPLQFPEESDNTGKMISYYQHWKPAFAPGTQRLYSNPSIGLFGHLAAQSLGQPFEKLMEQTVLPKLGLKHTFISVPETQMSLYAQGYDKAGKPVRVSPGALDAEAYGIKTSTSDLIHYVEVNMHPAKLEKPLQQAIAATHTGYYTVDGMTQGLGWEMYPYPIKVDALVEGNSTQMAMEPHKVNWLTPPQAAPLDTLVNKTGSTGGFGA... | Function: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 38728
Sequence Length: 358
Subcellular Location: Periplasm
EC: 3.5.2.6
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O05465 | MKLFTSTLTAKKSSTHKPLISLALSVLISTLLISETAQAADANDRLEQEVDKQAKQLMAQYQIPGMAFGIIVDGKSHFYNYGLADKQRNQPVSEDTIFELGSVSKTFAATLASYSELNGTLSLDDTADKYIPYLKNSAIGNTKLISLVTYSAGGYHYRCLKTLENNKELLQYYKSWHPDFPVNSKRLYSNASIGLFGYISALSMHSDYTKLIENTVLPSLKMTNTFVDVPANKMEDYAFGYNAAGEPIRVNPGMLDAEAYGIKSTSADMTRFMAANMGLVTVDSQMQQALDNNRKGYYRTKSFTQGLAWEMYPLPTTLQQ... | Function: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 44451
Sequence Length: 401
Subcellular Location: Secreted
EC: 3.5.2.6
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P18539 | MTKMNRCAALIAALILPTAHAAQQQDIDAVIQPLMKKYGVPGMAIAVSVDGKQQIYPYGVASKQTGKPITEQTLFEVGSLSKTFTATLAVYAQQQSKLSFKDPASHYLPDVRGSAFDGVSLLNLATHTSGLPLFVPDDVTNNAQLMAYYRAWQPKHPAGSYRVYSNLGIGMLGMIAAKSLDQPFIQAMEQGMLPALGMSHTYVQVPAAQMANYAQGYSKDDKPVRVNPGPLDAESYGIKSNARDLIRYLDANLQQVKVASVARRWPRRTSVITSAGAFTQDLMWENYPYPVKLSRLIEGNNAGMIMNGTPATAITPPQPE... | Function: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 41096
Sequence Length: 376
Subcellular Location: Periplasm
EC: 3.5.2.6
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P81073 | MNQKHLLRFIKKSYRVDADRVVYDAK | Function: AMP deaminase plays a critical role in energy metabolism.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Sequence Mass (Da): 3195
Sequence Length: 26
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
EC: 3.5.4.6
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P23109 | MPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFHLETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQITGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIK... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Sequence Mass (Da): 86490
Sequence Length: 747
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
EC: 3.5.4.6
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P10759 | MPLFKLTGQGKQIDDAMRSFAEKVFASEVKDEGGRHEISPFDVDEICPISLREMQAHIFHMENLSMSMDGRRKRRFQGRKTVNLSIPQSETSSTKLSHIEEFISSSPTYESVPDFQRVQITGDYASGVTVEDFEVVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEALVAIESFYPVFTPPPKKGEDPFRREDLPANLGYHLKMKGGVIYIYPDEAAASRDEPKPYPYPNLDDFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIK... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Sequence Mass (Da): 86432
Sequence Length: 747
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
EC: 3.5.4.6
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P0A3Z3 | MSNRRKNSLYPTLSAELSALMRTGWADTERHDLAPAEQAPYAALRRAALSARFPGERLVVPSGNLKVRSNDDTYPFRSYSGYVHMTGDQARDGALVLEPRPDGGHDAYCYQLPRDSRDDDEFWTGAHAELWTGRRRSLAESERVLGLPCRDVRTAAADLAAVSEVRTRIVRGIDPALEAAVTTDEERDAELEDALSDLRLVKDAWELGELRKAVDSTVRGFTDVVGELSRAVASSERWLEGTFFRRARLEGNAVGYGTICAAGEHATIMHWTDNDGPVRPGDLLLLDAGVETRSLYTADVTRTLPISGTFTPLQREVYDA... | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Sequence Mass (Da): 51925
Sequence Length: 470
EC: 3.4.11.9
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D5GHP2 | MTSDSTVDKILAGKYPAKQHAENVVERLLHVHPDLTDGVIYLESQRSKLYENSDQEVPFRQRRYFYYLSGCDLADSYLTYSIRDRKLTLFIPPIDPASVLWSGLPLSNSEALEKYDVDEVLPTSATALPTTSYSSLMFVIESQTSRTFHLQNTESLEPAIERARAIKDEYEVALIKKANRISALAHHSCLRAIKSAGNEREIEAVFTKECIANGAPKQAYSGIFGSGRSASTLHYVHNNQPLAGKLNLLLDAGAEYNNYASDITRTFPISGQFTKESREVYDIVLDMQKQCLAASKAGAVWDDIHILAHKVAIQGLLKIG... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Sequence Mass (Da): 50793
Sequence Le... |
C4JY72 | MSGVAEPDCYLTYDITSDTLTLYVPDFDLRRAIWMGPTLGLAEARERYNIDQAKYRSTLEQDILDWASRRAIGSVIYVIHDNQKPVVPFPYLKFNHEDLIPAMDTCREIKDGHEIGLIRRANEISTSAHTEILRNISGMRNEAEIQGKFLDSCVSLGAKNQSYEIIAASGENAAVLHYTRNDEPLKGRQLVCLDAGAEWNCYASDVTRTFPMQPRWPSAEAFSVYSVVQRMQEECIKRISEGVRYLDLHILAHKIAIEELLRLGIFRGGSIAEILKSGASLVFFPHGLGHHVGLEVHDVSGRSLMALEEQEYQGLPLRGC... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Sequence Mass (Da): 46144
Sequence Le... |
Q9AR04 | MSLTEEKPIRPIANFPPSIWGDQFLIYEKQVEQGVEQIVNDLKKEVRQLLKEALDIPMKHANLLKLIDEIQRLGIPYHFEREIDHALQCIYETYGDNWNGDRSSLWFRLMRKQGYYVTCDVFNNYKDKNGAFKQSLANDVEGLLELYEATSMRVPGEIILEDALGFTRSRLSIMTKDAFSTNPALFTEIQRALKQPLWKRLPRIEAAQYIPFYQQQDSHNKTLLKLAKLEFNLLQSLHKEELSHVCKWWKAFDIKKNAPCLRDRIVECYFWGLGSGYEPQYSRARVFFTKAVAVITLIDDTYDAYGTYEELKIFTEAVER... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin . Catalyzes the formation of both olefinic and oxygenated sesquiterpenes, with amorpha-4,11-diene being the major product .
