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 the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 36544
Sequence Length: 318
Domain: The C-terminal domain could be responsible for the substrate recognition.
Subcellular Location: Secreted
EC: 3.5.1.28
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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.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 31412
Sequence Length: 289
Subcellular Location: Periplasm
EC: 3.5.1.28
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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 | MMYRIRNWLVATLLLLCTPVGAATLSDIQVSNGNQQARITLSFIGDPDYAFSHQSKRTVALDIKQTGVIQGLPLLFSGNNLVKAIRSGTPKDAQTLRLVVDLTENGKTEAVKRQNGSNYTVVFTINADVPPPPPPPPVVAKRVETPAVVAPRVSEPARNPFKTESNRTTGVISSNTVTRPAARATANTGDKIIIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLLNDDPMFKGVLTRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMASWLEQHEKQSELLGGAGDVLANSQSDPYLSQAVLDLQFGHSQRVGYDVATSMISQLQRIGEIHKRRPEHASLGVLRSPDIPSVLVETGFISNNSEERLLASDDYQQQLAEAIYKGLRNYFLAHPMQSAPQGATAQTASTVTTPDRTLPN | 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): 47985
Sequence Length: 445
Subcellular Location: Periplasm
EC: 3.5.1.28
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P44493 | MKTKILFFLFFSTFSFSIFAAPITIAIDPGHGGKDPGAISRNLGIYEKNVTLSIAKELKALLDKDPHFRGVLTRKSDYYISVPERSEIARKFKANYLISIHADSSKSPDRRGASVWVLSNRRANDEMGQWLEDDEKRSELLGGAGKVLSHNNDKYLDQTVLDLQFGHSQRTGYVLGEHILHHFAKVTTLSRSTPQHASLGVLRSPDIPSVLVETGFLSNSEEEKKLNSQTYRRRIAYMIYEGLVAFHSGKTNTLVKDNLVQNIKQNDIKKSGKNNRTSEQNINEDNIKDSGIRHIVKKGESLGSLSNKYHVKVSDIIKLNQLKRKTLWLNESIKIPDNVEIKNKSLTIKENDFHKKQNSLVNNTNKDLKKEKNTQTNNQKNIIPLYHKVTKNQTLYAISREYNIPVNILLSLNPHLKNGKVITGQKIKLREK | 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 peptidoglycan binding.
Subcellular Location: Periplasm
EC: 3.5.1.28
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P26366 | MIYRIKNAVIAALILLCAQAGAASLSDIQVSNGEQQARITLSFIGEPEYAYSQDGKRTVALDIRQTGVIQGLPLQFSGNNLVKTIRAGTPKDAQSLRLLVDLTENGKTEAVKRQNGGNYTVIFTINADVPPPPPPVVAKRVESAPRPTEPARNPFKSSDDRLTGVTSSNTVTRPAARASAGAGDKVVIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLLNNDPMFKGVLTRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNRDATGASVWVLSNRRANSEMANWLEQHEKQSELLGGAGDVLANSQSDPYLSQAVLDLQFGHSQRVGYDVATNVLSQLDGVGSLHKRRPEHASLGVLRSPDIPSILVETGFISNHGEERLLASDRYQQQIADAIYRGLRKYFAAHPIQSAPQGGPGQTASTNQPGAITAAN | 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 | MSGSNTAISRRRLLQGAGAMWLLSVSQVSLAAVSQVVAVRVWPASSYTRVTVESNRQLKYKQFALSNPERVVVDIEDVNLNSVLKGMAAQIRADDPFIKSARVGQFDPQTVRMVFELKQNVKPQLFALAPVAGFKERLVMDLYPANAQDMQDPLLALLEDYNKGDLEKQVPPAQSGPQPGKAGRDRPIVIMLDPGHGGEDSGAVGKYKTREKDVVLQIARRLRSLIEKEGNMKVYMTRNEDIFIPLQVRVAKAQKQRADLFVSIHADAFTSRQPSGSSVFALSTKGATSTAAKYLAQTQNASDLIGGVSKSGDRYVDHTMFDMVQSLTIADSLKFGKAVLNKLGKINKLHKNQVEQAGFAVLKAPDIPSILVETAFISNVEEERKLKTATFQQEVAESILAGIKAYFADGATLARRG | 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 cell-wall glycopeptides.