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (+)-amor... |
Q46632 | MKDISFSVVIPAYNASESIITTLDCLNEQSYKNFDVIIVDDKSADAQKLAEVVSSERYSGLKINLVLSETKLNGAGARNRGIDLATGDYVCFLDADDEWHKDKLQQNLSLIERLEGQGDRRFIIYSQVNIIQDGSFLKVMPLKPVGEHESIAEYLFGCYGFIQTSTIVLKREDAAEIRFDERYIRHQDYDLCIRADKLGFKFVMIAQPLANYHMVTRFGSQHKGESVKYSLFWLDAMKPHLTRRDVYTYKAYKLPLRYKMDGKSLQASLSFARYFFLTNKDNRNDFLKRLMNKLRTRLTGK | Function: Involved in the biosynthesis of amylovoran, which functions as a virulence factor. May function as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor.
Sequence Mass (Da): 34788
Sequence Length: 301
Pathway: Glycan metabolism; exopolysaccharide bi... |
Q46633 | MAIYWIVSYSILVFCFFELAMINQASEAKTKILINYFFLIGVFALILFAGIRGPDSGMDDSQYVGFFHDFSRQTGMTGYQAVANIYRYENFFMVLAWVASCFTHESYFFLLFISFIAVSTNAWVYKKYSPLILCSLCLYSAHLFINKDMNQIRFGLCSAFAIAFICSLVARNYLLALLFIVLSTQSHSTGYTIVMIIPFFFIRERKYLPLVLVIASIPLGIIGGKKLFLDSLGIVPVLGERAASYSGTNFDTTSPVFGLANLKNIAFIGAFTLYYFRKGIMKEDRFVYILLIAYSIGAAVRITFSDFSIFGGRVGNLFLH... | Function: Involved in the biosynthesis of amylovoran which functions as a virulence factor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42570
Sequence Length: 375
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cell membrane
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Q46634 | MYKLLILIDGISNSGGTDRVASTLSSLLSNHNYDVTLYSLNSGEPYYPVDNKVSIRQPKSSMRLFKLFEFIRYAKNTRPDGVMIISMGKLSVQALLLSKLFRVKSRLICCDHVSIETFSAAVRKLKVFCYGLAEKVVVLTQHDKNYLTSAFSLKNVYVVGNISPFHHENSLNRFDDVFARKQNRVLAVGRLTYQKNFGRLLDIWKNVHKQGWKLLIVGDGEEKAELLEKIKKYHLEESAEIVSPSKKISEYYRSSGVIAMTSRYEGLPMVLIEAKNYALPAIAFDCKTGPAEIIKDDGYVVDYQSNELFTAQLNQLIASE... | Function: Involved in the biosynthesis of amylovoran which functions as a virulence factor. May be involved in the formation of galactose alpha-1,6 linkages in amylovoran.
Sequence Mass (Da): 39872
Sequence Length: 351
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
EC: 2.4.-.-
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Q46635 | MFSVLISLYNKEKPENLEQCLESLHQQTLNADEIVLVYDGPVSESLKAVATRWANLLPLVIVPLEKNLGLGKALNAGLERCTHNVVARMDTDDICLPERFEKQISYMESHPEVVLSGAAVIEFDEHGKERLKRLPLSNNDIHQFARMKNPFNHMCVVFRKDKVISAGSYQHHLYMEDYNLWLRIMSLGHPVANLPDVLMKVRAGSDMVNKRRGWNYIKSEVQLYRLKLALKQTGFIRGTLYFLIRTMTRLMPVKVMQFLYEKDRKG | Function: Involved in the biosynthesis of amylovoran which functions as a virulence factor.
Sequence Mass (Da): 30747
Sequence Length: 266
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
EC: 2.4.-.-
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Q46636 | MKRRELIRTAFSTIVATAALSSVSARARSEDLHGLTLKKVPPDAIPKNDVPIFSPDDVFTMPEQFWRDFKGKLYIGKAGTDPTLPQNLIDVFVKNANGGTALLSQPIDLNSETLKTFVAAKGALWSASEYSMALHNDNDEQIFYVPDVKNNGVSEFSRRLSQPGGYQLIGEISSFASLRQTRPLFSGAKVRLKGWHDGTEVGGGAFVGEMTPSEDDGGYIASSGQDFHWRRVSDDMNRITLFDFGAVADGKKDCLPAVMAMYHWAQNNNQKLSIQFPAGRFFISSFDISAKYIRFLRLAGAPVNFGYFPATTLVSDGKSE... | Function: Involved in the biosynthesis of amylovoran which functions as a virulence factor. May be involved in the polymerization or late modification of the repeating units.
Sequence Mass (Da): 82253
Sequence Length: 743
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Periplasm
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Q46628 | MREIEFTFKGLLIRLSLALSDLIFFNIALALAIVLINGFPGEILTGIPQHELDLKIATHILLSVICVGWFWVRLRHYTYRKPFWFELKEVFRTILIFSIVDLSVSALSKWELSRWIWILTWLLSMAMVPFGRACVKRLLNRKKLWKKQSIIIGSGKNAQEAWQALQSEEMMGFDVIAFYDVDGSQTALELFGVPVLKEEQQLWSLVDSDTQFIVAVEYEQSQSRDRWLKNLATHNCRSVSVIPSLRGVPLYGTDMAYIFSHEVMILRVSNNLAKHSSRFLKRTFDLVGALSIITLLLPALVILIFMVSRDGGAPIYGHER... | Function: Involved in the biosynthesis of amylovoran which functions as a virulence factor. May act as a sugar transferase and may be involved in the export of the repeating unit by flipping the lipid carrier to the periplasmic face of the inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da... |
Q8VYB5 | MGSSFETIDIATSARRIGVDNRISLKFYFRIADNILKQANIFRAEKNVIDLYVMLLRFSSLALETIPSHRDYRTSLKSNKEYLRMRLLDVLTELEKLKPVVQQRIDELYPKLKPRYNVQAHPANGSLGWSSAVKPSFNSYDHAKVRNPPGHNSGYMGSRGQQFLNAAPLEERFRKMSVNFRPNEETLSKHSILGPGGLSAQWQPPKYDTKVQYPSNIDFSPVVIPSFQQLVDSKPMITNGSNDEPEKPIVEPSVASNEKIQKNYTEELSSMISFEEPESVNENNLIRQPSPPPVLAEVQDLVPALCPEVREPECMIENSL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Zinc metalloprotease that cleaves 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57383
Sequence Length: 507
Domain: The JAMM motif is essential for the protease activity.
Subcellular Location: Me... |
Q6NKP9 | MVTLSSPSPSLSCVENVTCKSSHVSRVLISGTDNINHGESSEAKILRDVHISERLLEDFTELARENTEKDLETCGTLAAFLERGIFYVTTLIIPKQESTSNSCQAMNEVEVFSIQNERELYPVGWIHTHPSQGCFMSSVDLHTHYSYQVMVPEAFAIVVAPTDSSKSYGIFKLTDPGGMEVLRGCSETGFHPHKEPEDGNPVYEHCSNVYKNSNLRFEIFDLR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Zinc metalloprotease that cleaves 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Sequence Mass (Da): 24939
Sequence Length: 223
Domain: The JAMM motif is essential for the protease activity.