Sequence Mass (Da): 45634
Sequence Length: 417
Subcellular Location: Periplasm
EC: 3.5.1.28
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Q9K0V3 | MIKLTRRQIIRRTAGTLFALSPIASAVAKTVRAPQFTAARIWPSHTYTRLTLESTAALKYQHFTLDNPGRLVVDIQNANINTVLHGLSQKVMADDPFIRSIRAGQNTPTTVRLVIDLKQPTHAQVFALPPVGGFKNRLVVDLYPHGMDADDPMMALLNGSLNKTLRGSPEADLAQNTTPQPGRGRNGRRPVIMLDPGHGGEDPGAISPGGLQEKHVVLSIARETKNQLEALGYNVFMTRNEDVFIPLGVRVAKGRARRADVFVSIHADAFTSPSARGTGVYMLNTKGATSSAAKFLEQTQNNADAVGGVPTSGNRNVDTALLDMTQTATLRDSRKLGKLVLEELGRLNHLHKGRVDEANFAVLRAPDMPSILVETAFLSNPAEEKLLGSESFRRQCAQSIASGVQRYINTSVLKRG | 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 | MKKYIFMRVLRSLVSIFLVTTLTYTIIYTLVPRKLIFKQDPNYNKIATTADKRDNYENTVFERMGYIEYYDTKELQEKASSMDSSVTVEANATNKAIYEKYINQLGHGWTLGEFTESGQFYATREIPIFERVFHFYANLIDIDHTNKIQDPENPDLKRYLRFENDPAIGWSLVGSGTKHKYLLYFNSQFPFVHQNFVNLNLGDSYPTYANTPVLQVITQGQGQTKTAQVQFPTGKKTSSVNIYSRTYKSPSQADSREVASYGKDDPYTATESNYQYPSMIVSSAITGLIGLVLAYALAVPLGSAMARFKNTWIDSLSTGALTFLLALPTIALVYIVRLIGSSIALPDSFPILGAGDWRSYVLPAVILGLLGAPGTAIWIRRYMIDLQSQDFVRFARAKGLSEKEISNKHIFKNAMVPLVSGIPAAIIGVIGGATLTETVFAFPGMGKMLIDSVKASNNSMVVGLVFIFTCISIFSRLLGDIWMTIIDPRIKLTEKGGK | 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 | MALACLNSLNANAEIFSFDTRNSLNSDTLVLFHSADSTTYSLDFLPQSTQDQLNLAVADNSFSGKRGEVLEILVPSEIDAKRVLLVGIGDAKTLTPGEINALGGNIAAKLETVPQATVRVLTQGLNNAPLFGSELAHGIELRSYRYTQFKASNRVEKNYQIGVDDLSLNQKHHKNLQAVEAGVFLARDLTNAPAGNMYPESFANEARKLKSLGVKVTVLEAKDIERLNLGALAAVGKGSERPPKLVVAHWPGSKEAPIALVGKGITFDSGGYNIKATGTSIARMKSDMAGAATVLGTVKAMAIQKAPVNLVAIMPMAENMVSGHAMIPGDVITTAQGLTVEVLNTDAEGRLVLADGLWYARENYRPSVIIDVATLTGSKVSALGTVYAGLFTDSEPLVQQLTFAGQQVGEKVWRLPLDQAYDDELKSTIADLKNTGKEGSAGASAAAMFLKRFAGDQPWAHLDIAGHALTATDTAVVPAGATGYGVRLLSTWLTQPKAQN | 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 Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 53027
Sequence Length: 500
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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Q6FFD8 | MKFTLQSTAPQSAQHEYLLVLVTEQQLKNTADTYKINTLDTITHTSQFKSGFNEVLTLIGQAETCSYLNLVGLGDLKDLQPAKIAKLAQTIIKLVQTKFKQIHLDISALPIELHYLFALNLTQANYVFDEFKSKKSEAQLEQIHLITAQTGLTTQQLDLIQAIASGQDLARDLGNRPGNICFPEYLADQAKALAHEFPELLKVTILDEQQMADLGMNAFLAVSQGSDRPGRIITLEYNAQLEQAPVVLVGKGVTFDTGGISIKPAQGMDEMKFDMCGAASVLGTIRTLCEARLPIHVVGAVAAAENMPSGQATRPGDIVTTMSGQTVEILNTDAEGRLVLCDTLTYIKRFNPSLVIDIATLTGACVVALGKVVSGLFSPDDALAQELQQAGEQSFDRVWRLPVMDDYQELLDSPFADIANIGGPYGGAITAACFLQRFTRDYRWAHLDIAGTAWLSGTAKGATGRPVPLLVQFLANRVGTND | 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 preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 52317
Sequence Length: 482
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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B0VMG3 | MKFTTYTTFPEQTSNESLWILVDSEQLQSNLNTYQINNLESILTATQFKANFNETLPLFGQLSTQPHSQLLGLGKAAELQAAKLAKLAQTIIKSAQNKFKHIAIDIAALPVEYHYLFALSLTQAAYGYDEFKSTKNEFVLQQVDLISSQTSLDENQLALVHAVQSGQSYARDLGNRPGNICFPEYLAEQALALAAEFPDLLKVTVLNEQQMADLGMYAFLAVSKGSERPGRIVTLEYQAQLEQAPVVLVGKGVTFDTGGISLKPGLGMDEMKFDMCGAASVLGTIRALCEARLPIHVVGAIAAAENMPSGKATRPGDIVTTMSGQTVEILNTDAEGRLVLCDTLTYIKRFNPAVVIDIATLTGACVVALGKVLSGLFSPDDTLAAELQQAGEQSFDRVWRMPVIDDYQELLDSPFADIANIGGPHGGAITAACFLERFTRDYRWAHLDVAGTAWLSGSAKGATGRPVPLLMQFLANRVSTNG | 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 preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 52150
Sequence Length: 482
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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C1F4B7 | MKTTLVSTPLAQLETELLAVFATDTAPAADMANGTQASPQVQLLTRDAALDAAVKTILASGDFKAEANETLLIHAPQGMAARRLLLVGAGKQARFTVHALRKAAGSAVRAARAKNIREATLAIPQSQGLDVTATARALGHGAAVADFDPDFYRSDRKDKSLQSLTLALPEATDANAAEAGLREGIALGESQNLTRTLVNEPGNRLTPTLLGEQAKKMCAEQGLRCQVYSSEKLHELKMGSFWSVTQGSDEPPALIVMEYTPEGAAEGPVLGLVGKGITFDSGGLSLKPADSMEKMKYDMAGAAAMIGAMRAIALLKPRIKVISVICSAENMPSGKAQKPGDVQISMIGKSIEVLNTDAEGRLVLADGLAYAKQLGATHLIDAATLTGAVMVALGGVNAGVFCNDEEAWQHFEAALGQSGEKFWRLPLDEEYREMLRSPIADIKNVGGRYGGASTAAMFLKEFVGDTPWVHLDIAGTAWMDEAKPWMSSGPSGIAMPSIVEWVRSFAR | 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 preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 53618
Sequence Length: 507
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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P45334 | MKYQAKNTALSQATDCIVLGVYENNKFSKSFNEIDQLTQGYLNDLVKSGELTGKLAQTVLLRDLQGLSAKRLLIVGCGKKGELTERQYKQIIQAVLKTLKETNTREVISYLTEIELKDRDLYWNIRFAIETIEHTNYQFDHFKSQKAETSVLESFIFNTDCAQAQQAISHANAISSGIKAARDIANMPPNICNPAYLAEQAKNLAENSTALSLKVVDEEEMAKLGMNAYLAVSKGSENRAYMSVLTFNNAPDKNAKPIVLVGKGLTFDAGGISLKPAADMDEMKYDMCGAASVFGTMKTIAQLNLPLNVIGVLAGCENLPDGNAYRPGDILTTMNGLTVEVLNTDAEGRLVLCDTLTYVERFEPELVIDVATLTGACVVALGQHNSGLVSTDNNLANALLQAATETTDKAWRLPLSEEYQEQLKSPFADLANIGGRWGGAITAGAFLSNFTKKYRWAHLDIAGTAWLQGANKGATGRPVSLLTQFLINQVK | 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 Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 53529
Sequence Length: 491
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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A1WUV1 | MELKTKSGDPARQRTACVVVGVYERRRMSEAARAVDAASDGYLSHLLRRGDLEGEAGQTLLLPDCPGVRTDRVLLVGCGRERDFNERTYRKAVTAAARALEQAGTGEAILFLPELPVRGRDVAWRVAATAEILETTLYRFDTYKSDPRPPRRPLRQATLAVPRRADLRRAQPALTLGQAAGRGANFSRDLGNTPANICTPGYLGEQAEALAQRFDGVRAEILGPAELEEQGLAALLAVARGAEAPPRLVVLHYRGADDDQAPVALVGKGITFDSGGISIKPSASMDEMKYDMSGAAAVFGAVHAAAEAQLPLNLVAVIPATENMPDGRATRPGDIIDSLDGQRIEVLNTDAEGRLVLADGLAYARRLEPSEVVDVATLTGAAIIGLGHHRHAVMGNAPGLVRDLLQAGERAADRGWELPLDEEYDEQLRSPFADVANIGGQPAGTITAGCFLQRFARGLRWAHLDIAGTAWKSGEHKGATGRPVPLLTHFLAGRAGWTL | 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 preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 53334
Sequence Length: 499
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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Q7VGF0 | MKVSISHKNNFKGVSYQAQALLMSKSVFAKSPYAKLCKSFGFEGEGKFFLQEQALLLVCVEELGLDSIREAGASIARHFRTLPYKNVNVALNGKLDDSKAYALLLGALLGVYECVSYKTKTPPLHLKEIILLDEKNEVASESVLKKVHIVAQSVNEVREIINTIPQVATPKYLAKYAKELSKEVGNLECKILDEEALQKEKMGAFLAVNRASCNPPRLIHLSYKPKGAKKRIVLVGKGLTYDCGGLSLKPADFMVTMKADKSGGCAVMGIIKAIAQLGANIEVHSIIGAAENMIGGNAYKPDDVLYSREGKSIEVRNTDAEGRLVLVDCLSYAQDLKPDILIDFATLTGACVVALGEFTSGIMGHNDRLKAQFEKCALESGELMATLPFNRHLKKLIESKIADVCNVGSSRYGGAISAGLFLSEFIREEFKQKWLHIDIAGPAYVEKEWDINPSGASGAGVRAGIEFILAQGKA | 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 preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 51523