EC: 3.4.19.-
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Q5PNU3 | MKIDLNKVAREIEVDNRIPLRNYYRIADNLLRQASIYREEKNVVDLYIMLLRYSSLISETIPFHRDYQASLPQERLGSRKRLRAVINELESLKPEFNQLVDKLNRVEDESRQDGSDLPVVSYSSDAVEWPPAHKASYSRPDINKPLPTSQPSWTYNNNLTSSSNRTQIDQQFQKLSFDFLPPNQATLSRHSFLGPNGLKRQMVAPKSEIKVQYPSNTDWGSADNSGLIEAGPSSSSASLNGDSQEVSTLNSVLSLDDGRWQRHSEAVNSQFISDATEDPFQFVGMKQPSPPPVLAQVHQELAQICPSKVADPRPGPAIPS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Zinc metalloprotease that cleaves 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, but is not implicated in protein degradation by the 26S proteasome, deneddylation, or desumoylation. Required for intracellular trafficking (e.g. trafficking from the Golgi to the v... |
Q46630 | MINSILVVCIGNICRSPTGERLLKAALPERKIASAGLKAMVGGSADETASIVANEHGVSLQDHVAQQLTADMCRDSDLILVMEKKHIDLVCRINPSVRGKTMLFGHWINQQEIADPYKKSRDAFEAVYGVLENAAQKWVNALSR | Function: May function as a phosphatase required for amylovoran (an exopolysaccharide that functions as a virulence factor) production.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 15772
Sequence Length: 144
EC: 3.1.3.48
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Q46637 | MKILLVGNHTCGNRGDGAILRGIIDSLHLERTDLDIDIISRFPTSSSYLLQQNILPDELFLETKKSNSLVAKVKRRLMPKIMMAHIRGSGFFKNLAVPEYLQQFTDKLKQYDAVIQVGGSFFVDLYGPLQFEHSLCALLAKKPVYMIGHSVGPFQKERFNQIANFVFSRVNSLVLRESVSLEMMEKAGITTQKVIPGADTAFLVRTRTLDAPGHNLIHWQNQIAASKTIAITVRELAPFDKRLGVTQQEYEMAFGKVINAMIERGYQVVALSTCTGIDSYHRDDRMVAITLGDYVQQKDKYRVVMDEFNDLELGILLAGC... | Function: Involved in the biosynthesis of amylovoran which functions as a virulence factor.
Sequence Mass (Da): 46292
Sequence Length: 415
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
EC: 2.-.-.-
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Q46639 | MSSYIVHRQNITRKEQSTIYWVNVLLSMLTGLLLVAIAWPISWFYHLPQLGGLIMLTSLNFLVLGSLSQYQAHFIKAKRMILLAKIEMVTKFLAFAFTVILLYYSPLGVSAVILGLFANAALRIGCMIWFGDKSWRPTFEFDQGTFYSSLKYGIYQLGSQTINQLRTQADSLIVGKVMGAELLGVYSLAKELILQPLKLVTPVINRLALPRFAEKQHDPVRLQQLFLKGTFVIMLFSAIMYLAIGILSPVIVRVLYGPAHEAVGQLIPLMLLFGMLRPMGGLTGAISQANGRTNVEFYWNVVASIIVVLVLASVWIWPQV... | Function: Involved in the biosynthesis of amylovoran which functions as a virulence factor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43726
Sequence Length: 388
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cell membrane
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C9K7C1 | MYCDKGASSLANGLLPNVSGDITAKDNILDALDSSAEEHFWGRYIDGFEGQIFPQIPVSVHEAHLTGRARYEIILGNSMVTTLYTVSSIIRTGWALLVSQYTESQDVVIVSSLELPSQAMGGTILFPIRFRIRQDGRTEELLQSAKKHADKVLSSQKHDFPHTKDFVDPFSNSILLICTESQPSHSLEELLTELSASKKCALVLRCELLEDKISISAMFDPQVVRPRQTRRILDQLGHILKQISGSDMLVGDLDFLSPEDRQEIGRWNSRSALSDECIHALISKQAQQNPAAMAVNAHDGNFTYGELESYATRLAAHLIH... | Function: Nonribosomal peptide synthetase; part of the gene clusters that mediate the biosynthesis of AM-toxins, host-selective toxins (HSTs) causing Alternaria blotch on apple, a worldwide distributed disease (Probable). AM-toxins are cyclic depsipeptides containing the 3 residues 2-hydroxy-isovaleric acid (2-HIV), de... |
P37730 | MAKKAKFFKNGIWYWLFIAPTLLSLIIVVLIPFIIGIYYSFTDWNGINQPVFIGLKNFMTLRDDAEFWNSIIFTAKFAVACIVIINVVGLSLAMLVTRKIFARNFMRTAFYLPNLIGGLILGFIWNFIFVDVFQTISDATHIGWLGGWLSTTNTGFWGLVIVTSWQMIGYVMVIYIAYIESIPTDLIEASKIDGANSWQQFRNVVFPLIAPAFTVSLFITLSNSFKLFDQNLSLTAGAPGNTTQMITLNIYQTAFSAQEMAVGQAKAVIMFLIIAVISVIQVYLTQKREVEM | Function: Probably part of a binding-protein-dependent transport system starch degradation products. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32908
Sequence Length: 292
Subcellular Location: Cell membrane
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Q03045 | MRLLPSSCAGALSLLCSLAIAAPTELKARDLSSFIASERAIALQGALNNIGPDGSAVPGAGAGFVVASPSKANPDYFYTWSRDSALTLKMIIDEFILGNTTLQTIIEQYIHAQAVLQTVSNPSGTFLPDGVGLGEPKFMVDGTRFNGPWGRPQRDGPALRAIALMTYSNWLIKNGQFAEAKTKIWPIIANDLSYVGQYWNQSGFDLWEETYASSFFTIQNQHRALVEGAQLAHDLGVTCTGCDQAPEVLCFLQSFWNGKYIVSNINVNNGRTGLDGNSILGAISTFDIDAYCDSPTLQPCHSQSLANFKVLTDTFRNLYT... | Catalytic Activity: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
Sequence Mass (Da): 66432
Sequence Length: 616
Subcellular Location: Secreted
EC: 3.2.1.3
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O74254 | MKLLSKVFVTALGLTSIVNAAPTSSSSAEEAQKTVPVELSIGVKQLPNIHNDSAVDANAVAKGYSLVNVSLTARGLTGILKLKEATNIYGYDFEYLNLSVEYQSDTRLNVHIEPTDLTDVFVLPEELVVKPKLEGDAKTFNFENSDLVFEYDEEDFGFEVLRSSTREVLFSTKGNPLVFSNQFIQFNTTLPKGHSITGLGESIHGSLNEPGVVKTLYANDIADPIDGNIYGVHPVYYDQRYNTNTTHAVYWRTSAIQEVVVGETSLTWRALSGVIDLYFFSGPDPKDVIQQYVSEIGLPAMQPYWALGYHQCRWGYDTVE... | PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Catalytic Activity: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
Sequence Mass (Da): 105717
Sequence Length: 946
Subcellular Location: Secrete... |
P29761 | MSRKLIKYLPLLVLASSVLSGCSNNVSSIKIDRFNNISAVNGPGEEDTWASAQKQGVGTANNYVSKVWFTLANGAISEVYYPTIDTADVKEIKFIVTDGKSFVSDETKDTISKVEKFTDKSLGYKLVNTDKKGRYRITKEIFTDVKRNSLIMKAKFEALEGSIHDYKLYLAYDPHIKNQGSYNEGYVIKANNNEMLMAKRDNVYTALSSNIGWKGYSIGYYKVNDIMTDLDENKQMTKHYDSARGNIIEGAEIDLKKNSQFEIVLSFGNSEDEAVKASIETLSENYDSLKSAYIDEWEKYCNSLNNFNGKANSLYYNSMM... | Function: CGA has typical kinetic properties for a glucoamylase, but this bacterial enzyme had higher isomaltose-hydrolyzing activity than other eukaryotic glucoamylases.