Sequence Length: 474
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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O25294 | MLKIKLEKTTFENAKAECSLVFIINKDFSHAWVKNKELLETFKYEGEGVFLDQENKILYAGVKEDDVHLLRESACLAVRTLKKLAFKSVKVGVYTCGAHSKDNALLENLKALFLGLKLGLYEYDTFKSNKKESVLKEAIVALELHKPCEKTCANSLEKSAKEALKYAEIMTESLNIVKDLVNTPPMIGTPVYMAEVAQKVAKENHLEIHVHDEKFLEEKKMNAFLAVNKASLSVNPPRLIHLVYKPKKAKKKIALVGKGLTYDCGGLSLKPADYMVTMKADKGGGSAVIGLLNALAKLGVEAEVHGIIGATENMIGPAAYKPDDILISKEGKSIEVRNTDAEGRLVLADCLSYAQDLNPDVIVDFATLTGACVVGLGEFTSAIMGHNEELKNLFETSGLESGELLAKLPFNRHLKKLIESKIADVCNISSSRYGGAITAGLFLNEFIRDEFKDKWLHIDIAGPAYVEKEWDVNSFGASGAGVRACTAFVEELLKKA | 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 Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Sequence Mass (Da): 54433
Sequence Length: 496
Subcellular Location: Cytoplasm
EC: 3.4.11.1
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Q9H4A4 | MASGEHSPGSGAARRPLHSAQAVDVASASNFRAFELLHLHLDLRAEFGPPGPGAGSRGLSGTAVLDLRCLEPEGAAELRLDSHPCLEVTAAALRRERPGSEEPPAEPVSFYTQPFSHYGQALCVSFPQPCRAAERLQVLLTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKYKYSALIEVPDGFTAVMSASTWEKRGPNKFFFQMCQPIPSYLIALAIGDLVSAEVGPRSRVWAEPCLIDAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMDITGEENPLNKLRVKIEPGVDPDDTYNETPYEKGFCFVSYLAHLVGDQDQFDSFLKAYVHEFKFRSILADDFLDFYLEYFPELKKKRVDIIPGFEFDRWLNTPGWPPYLPDLSPGDSLMKPAEELAQLWAAEELDMKAIEAVAISPWKTYQLVYFLDKILQKSPLPPGNVKKLGDTYPSISNARNAELRLRWGQIVLKNDHQEDFWKVKEFLHNQGKQKYTLPLYHAMMGGSEVAQTLAKETFASTASQLHSNVVNYVQQIVAPKGS | 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 (LTB-4) (By similarity).
Catalytic Activity: Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.
Sequence Mass (Da): 72596
Sequence Length: 650
Subcellular Location: Secreted
EC: 3.4.11.6
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O09175 | MESSGPSSCHSAARRPLHSAQAVDVASASSFRAFEILHLHLDLRAEFGPPGPGPGSRGLNGKATLELRCLLPEGASELRLDSHSCLEVMAATLLRGQPGDQQQLTEPVPFHTQPFSHYGQALCVVFPKPCCAAERFRLELTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKCTYSALVEVPDGFTAVMSASTWERRGPNKFFFQMSQPIPSYLIALAIGDLASAEVGPRSRVWAEPCLIEAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMDVSGEENPLNKLRVKIEPGVDPDDTYNETPYEKGYCFVSYLAHLVGDQEQFDKFLKAYVDEFKFQSILAEDFLEFYLEYFPELKKKGVDSIPGFEFNRWLNTPGWPPYLPDLSPGDSLMKPAEELAELWAASEPDMQAIEAVAISTWKTYQLVYFLDKILQKSPLPPGNVKKLGETYPKISNAQNAELRLRWGQIILKNDHQEEFWKVKDFLQSQGKQKYTLPLYHAMMGGSEMARTLAKETFSATASQLHSNVVNYVQQILAPKGS | 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 (LTB-4).
Catalytic Activity: Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.
Sequence Mass (Da): 72620
Sequence Length: 650
Subcellular Location: Secreted
EC: 3.4.11.6