Catalytic Activity: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of b... |
D8Q9M3 | MGLASTVSLALLGLCSLARAQTSAADAYVSAESPIAQAGILANIGPSGSKSHGAASGVIIASPSTSNPDYLYTWTRDAALVSRALVDEFIEGESSLQSVIDSYVSSQQKLQRVDNPSGSYTSGGLGEPKFNIDLTAFTGAWGRPQRDGPALRAITLITYGNHLLSSGNTSYVTDTIWPVVKADLDYVVSYWNQTGFDLWEEVSSSSFFTTAEQHTALRLGATFATAVGASASTYLTQADNVLCFLQSYWNSNGGYATANTGGGRSGIDANTVLTSIHTFDIEAGCDSVTFQPCSDRALSNLKVYVDSFRGLYSINPTGAT... | Catalytic Activity: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
Sequence Mass (Da): 60941
Sequence Length: 576
Subcellular Location: Secreted
EC: 3.2.1.3
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A1DN11 | MTVTISFEPYVGSSVDALSIPLYLRCQLVFKLSKPLAAVPLLESGVNRLVQALPFLSGEFTAVPASDGGKEILLVRPVLNFELSRILKIKYHETSLRHVCKQMNRPSSQGGDLPHEPYMPYPRLPDPSRPQPIVGFQVNVHTDGIILSVATHHCSFDATGMGSIVQNLAACCRSPPSDEPDLTTSPAQEAEARKVLSQVRETPFDPKMFPEYRPLDSMLSYYKGVQSALQGRQTTIVNRCFTIAADKINALKRRCNQLIPEMVKKYGLSTEDAIGSAWVSSNDVVAALLWTCINRARYPEIRERSVHQLPPDLLHATSSL... | Function: O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the prenylated pyrroloindoline diketopiperazine acetylaszonalenin . The first step in the pathway is the formation of (R)-benzodiazepinedione by condensation of tryptophan and anthranilic acid catalyzed by the non-ribosomal peptid... |
P54802 | MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKPGLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGELTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYLALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTPVLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELIKEFGTDHIYGADTFNEMQPP... | Function: Involved in the degradation of heparan sulfate.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides.
Sequence Mass (Da): 82266
Sequence Length: 743
Subcellular Location: Lysosome
EC: 3.2.1.50
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P80884 | MTSKVQLVFLFLFLCVMWASPSAASCDEPSDPMMKQFEEWMAEYGRVYKDNDEKMLRFQIFKNNVNHIETFNNRNGNSYTLGINQFTDMTNNEFVAQYTGLSLPLNIKREPVVSFDDVDISSVPQSIDWRDSGAVTSVKNQGRCGSCWAFASIATVESIYKIKRGNLVSLSEQQVLDCAVSYGCKGGWINKAYSFIISNKGVASAAIYPYKAAKGTCKTNGVPNSAYITRYTYVQRNNERNMMYAVSNQPIAAALDASGNFQHYKRGVFTGPCGTRLNHAIVIIGYGQDSSGKKFWIVRNSWGAGWGEGGYIRLARDVSS... | Function: Cysteine protease . Displays a high level of diversity in substrate specificity at the P1-P1' cleavage site . A hydrophilic P1 residue is preferred, with Gln or Arg strongly preferred . Favors an Ile/Leu residue at the P2 position of substrates, with an overall higher preference for Leu . The optimal tripepti... |
A1DN10 | MSPLSMQTDSVQGTAENKSLETNGTSNDQQLPWKVLGKSLGLPTIEQEQYWLNTAPYFNNLLIQCGYDVHQQYQYLAFYHRHVLPVLGPFIRSSAEANYISGFSAEGYPMELSVNYQASKATVRLGCEPVGEFAGTSQDPMNQFMTREVLGRLSRLDPTFDLRLFDYFDSQFSLTTSEANLAASKLIKQRRQSKVIAFDLKDGAIIPKAYFFLKGKSLASGIPVQDVAFNAIESIAPKQIESPLRVLRTFVTKLFSKPTVTSDVFILAVDCIVPEKSRIKLYVADSQLSLATLREFWTLGGSVTDSATMKGLEIAEELWR... | Function: Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of the prenylated pyrroloindoline diketopiperazine acetylaszonalenin . The first step in the pathway is the formation of (R)-benzodiazepinedione by condensation of tryptophan and anthranilic acid catalyzed by the non-r... |
Q96K21 | MNYDSQQPPLPPLPYAGCRRASGFPALGRGGTVPVGVWGGAGQGREGRSWGEGPRGPGLGRRDLSSADPAVLGATMESRCYGCAVKFTLFKKEYGCKNCGRAFCSGCLSFSAAVPRTGNTQQKVCKQCHEVLTRGSSANASKWSPPQNYKKRVAALEAKQKPSTSQSQGLTRQDQMIAERLARLRQENKPKLVPSQAEIEARLAALKDERQGSIPSTQEMEARLAALQGRVLPSQTPQPAHHTPDTRTQAQQTQDLLTQLAAEVAIDESWKGGGPAASLQNDLNQGGPGSTNSKRQANWSLEEEKSRLLAEAALELREEN... | Function: Key regulator of abscission step in cytokinesis: part of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Together with CHMP4C, required to retain abscission-competent VPS4 (VPS4A and/or ... |
Q9DAZ9 | MESRCYGCAVKFTLFKKEYGCKNCGRAFCNGCLSFSALVPRAGNTQQKVCKQCHTILTRGSSDNASKWSPPQNYKKRVAALEAKKKSSTSHSQSLTHKDQAIAERLARLRQENKPKSVPSQAEIEARLAALKDEVQGPIPSTQEMEDRLAALQGRVPPSHTVRPAHQAPDTRTQAQQTQDLLTQLTAEVAIDENCQPRASASLQNDLNKGAARSQRTNSQGQASQSLEEEKYKLLAEAAVELQEENTRQERILALAKRLAVLKGQDPSRVTLQDYHLPDSDEDEETAIQRVMQQLTEEAALDEASGFNIPEKPAPGSRAQ... | Function: Key regulator of abscission step in cytokinesis: part of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Together with CHMP4C, required to retain abscission-competent VPS4 (VPS4A and/or ... |