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P00811 | MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNALQ | 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 | MKRLLAFCLLFFAALGQAKVPPPARSAADAEIQRAVAAFMQQYQVPGVAVGITVDGAERYYNYGVSSRKTQAKVGANTLFEVGSVSKTFTATLASYAQVNQQLSLADHPGKYLPEMKGHDFDKVTLLNLGTHTAGGFPMQVPTQVKTDQQLTAYFQSWHPQYPAGTKRTYANPGIGMLGVIAAKSMRMPFQKAMTGVLLPKLGLTNTYLTVPPAKMAFYAQGYDDKGQPVRMSPGALWEPTYGIKTTARDLLRFVEINLDQVKVEPKLKRAIDGTHVGYYRLGEMTQGLVWEQLPYPASETSLQANSSQKVIFESNAVAALTPPRPPQANVLINKTGSTRGFGAYVAFNPARKIGIVLLMNRSVPMDGRIKLAHTILDTAGGMAK | 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 | MKKSLSATLISALLAFSAPGFSAADNVAAVVDSTIKPLMAQQDIPGMAVAVSVKGKPYYFNYGFADVQAKQPVTENTLFELGSVSKTFTGVLGAVSVAKKEMTLNDPAEKYQPELALPQWKGITLLDLATYTAGGLPLQVPDAVKSRADLLHFYQQWQPSRKPGDMRLYANSSIGLFGALTANAAGMPYEQLLTARILAPLGLSHTFITVPESAQSQYAYGYKNKKPVRVSPGQLDAESYGVKSASKDMLRWAEMNMEPSRAGNADLEMAMYLAQTRYYKTAAINQGLGWEMYDWPQQKDMIINGVTNEVALQPHPVTDNQVQPYNRASWVHKTGATTGFGAYVAFIPEKQVAIVILANKNYPNTERVKAAQAILSALE | 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 | MDNSMKNIFRQGRLFIALSLAMTSISAFALTQQEVDDIIKPLMKQEQIPGMSVAISVNGKQAIYHYGVQSKQTQIPVSDRTLYEIGSLSKTFTATLATYAQIQGKLDFSQSVSHYLPELKGSAFDNVSVMNLATHTSGLSLFVPSDIKTNDQLMAYYQKWLPDNEVGQYRSYSNLGVGLLGIVTAKQLNMPFSQAMEKLMLPSLGLKHTYIHVPKSQEKYYAQGYNKQNQPVRLNLEILGPEAYGLKSNAKDLIRYLEINMQSIKVAKTWQEAIENTHTGVYLTDSFVQDMMWESYPWPVSLSQLLQGNRDDMALKPQKVELIKPAMAPEVRAYYNKTGSSNGFATYAIFIPEEKIAIVMLSNKWIPIPQRITATYQLLEKIER | 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 | MRDTRFPCLCGIAASTLLFATTPAIAGEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRVTPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR | 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 | ATDIRQVVDSTVEPLMQQQDIAGLSVAVIQNGKAQYFNYGVANKDSKQPITENTLFEIGSVSKTFTATLAGYALANGKLKLSDPASQYLPALRGDKFDHISLLNLGTYTAGGLPLQFPEESDNTGKMISYYQHWKPAFAPGTQRLYSNPSIGLFGHLAAQSLGQPFEKLMEQTVLPKLGLKHTFISVPETQMSLYAQGYDKAGKPVRVSPGALDAEAYGIKTSTSDLIHYVEVNMHPAKLEKPLQQAIAATHTGYYTVDGMTQGLGWEMYPYPIKVDALVEGNSTQMAMEPHKVNWLTPPQAAPLDTLVNKTGSTGGFGAYVAYVPSKGLGVVILANKNYPNAERVKAAHAILSAMDQ | 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 | MKLFTSTLTAKKSSTHKPLISLALSVLISTLLISETAQAADANDRLEQEVDKQAKQLMAQYQIPGMAFGIIVDGKSHFYNYGLADKQRNQPVSEDTIFELGSVSKTFAATLASYSELNGTLSLDDTADKYIPYLKNSAIGNTKLISLVTYSAGGYHYRCLKTLENNKELLQYYKSWHPDFPVNSKRLYSNASIGLFGYISALSMHSDYTKLIENTVLPSLKMTNTFVDVPANKMEDYAFGYNAAGEPIRVNPGMLDAEAYGIKSTSADMTRFMAANMGLVTVDSQMQQALDNNRKGYYRTKSFTQGLAWEMYPLPTTLQQLVEGNSTETILQPQPIQLNEPPTPVLNDVWVNKTGATNGFGAYIAYMPAKKTGMFILANKNYPNTERVKAAYTILDSVMNN | 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 | MTKMNRCAALIAALILPTAHAAQQQDIDAVIQPLMKKYGVPGMAIAVSVDGKQQIYPYGVASKQTGKPITEQTLFEVGSLSKTFTATLAVYAQQQSKLSFKDPASHYLPDVRGSAFDGVSLLNLATHTSGLPLFVPDDVTNNAQLMAYYRAWQPKHPAGSYRVYSNLGIGMLGMIAAKSLDQPFIQAMEQGMLPALGMSHTYVQVPAAQMANYAQGYSKDDKPVRVNPGPLDAESYGIKSNARDLIRYLDANLQQVKVASVARRWPRRTSVITSAGAFTQDLMWENYPYPVKLSRLIEGNNAGMIMNGTPATAITPPQPELRAGWYNKTGSTGGFSTYAVFIPAKNIAVEMLANKWFPNDDRVEAAYHIIQALEKR | 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 | MPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFHLETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQITGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKSTE | 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 | MPLFKLTGQGKQIDDAMRSFAEKVFASEVKDEGGRHEISPFDVDEICPISLREMQAHIFHMENLSMSMDGRRKRRFQGRKTVNLSIPQSETSSTKLSHIEEFISSSPTYESVPDFQRVQITGDYASGVTVEDFEVVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEALVAIESFYPVFTPPPKKGEDPFRREDLPANLGYHLKMKGGVIYIYPDEAAASRDEPKPYPYPNLDDFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKNLTLKELFAQLNMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVDAKYQHAEPRLSIYGRSPDEWSKLSSWFVGNRIYCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQTHPDLSVFLKHITGFDSVDDESKHSGHMFSSKSPKPEEWTMENNPSYTYYAYYMYANIMVLNCLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKSTE | 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 | MSNRRKNSLYPTLSAELSALMRTGWADTERHDLAPAEQAPYAALRRAALSARFPGERLVVPSGNLKVRSNDDTYPFRSYSGYVHMTGDQARDGALVLEPRPDGGHDAYCYQLPRDSRDDDEFWTGAHAELWTGRRRSLAESERVLGLPCRDVRTAAADLAAVSEVRTRIVRGIDPALEAAVTTDEERDAELEDALSDLRLVKDAWELGELRKAVDSTVRGFTDVVGELSRAVASSERWLEGTFFRRARLEGNAVGYGTICAAGEHATIMHWTDNDGPVRPGDLLLLDAGVETRSLYTADVTRTLPISGTFTPLQREVYDAVYEAQEAGIATVKPGAAYRDFHEAAQRHLAARLVEWGFIEGPAERAYELGLQRRFTMAGTGHMLGLDVHDCARARTEEYVEGVLEPGMCLTVEPGLYFQADDLTVPEEWRGIGVRIEDDLVVTEDGHENLSAGLPRSADEVEAWMARFAG | 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 | MTSDSTVDKILAGKYPAKQHAENVVERLLHVHPDLTDGVIYLESQRSKLYENSDQEVPFRQRRYFYYLSGCDLADSYLTYSIRDRKLTLFIPPIDPASVLWSGLPLSNSEALEKYDVDEVLPTSATALPTTSYSSLMFVIESQTSRTFHLQNTESLEPAIERARAIKDEYEVALIKKANRISALAHHSCLRAIKSAGNEREIEAVFTKECIANGAPKQAYSGIFGSGRSASTLHYVHNNQPLAGKLNLLLDAGAEYNNYASDITRTFPISGQFTKESREVYDIVLDMQKQCLAASKAGAVWDDIHILAHKVAIQGLLKIGVLRNGSVDEILSNRTSTAFLPHGLGHYLGMDTHDCGGNPNYADPDPMFKYLRKRGPLPAGAVITVEPGIYFCEFIIKPYLEDEKHAKYIDKDVLNRYWDVGGVRIEDNILITEGGYENLTNVAKEVDDMLKFING | 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 Length: 455
EC: 3.4.11.9
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C4JY72 | MSGVAEPDCYLTYDITSDTLTLYVPDFDLRRAIWMGPTLGLAEARERYNIDQAKYRSTLEQDILDWASRRAIGSVIYVIHDNQKPVVPFPYLKFNHEDLIPAMDTCREIKDGHEIGLIRRANEISTSAHTEILRNISGMRNEAEIQGKFLDSCVSLGAKNQSYEIIAASGENAAVLHYTRNDEPLKGRQLVCLDAGAEWNCYASDVTRTFPMQPRWPSAEAFSVYSVVQRMQEECIKRISEGVRYLDLHILAHKIAIEELLRLGIFRGGSIAEILKSGASLVFFPHGLGHHVGLEVHDVSGRSLMALEEQEYQGLPLRGCRAPCTLSAPHLRAGMVVTVEPGIYFSRLALDDAKQKPLSKYIDMQLVAEYIPVGGVRIEDDVLVTRDGWENLTSAPKGRAMLDIIGEGARLRA | 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 Length: 413
EC: 3.4.11.9
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Q9AR04 | MSLTEEKPIRPIANFPPSIWGDQFLIYEKQVEQGVEQIVNDLKKEVRQLLKEALDIPMKHANLLKLIDEIQRLGIPYHFEREIDHALQCIYETYGDNWNGDRSSLWFRLMRKQGYYVTCDVFNNYKDKNGAFKQSLANDVEGLLELYEATSMRVPGEIILEDALGFTRSRLSIMTKDAFSTNPALFTEIQRALKQPLWKRLPRIEAAQYIPFYQQQDSHNKTLLKLAKLEFNLLQSLHKEELSHVCKWWKAFDIKKNAPCLRDRIVECYFWGLGSGYEPQYSRARVFFTKAVAVITLIDDTYDAYGTYEELKIFTEAVERWSITCLDTLPEYMKPIYKLFMDTYTEMEEFLAKEGRTDLFNCGKEFVKEFVRNLMVEAKWANEGHIPTTEEHDPVVIITGGANLLTTTCYLGMSDIFTKESVEWAVSAPPLFRYSGILGRRLNDLMTHKAEQERKHSSSSLESYMKEYNVNEEYAQTLIYKEVEDVWKDINREYLTTKNIPRPLLMAVIYLCQFLEVQYAGKDNFTRMGDEYKHLIKSLLVYPMSI | 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 = (+)-amorpha-4,11-diene + diphosphate
Sequence Mass (Da): 63933
Sequence Length: 546
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Sesquiterpene biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.2.3.24
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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 biosynthesis.