Q84BZ0 | MSADPFVIVGAGHAARRTAEALRARDADAPIVMIGAERELPYDRPALSKDALLNDDGEQRAFVRDAAWYDAQRIALRLGTRVDAIEREAQRVRLDDGTTLPYAKLVLATGSRVRTFGGPIDAGVVAHYVRTVADARALRAQLVRGRRVAVLGGGFIGLEVAAAARQLGCNVTVIDPAARLLQRALPEVVGAYAHRLHDERGVGFQMATLPRAIRAAAGGGAIVETDRGDVHADVVVVGIGVLPNVELAQAAGLDVDNGIRVDAGCRTADRAIFAAGEVTMHFNPLLGRHVRIESWQVAENQPAVAAANLLGADDAYAELP... | Function: Part of the multicomponent anthranilate dioxygenase, that converts anthranilate to catechol. Probably transfers electrons from ferredoxin (AndAb) to NADH.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 42869
Sequence Length: 40... |
Q9BQD7 | MEQDDPVEALTELRERRLGALELLQAAAGSGLAAYAVWALLLQPGFRRVPLRLQVPYVGASARQVEHVLSLLRGRPGKTVDLGSGDGRIVLAAHRCGLRPAVGYELNPWLVALARLHAWRAGCAGSVCYRRKDLWKVSLRDCRNVSVFLAPSVLPLLEDKLRTELPAGARVVSGRFPLPTWQPVTAVGEGLDRVWAYDVPEGGQAGEAASSRIPIQAAPGPSSAPIPGGLISQAS | Function: Mitochondrial protein-lysine N-methyltransferase that trimethylates adenine nucleotide translocases ANT2/SLC25A5 and ANT3/SLC25A6, thereby regulating mitochondrial respiration . Probably also trimethylates ANT1/SLC25A4 .
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(... |
Q501J2 | MDQDDPAEALTELREKRLGLLEIVQAAAGSGLAVYTIWALLLQPGFRRVPLRLQVPYVGASARQVENVLSLLRGRPGKMVDLGSGDGRIVLAAHQCGLRPAMGYELNPWLVGLARLHAWRAGCSASVCYHRKDLWKVSLRDCHNVSVFLAPSVLQLLEDKLQAELPVGARVVSGRFPLPTWQPVAVVGEGTDRVWAYDVHGSGPTVSSCGVPIKAIPESSSTLVPRAPV | Function: Mitochondrial protein-lysine N-methyltransferase that trimethylates adenine nucleotide translocases ANT2/SLC25A5 and ANT3/SLC25A6, thereby regulating mitochondrial respiration. Probably also trimethylates ANT1/SLC25A4.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)... |
Q9GZV1 | MAKAPSWAGVGALAYKAPEALWPAEAVMDGTMEDSEAVQRATALIEQRLAQEEENEKLRGDARQKLPMDLLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLV... | Function: Functions as a negative regulator of myocyte differentiation. May interact with both sarcoplasmic structural proteins and nuclear proteins to regulate gene expression during muscle development and in response to muscle stress.
PTM: Phosphorylation at Ser-99 by PKB/AKT2 in response to oxidative stress induces ... |
Q9WV06 | MEGPEAVQRATELIEQRLAQEEETEKLRRSAPGKLSMDMLVLEEEKRLGVQSPALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAAAQEPPPEPEEITGPVNEETFLKAAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKLLSTPLHVAVRTGHVEIVEHFLSLGLDINAKDREGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTPTDLVQLWQADTRHALEHPEPESEQNGLERPGSGRE... | Function: Functions as a negative regulator of myocyte differentiation. May interact with both sarcoplasmic structural proteins and nuclear proteins to regulate gene expression during muscle development and in response to muscle stress.
PTM: Phosphorylation at Ser-68 by PKB/AKT2 in response to oxidative stress induces ... |
Q96BM1 | MPWDARRPGGGADGGPEASGAARSRAQKQCRKSSFAFYQAVRDLLPVWLLEDMRASEAFHWDERGRAAAYSPSEALLYALVHDHQAYAHYLLATFPRRALAPPSAGFRCCAAPGPHVALAVRYNRVGILRRILRTLRDFPAEERARVLDRRGCSRVEGGGTSLHVACELARPECLFLLLGHGASPGLRDGGGLTPLELLLRQLGRDAGATPSAAGAPASAPGEPRQRRLLLLDLLALYTPVGAAGSARQELLGDRPRWQRLLGEDKFQWLAGLAPPSLFARAMQVLVTAISPGRFPEALDELPLPPFLQPLDLTGKG | Function: Substrate receptor subunit of a cullin-RING superfamily E3 ligase complex (CUL5-based E3 ubiquitin ligase complex) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . Depending of the metabolic state of the cell, promotes the proteasomal degradation of IMPDH2, the rat... |
C5BV64 | MRVLGMISGTSHDGIDVAVVRFTLDAGGAQLRGVVEHATTVPYPTALRARVAGALPPAQVGMAEVCALDADLGHAFADAAAEAAAAPDVPEPPDLVCSHGQTMYHWVAEGSALGTLQLGSPAWIAERLGVPVVADVRIRDVTAGGQGAPLVPLLDELLLAGASGRTAVLNLGGIANVTVVGDGADPVAYDVGPANALIDAAVAAAGRGAYDADGALAAAGRVHAPLLDALLTEPYYARRPPKSTGKELFDPGYVDRVRRGAGGAAAADLSLEDLVSTLTELTARVVAQDVRRLDVARLVVSGGGVRNPVLLGALTAAVPG... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q7VUW3 | MDSTTHGPRTHVPGRLFIGLMSGTSMDGADGVLVRLDGPRPEVLASASLPMPAALRDELFALNHAGANELERAALAANGLARLYARAVRQLLDQAGLQPGDVAAIGAHGQTVRHRPDLGYTLQLNAPALLAELAGIDVVADFRSRDVAAGGQGAPLVPPFHAALFAGGQARAVLNLGGIANVTLLEPGRPPRGFDTGPANVLLDAWCQRHTGQPYDADGRFAAQGQVLADLLEHLIASEPWFALAPPKSTGRDLFNLDWLLARLQAFDGPAPQPQDVQATLQRLTARTVANAIDASAAAPRDVLVCGGGARNPGLMRELA... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
A6X3N5 | MQPIWAVGLMTGTVLDGNIDVALLKTDGETIAEFGAYALKPYPRWIRDLLEQAQAEARVWNFEGAEPAIFAEAEEALTRAQSAAVRELVEESGLSMADIGVVGFHGQTVLHRAPQAGRLGDTRQLGDGRLMSQLLATKVAYDFRTADIRAGGQGAPLAAVYHAALLRSADASGNTAILNLGGVGNITWWDGDDALVAFDTGPANAPINDFMKKRGLGEMDRDGALAAKGKVDEDRLAELLKHPYLIAPYPKSLDRFDFTEMMADGLNEENGAATLTAFTTSAVGKALDILPRRPKRLAVSGGGRRNPTMMHMLVERAEVE... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q46HU0 | MRVLGLMSGTSADGIDAVLVDFTGDPSRPKWQILNTFSYEYPSSIREKIIQVGQGLKISSKDWLELAEEITELNAFAARTCDPDSTAEVVGCHGQTLFHRSVKKSKRGGSLQILLGPLLANLLDQIVIYDFRSKDIASGGHGAPLVALVDEALVGRLYGWRGVLNLGGIANLTIIPPKTGIDKTSQCLGWDCGPANSLVDLAVKESTNSSLTFDENGSLASLGIPKLEIIDKWLRDPFFYLEPPRSTGREQFGFQYLQKRKKELGDISKEDLISTLTTFTASIISQDLDNLFKLKQIRLIELLVAGGGSKNLFLMRQLQK... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q15RS7 | MNKHIEQLYRSAKKRSRLIIGLMSGTSLDGLDVALCRIEGHGTDTQIELVAFCTVDYDDGYKQKIKSVFAKRQVDLQQVTLLNPWVGVLHGQMVNQCLEKWNIAATDIDAIASHGQTIYHCPLGQHGQSEFGNATLQIGDADHLAVTTGILTIGDFRQKHIAAGGEGAPLAVYGDYLFFTSKQENRILLNMGGIANLTFLPCSADASAVFSSDIGPGNTIMDAYVQRHFSPLHYDKDSAMASQGKVHLGLLDSLLEHAFFALDFPKTTGPEVFNLDYLSVAQAHSATRQLAHEDVLATLNLFSARTIANAINDAAIELEE... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q9I5Q5 | MPRYLGLMSGTSLDGMDIVLIEQGDRTTLLASHYLPMPAGLREDILALCVPGPDEIARAAEVEQRWVALAAQGVRELLLQQQMSPDEVRAIGSHGQTIRHEPARHFTVQIGNPALLAELTGIDVVADFRRRDVAAGGQGAPLVPAFHQALFGDDDTSRAVLNIGGFSNVSLLSPGKPVRGFDCGPGNVLMDAWIHHQRGEHFDRDGAWAASGQVNHALLASLLADEFFAARGPKSTGRERFNLPWLQEHLARHPALPAADIQATLLELSARSISESLLDAQPDCEEVLVCGGGAFNTALMKRLAMLMPEARVASTDEYGI... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P (By similarity). Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus ... |
Q3K5W7 | MALYIGVMSGTSLDGLDIALIEQSSAINLVATHYIPMPDTLRAELLGLCAGGPDEIARSAIAQQNWVKLAAQGIHTLLEQQQLKPEAIRAIGSHGQTIRHEPARGFTVQIGNPALLTELTGITVVSDFRSRDVAAGGQGAPLVPAFHEALFEERTGNRAVLNVGGFSNLSLIEPNKPVAGFDCGPGNVLMDAWIHQQRGENYDRNGQWAASGKVEPTLLKALLSDPFFVTQGPKSTGREVFNLPWLEQQLSCLPGFAAENVQATLLELTALTIVESLQSAQSNTEELLVCGGGAHNVTLMKRLADLLPNAKVASTATHGV... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q88QQ4 | MALYLGVMSGTSLDGLDIALVEQGEQLELLATHYLPMPPDLRQDLLALCSSGPDEIARAALAENRWASLAGEGIRQLLARQGLKPEAVRAIGSHGQTIRHEPARGFTVQIGNPALLAELTGISVVADFRRRDVAAGGQGAPLVPAFHETLFSQLGRRLAILNVGGFSNLSLIEQDKPVHGFDCGPGNVLLDAWIEREHGHPYDADGAWAASGVAQPGLLSALMADPFFAGSGPKSTGREVFNLPWLDRHLANLPAYRAQDVQATLLELTARSIIDSLGKAQQGTEALLVCGGGARNGALMARLGQLLPAARVASTGAYGV... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P (By similarity). Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus ... |
Q3ICY1 | MHPHISKLYNSALKPSRLIIGLMSGTSLDGLDVALCKITAAGVHTQIEVLKFTTVDYSDDYKTKIKQVFAKRECNLEYLTLLHPWVGKFHGDMVNQCLNSWQVNPANIDVIASHGQTIYHCPKSQHQYNDFNNGTLQIGDSDQIAVTTGITTIGDFRQKHIAAGGEGAPLAVYGDYLFFSSSDENRILLNMGGIANLTFLPQNGDSNAVFSSDIGPCNTIMDAYVQRYFNNMHYDENAAIAKAGFINTALLTALCDNHFLTLKMPKTTGPEVFNLAYLEAAQQASNTQKLSHQDVMATLNRFTAEVIANALNTCVKMAPN... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q4FQ90 | MDDLNYATLTEALEQTVFENFDDGLYIGMMSGTSLDGMDAILCQFSNHTNSSNISNEDNTQQPMHLLATYSQDFPPRLREVLLALCQPNGINQLTPTAGEPDSELEWFGWASKAYAEFASDVVNTLLQQSNTDIESVLAIGCHGQTVRHRPQMGFSLQLVDANIIAERTGISVVSDFRRRDMAVGGQGAPLVPAFHQALFAVPDSTRILLNLGGIANIAVLPAISDDLSDFNEHSDNQPSDSVVGYDTGPANLLLDAWTALHTDKDYDAGGTWAQSGQVVEPLLNQLLEHPFFVKAYPKSTGREDFNLAWLQDELQKFDQ... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q8Y241 | MTTLASSISERYIGLMSGTSLDGVDGVLVDFSGPRPMLLTDAYVPFPPALRQAFFDLQSAGHNEIHREALAANALADLYAECVAQLLHESGCDPREVRAIGAHGQTIRHQPGEHDGIGYTRQTQHAAVLAERTGIDVIADFRSRDIAAGGQGAPLVPAVHRALFALPDAWRVVCNIGGIANLTVLPPQQSDARDRVLGFDCGPGNALLDYWVHAHRGEAYDRNGEWARSGWIDAALLETLRSEPFFARMPPKSTGRDLFNPTWLQQQAGDTLERIRPEDVQATLLALTADTIADAVRTHAPRTASLVVCGGGARNGALMQ... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q6P6B7 | MAQPGDPRRLCRLVQEGRLRALKEELQAAGGCPGPAGDTLLHCAARHGHRDVLAYLAEAWGMDIEATNRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRKNLGVIQELVEHGANPLLKNKDGWNSFHIASREGDPLILQYLLTVCPGAWKTESKIRRTPLHTAAMHGHLEAVKVLLKRCQYEPDYRDNCGVTALMDAIQCGHIDVARLLLDEHGACLSAEDSLGAQALHRAAVTGQDEAIRFLVSELGVDVDVRATSTHLTALHYAAKEGHTSTIQTLLSLGADINSKDEKNRSALHLACAGQHL... | Function: Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity. Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing the charging of S... |