EC: 2.4.-.-
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Q46633 | MAIYWIVSYSILVFCFFELAMINQASEAKTKILINYFFLIGVFALILFAGIRGPDSGMDDSQYVGFFHDFSRQTGMTGYQAVANIYRYENFFMVLAWVASCFTHESYFFLLFISFIAVSTNAWVYKKYSPLILCSLCLYSAHLFINKDMNQIRFGLCSAFAIAFICSLVARNYLLALLFIVLSTQSHSTGYTIVMIIPFFFIRERKYLPLVLVIASIPLGIIGGKKLFLDSLGIVPVLGERAASYSGTNFDTTSPVFGLANLKNIAFIGAFTLYYFRKGIMKEDRFVYILLIAYSIGAAVRITFSDFSIFGGRVGNLFLHTEPLLFAFLMLRIRNLLLNFFMLFSITTYYLAYNTILSAQSIMGYSVAPLFRIFS | 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 | MYKLLILIDGISNSGGTDRVASTLSSLLSNHNYDVTLYSLNSGEPYYPVDNKVSIRQPKSSMRLFKLFEFIRYAKNTRPDGVMIISMGKLSVQALLLSKLFRVKSRLICCDHVSIETFSAAVRKLKVFCYGLAEKVVVLTQHDKNYLTSAFSLKNVYVVGNISPFHHENSLNRFDDVFARKQNRVLAVGRLTYQKNFGRLLDIWKNVHKQGWKLLIVGDGEEKAELLEKIKKYHLEESAEIVSPSKKISEYYRSSGVIAMTSRYEGLPMVLIEAKNYALPAIAFDCKTGPAEIIKDDGYVVDYQSNELFTAQLNQLIASEQLRKNFAQAAWQNSADYGPELILKKWNDILN | 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 | MKRRELIRTAFSTIVATAALSSVSARARSEDLHGLTLKKVPPDAIPKNDVPIFSPDDVFTMPEQFWRDFKGKLYIGKAGTDPTLPQNLIDVFVKNANGGTALLSQPIDLNSETLKTFVAAKGALWSASEYSMALHNDNDEQIFYVPDVKNNGVSEFSRRLSQPGGYQLIGEISSFASLRQTRPLFSGAKVRLKGWHDGTEVGGGAFVGEMTPSEDDGGYIASSGQDFHWRRVSDDMNRITLFDFGAVADGKKDCLPAVMAMYHWAQNNNQKLSIQFPAGRFFISSFDISAKYIRFLRLAGAPVNFGYFPATTLVSDGKSEFLFKVNARWVELSNISFEGQIEHSPNGQGFFHNICPAGQYFRGSCLRFTGVGGVSLSLIDTLDCKIDQWYASKCTGDVIRGSWSFTKKGNWDHNTAIELSNFNVQHCRQGKVLNLPRCTQSIIHNGWIEHSEFPGDLSNGQWIVDALSLEGCKNPLIAHCSRLNMRQTNLQSGSWIDNSLANDEWLSSFERGSTRVESYGIAVDGSMKYNYLTSRFRIENHSSQEKWYELGNIHTPDVGDSWEIEVFGQSQFSNGSGTKALMSVTDDRHTGGKAIINLQRKIHGFEASWSVEGSSPINDVVYTTSNDSDTRVFVKLAQWLGSAGVMIKTTAKDRFVTGHCARFDSRMVHSEPPKGEKVHSAVRRFSLHNGLAGIGANEQGDLLVESRHIDAAKVETSRAEGYISLVINGQQVAVPYFALKQNS | 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 | MREIEFTFKGLLIRLSLALSDLIFFNIALALAIVLINGFPGEILTGIPQHELDLKIATHILLSVICVGWFWVRLRHYTYRKPFWFELKEVFRTILIFSIVDLSVSALSKWELSRWIWILTWLLSMAMVPFGRACVKRLLNRKKLWKKQSIIIGSGKNAQEAWQALQSEEMMGFDVIAFYDVDGSQTALELFGVPVLKEEQQLWSLVDSDTQFIVAVEYEQSQSRDRWLKNLATHNCRSVSVIPSLRGVPLYGTDMAYIFSHEVMILRVSNNLAKHSSRFLKRTFDLVGALSIITLLLPALVILIFMVSRDGGAPIYGHERVGRDGRKFKCLKFRSMVVNSKEVLEEVLRTDPVARAEWDEDFKLKNDPRITRIGHFIRKTSLDELPQLWNVVRGEMSLVGPRPVIEAELERYAGDVDYYFMAKPGMTGLWQVSGRNDVSYETRVYFDSWYVKNWSLWNDIAILFKTIGVVLKRDGAY | 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): 55074
Sequence Length: 477
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
Subcellular Location: Cell membrane
EC: 2.-.-.-
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Q8VYB5 | MGSSFETIDIATSARRIGVDNRISLKFYFRIADNILKQANIFRAEKNVIDLYVMLLRFSSLALETIPSHRDYRTSLKSNKEYLRMRLLDVLTELEKLKPVVQQRIDELYPKLKPRYNVQAHPANGSLGWSSAVKPSFNSYDHAKVRNPPGHNSGYMGSRGQQFLNAAPLEERFRKMSVNFRPNEETLSKHSILGPGGLSAQWQPPKYDTKVQYPSNIDFSPVVIPSFQQLVDSKPMITNGSNDEPEKPIVEPSVASNEKIQKNYTEELSSMISFEEPESVNENNLIRQPSPPPVLAEVQDLVPALCPEVREPECMIENSLPDESLRSESPLELHIATSMMDTFMRLAKSNTKKNLETCGILAGSLKNRKFYITALIIPKQESTSDSCQATNEEEIFEVQDKQSLFPLGWIHTHPTQSCFMSSIDVHTHYSYQIMLPEAVAIVMAPQDSSRNHGIFRLTTPGGMTVIRNCDRRGFHAHSSPEDGGPIYNTCKEVYMNPNLKFDVIDLR | 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: Membrane
EC: 3.4.19.-
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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 | MKIDLNKVAREIEVDNRIPLRNYYRIADNLLRQASIYREEKNVVDLYIMLLRYSSLISETIPFHRDYQASLPQERLGSRKRLRAVINELESLKPEFNQLVDKLNRVEDESRQDGSDLPVVSYSSDAVEWPPAHKASYSRPDINKPLPTSQPSWTYNNNLTSSSNRTQIDQQFQKLSFDFLPPNQATLSRHSFLGPNGLKRQMVAPKSEIKVQYPSNTDWGSADNSGLIEAGPSSSSASLNGDSQEVSTLNSVLSLDDGRWQRHSEAVNSQFISDATEDPFQFVGMKQPSPPPVLAQVHQELAQICPSKVADPRPGPAIPSLEGKEGSNSYQHLHVPVRIMDDFLRLARSNTERNLETCGVLAGSLKNRVFHITTLIIPKQESTSDSCQTLNEEEIFEVQDRLSLFPLGWIHTHPTQTCFMSSVDLHTHYSYQIMLPEAVAIVMAPTDESTPHGIFHLSDPSGVSVIRNCQQRGFHPHEESEDGNPIYEHCSHVFLNAKLKYEVLDLR | 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 vacuole and the vacuolar trafficking of endocytosed cargo), endocytosis and vacuole biogenesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57268
Sequence Length: 507
Domain: The JAMM motif is essential for the protease activity.