A2AS55 | MALPGDPRRLCRLVQEGRLRDLQEELAVARGCRGPAGDTLLHCAARHGRQDILAYLVEAWSMDIEATNRDYKRPLHEAASMGHRDCVRYLLGRGAVVDSLKKADWTPLMMACTRKNLDVIQDLVEHGANPLLKNKDGWNSFHIASREGHPVILRYLLTVCPDAWKTESNIRRTPLHTAAMHGCLEAVQVLLERCHYEPDCRDNCGVTPFMDAIQCGHVSIAKLLLEQHKACSSAADSMGAQALHRAAVTGQDEAIRFLVCGLGIDVDVRAKSSQLTALHYAAKEGQTNTVQTLLSLGADINSTDERNRSVLHLACAGQHV... | Function: Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity . Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing the charging of ... |
Q499M5 | MAPPGDPRRLCRLVQEGQLRALREELEVAGGCWDPEMFRGSQGPAGDTLLHFASRHGRQDILAYLVEAWSMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAVVDSLKKADWTPLMMACTRKNLEVIQDLVEHGANPLLKNKDGWNSFHIASREGDPVILRYLLTVCPDVWKTESKIRRTPLHTAAMHGCFEAVQELLERCHYEPDCRDNCGVTPFMDAIQCGHVSIAKLLLENHEACSSATDSLGAQALHRAAVTGQDEAIRFLVCGLGIDVDVRAKSSQLTALLYAAKEGQTSTVQTLLSLGADINSTDERNRSAL... | Function: Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity. Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing the charging of S... |
Q945B4 | MGSCSPQLPLICLSDQTLKPGSSKWVKVRSDVRKALEDYGCFEAKIDQVSMELQGSVLKAMQELFALPTEAKQRNVCPKPFAGYFSHNGLSESFGIKDANILEKAHEFTQQLWPEGNKSIKMIQLYAEKLAELDMMVRRLILESYGIEYFIDEHLNSTYYRMRLMKYIARPDNDITAAVGANVDNGANDNADGDANVNDDGASIGVKVNVDVGDDVNDNDSVNIGVGVDINVETNVNGDLDAEANGDATAWVVGAVSGNASVGAKEANVDAELGLPSHTDKSLSGIIYQHQIDGLEVKTKEGKWIRVKPAPNTVIVIAGD... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase involved in glucosinolates biosynthesis. Catalyzes the conversion of methylsulfinylalkyl glucosinolates to hydroxyalkyl glucosinolates.
Sequence Mass (Da): 44943
Sequence Length: 410
EC: 1.14.11.-
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Q8NK92 | MRPLSHLSFFNGLLLGLSALSAATSVVHERREATSSNWVKRARVNPSDKHVVRIGLTQSSLEEAHDLLMDVSNPSSPNYARFYSADEVAAKFAPSTETVNEVQNWLTEKGINASRVAQTQNHGWLVFHATSKEIENLFDTTYYEYHNRKTGKKAIACEQYHVPASVQKHIDYVHPGVNLNPSSGKPSSIRRRAAASKKTKLPARGPRPIQQHDVKGLNVTNCDQLITPECIRALYKIPSARAAPHPNNSLGIFEEGDYYAQEDLDLFFKTFAKDIPQGTHPIPAFIDGAEAPVPVTKAGGESDLDFELAYPIVHPQSITL... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Serine endopeptidase which hydrolyzes a range of fluorogenic peptide substrates containing the basic residues arginine or lysine at the P1 position and prefers paired basic resides. Also hydrolyzes clupeine and salmine, activates plasminogen and converts trypsinogen t... |
Q9ZUC1 | MNAALATTTATTPVLRRETPLLHYCSLTTKSPVYQINRVRFGSCVQTVSKKFLKISASSQSASAAVNVTADASIPKEMKAWVYSDYGGVDVLKLESNIVVPEIKEDQVLIKVVAAALNPVDAKRRQGKFKATDSPLPTVPGYDVAGVVVKVGSAVKDLKEGDEVYANVSEKALEGPKQFGSLAEYTAVEEKLLALKPKNIDFAQAAGLPLAIETADEGLVRTEFSAGKSILVLNGAGGVGSLVIQLAKHVYGASKVAATASTEKLELVRSLGADLAIDYTKENIEDLPDKYDVVFDAIGMCDKAVKVIKEGGKVVALTGA... | Function: Reduces the double bond in short-chain unsaturated carbonyls . Acts preferentially on alpha,beta-unsaturated ketones rather on alpha,beta-unsaturated aldehydes . Has no activity with (E)-2-hexenal and (E)-2-pentenal . Contributes to detoxify stromal reactive carbonyls produced under oxidative stress .
Sequenc... |
Q9V035 | MFGYWGKILRVNLTDGTIKEETFNEEFAKKWLGTRGFGIYFLLKEMDPKVDPFSPENKLIFATGPLTGTSAPTGGRYMVITKSPLTGYIAMANSGGYFGAELKFAGWDAIIIEGKADHPVYLYIHDENVEIRDASKVWGKLVSETEKALKEEVGDKHVQIASIGPAGENKVRFAAVMNNGHRAAGRGGVGAVMGSKNLKAIVVRGHKRVEVADKGKFMEVIREKIEKLKKDPVAGGGLPKYGTAVLVNIINEHGLYPTRNFQTGVFEYAYEQSGEAMAAKYLIRNKPCFACPIGCGRVNYLPSIGETEGPEYESTWALGA... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Catalytic Activity: an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 67520
Sequence Length: 607
EC: 1.2.7.5
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Q51739 | MYGNWGRFIRVNLSTGDIKVEEYDEELAKKWLGSRGLAIYLLLKEMDPTVDPLSPENKLIIAAGPLTGTSAPTGGRYNVVTKSPLTGFITMANSGGYFGAELKFAGYDAIVVEGKAEKPVYIYIKDEHIEIRDASHIWGKKVSETEATIRKEVGSEKVKIASIGPAGENLVKFAAIMNDGHRAAGRGGVGAVMGSKNLKAIAVEGSKTVPIADKQKFMLVVREKVNKLRNDPVAGGGLPKYGTAVLVNIINENGLYPVKNFQTGVYPYAYEQSGEAMAAKYLVRNKPCYACPIGCGRVNRLPTVGETEGPEYESVWALGA... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the oxidation of aldehydes to their corresponding carboxylic acids. May have a pyroglycolytic (saccharolytic) role.
Catalytic Activity: an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequ... |
Q8GZP5 | MANTKDSYHIITMDTKESSIPSLPMKEIPGDYGVPFFGAIKDRYDFHYNQGADEFFRSRMKKYDSTVFRTNVPPGPFNARNSKVVVLVDAVSYPILFDNSQVDKENYFEGTFMSSPSFNGGYKVCGFLGTSDPKHTTLKGLFLSTLTRLHDKFIPIFTTSITSMFTSLEKELSEKGTSYFNPIGDNLSFEFLFRLFCEGKNPIDTSVGPNGPKIVDKWVFLQLAPLISLGLKFVPNFLEDLVLHTFPLPYILVKRDHQKLYNAFYNSMKDILDEAEKLGVKRDEACHNFVFLAGFNSYGGLKVFFPSLIKWIGTSGPSLH... | Function: Cytochrome P450 metabolizing both 13- and 9-hydroperoxides of linoleic and linolenic acids, but with a marked preference for 9-hydroperoxy fatty acids . Has no activity toward 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid (13-HPOT) . Catalyzes not only the synthesis of allene oxide, but also its hydr... |
Q3SYW1 | MSASAVFILDVKGKPLISRNYKGDVAMSEIDHFMPLLMQREEEGALTPLLSHGRVHFLWIKYSNLYLVATTLKNANASLVYSFLYKIVEVFSEYFKELEEESIRDNFVIVYELLDELMDFGFPQTTDSKILQEYITQQGNKLETGKSRVPPTVTNAVSWRSEGIKYKKNEVFIDVIESVNLLVNANGSVLLSEIVGSIKLKVFLSGMPELRLGLNDRVLFELTGRSKNKSVELEDVKFHQCVRLSRFDNDRTISFIPPDGDFELMSYRLSTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANGVEISVPVPSDA... | Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
PT... |
P35602 | MATSAMFILDLKGKTIISRNYRGDIDMTAIDKFIHLLMEKEEEGSAAPVLTYQDTNFVFIKHTNIYLVSACRSNVNVTMILSFLYKCVEVFSEYFKDVEEESVRDNFVVIYELLDEMMDFGFPQTTESRILQEYITQEGQKLISAPRPPMAVTNAVSWRSEGIKYRKNEVFLDVIESVNMLASANGTVLQSEIVGSVKMRVYLTGMPELRLGLNDKVLFEGSGRGKSKSVELEDVKFHQCVRLSRFDTDRTISFIPPDGAFELMSYRLTTVVKPLIWIETSIERHSHSRVSFIIKAKSQFKRRSTANNVEIIIPVPSDAD... | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles (Probable). Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (Probable). Required for many aspects of development a... |
P47795 | MIHSLFLMNGGGAVFLEKHWRSVVSRSVCAYLLEAQLKAGQPENVAPVLATPHHYLVSTHRHGISFVAVIQAEVPPLFVIEFLHRVAETLQDYFGECSEASIKDNVVIVYELLEEMLDNGFPLATESNILKELIKPPTILRSVVNSITGSSNVGDQLPTGQLSNIPWRRVGVKYTNNEAYFDVTEEIDAIIDKSGSTVFAEIQGVIDACIKLTGMPDLTLSFLNPRLLDDVSFHPCVRFKRWESERVLSFIPPVGNFRLMSYHVNSQNLVAIPVYVKHNINFRDDGSTGWFDITIGPKQTMGKVVENILVIIHMPKVVLN... | Function: Component of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP47 is a subunit of the plasma membrane adapter.
PTM: Regulated... |
Q8LEZ8 | MIHFVLLVSRQGKVRLTKWYSPYTQKERSKVIRELSGVILNRGPKLCNFIEWRGYKVVYKRYASLYFCMCIDEADNELEVLEIIHHYVEILDRYFGSVCELDLIFNFHKAYYILDELLIAGELQESSKKTVARIISAQDQLVEVAKEEASSISNIIAQATK | Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting at the trans-Golgi network and early endosomes (TGN/EE). The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo mole... |
P61966 | MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTSKKSVLKAIEQADLLQEEDESPRSVLEEMGLA | Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane ... |
P56377 | MQFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLEIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQEEAETPRSVLEEIGLT | Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane ... |
Q96PC3 | MIHFILLFSRQGKLRLQKWYITLPDKERKKITREIVQIILSRGHRTSSFVDWKELKLVYKRYASLYFCCAIENQDNELLTLEIVHRYVELLDKYFGNVCELDIIFNFEKAYFILDEFIIGGEIQETSKKIAVKAIEDSDMLQEVSTVSQTMGER | Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane ... |
O94669 | MSTIEAIYLVDTNGALLLQLESRGRTSPITLEHIKNELFRYKLRNEEPPFILHNKNFLIFQELEEDVRLCIPTTCDTEPLYIHDIMRRIVDVVKTFFGGFNASKVEKNVCVIVQLLAEMIDYGYATCMEPNALQDIVPLPSFMNKFMAVTGLQTNTPTLARDTVPWRTAKAKYATNEFFIHVLERVSAVYQPNGKLAFGTVKSDMECKCQISGMPLLLLSLRPGTKLGNVRFHQSVNLKRWKQHPDQIEFIPPDGKFTLASFQTDFATQKSLPVVVEAKNKLDGRFEVRIRNTGKKSVENLKILITIPQALKSVTVTEGN... | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole (By similarity... |
P38153 | MYLSFYITDTKNKLIFQYLLGATAPSFKHLWTRVQSTCPQLLEDSSSDDYLDHSMVGRDLEVYKYFSVINKLNYWCLASTSKSKGPLDCFTFLETIDRILLEYFDKDKLSIKKIVNNYDRISLIFNCCVEAGEPNVSDMLYVNKIKEAVPERSDLSKFISSTAHNLQQAVQLPQQRQQQLQQNQISRGSNSLIENEEIVPWRTSRASKHENNELYVDLLETFHVVFEKKKSHLRLLTGSIHGIVDVRSYLNDNPLVAVKLNTMGNDIGIPSLHDCVEINDGVFSPSNITFIPPDGKFRLLEYSVDLSSQVKQSGVRMNSI... | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. Required for ... |
Q92572 | MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEGGLLIGGSDNKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHNILAEMVMGGMVLETNMNEIVTQIDAQNKLEKSEAGLAGAPARAVSAVKNMNLPEIPRNINIGDISIKVPNLPSFK | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with... |
Q1JQA3 | MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLEKSEGGLSAAPARAVSAVKNINLPEMPRNINIGDLNIKVPNLSQFV | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with... |
P59780 | MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLEKSEGGLSAAPARAVSAVKNINLPEIPRNINIGDLNIKVPNLSQFV | Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with... |
Q8VZ37 | MIKAVMMMNTQGKPRLAKFYDYLPVEKQQELIRGVFSVLCSRPENVSNFLEIESLFGPDSRLVYKHYATLYFVLVFDGSENELAMLDLIQVLVETLDKCFSNVCELDIVFNYSKMHAVLDEIVFGGQVLETSSAEVMKAVEEISKLEAASNSISLVPKSVSGWRGR | Function: Part of the AP-3 complex, an adaptor-related complex which seems to be clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. It also ... |
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