Subcellular Location: Membrane
EC: 3.4.19.-
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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 | MKILLVGNHTCGNRGDGAILRGIIDSLHLERTDLDIDIISRFPTSSSYLLQQNILPDELFLETKKSNSLVAKVKRRLMPKIMMAHIRGSGFFKNLAVPEYLQQFTDKLKQYDAVIQVGGSFFVDLYGPLQFEHSLCALLAKKPVYMIGHSVGPFQKERFNQIANFVFSRVNSLVLRESVSLEMMEKAGITTQKVIPGADTAFLVRTRTLDAPGHNLIHWQNQIAASKTIAITVRELAPFDKRLGVTQQEYEMAFGKVINAMIERGYQVVALSTCTGIDSYHRDDRMVAITLGDYVQQKDKYRVVMDEFNDLELGILLAGCHLTIGTRLHSAIISMNFGTPAVAINYEHKSLGVMKQLGLPEMASDVQSLMDGSIIAKVNGVLDNYEEIEQQVARAVEQERILGNKITADVLKSIG | 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 | MSSYIVHRQNITRKEQSTIYWVNVLLSMLTGLLLVAIAWPISWFYHLPQLGGLIMLTSLNFLVLGSLSQYQAHFIKAKRMILLAKIEMVTKFLAFAFTVILLYYSPLGVSAVILGLFANAALRIGCMIWFGDKSWRPTFEFDQGTFYSSLKYGIYQLGSQTINQLRTQADSLIVGKVMGAELLGVYSLAKELILQPLKLVTPVINRLALPRFAEKQHDPVRLQQLFLKGTFVIMLFSAIMYLAIGILSPVIVRVLYGPAHEAVGQLIPLMLLFGMLRPMGGLTGAISQANGRTNVEFYWNVVASIIVVLVLASVWIWPQVEYVALTLSISQVLISVFAHPFFIKPVIGIRFLPYARQWISVSAVFVGIIALVSHYNLFIMPEWFSRWL | 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 | MYCDKGASSLANGLLPNVSGDITAKDNILDALDSSAEEHFWGRYIDGFEGQIFPQIPVSVHEAHLTGRARYEIILGNSMVTTLYTVSSIIRTGWALLVSQYTESQDVVIVSSLELPSQAMGGTILFPIRFRIRQDGRTEELLQSAKKHADKVLSSQKHDFPHTKDFVDPFSNSILLICTESQPSHSLEELLTELSASKKCALVLRCELLEDKISISAMFDPQVVRPRQTRRILDQLGHILKQISGSDMLVGDLDFLSPEDRQEIGRWNSRSALSDECIHALISKQAQQNPAAMAVNAHDGNFTYGELESYATRLAAHLIHIGVKPGNFVPTLFEKSKWTQVGILAILKAGAAFVMLDPSHPPARNQLICRKANACFALASAPCEPVLSMAVPHVITLSHSFMEELGRLQPPHEQKSPCLDPRAVAYLLFTSGSTGQPKGAILEHRSFAAASRGVVAMTHMSSTTRTLQHSSYSFGAAIVEIIATLVAGGCVVVLSDTERLSNVAASMVAYSVNWAFMTPSFARTVNPADVPCLRVLATGGEGVTSDIVETWASFVSLYTVYGSAEQSSIAAMAGPLATHQRGNSANVGSPFAGCYAWIVQPDRPEKLAPVGCVGELVLEGALVARGYIDEVESTAAAFPKGFSWRCLFPLHQEGSTRFYRTGDLVRYAVDGTLEFVARRNGYIKLRGQRIELGEIESQLKAVARQPYEFCVEVVVPKGETADKAVLVAFVALGSAYTDNEICESAISSPEQFDQGILVDVLGHVEERLAETLPAFMIPRFFFPLQHFPVTSSGKIARKILREQAAQMSVLQLAELSLGSVEKKELQSDMERYLRSVWVQLLGVPEDFIGANDSFFRVGGDSLKAIKLFQRLRRDGYNLNVTSIVAAPTLSQMARNCSLLD | 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), dehydroalanine, L-alanine which are common for all 3 AM-toxins I to III. The fourth precursor is L-alpha-amino-methoxyphenyl-valeric acid (L-Amv) for AM-toxin I, L-alpha-amino-phenyl-valeric acid (L-Apv) for AM-toxin II, and L-alpha-amino-hydroxyphenyl-valeric acid (L-Ahv) for AM-toxin III (Probable). AM-toxins have two target sites for affecting susceptible apple cells; they cause invagination of the plasma membrane and electrolyte loss and chloroplast disorganization . The non-ribosomal peptide synthetase AMT1 contains 4 catalytic modules and is responsible for activation of each residue in AM-toxin . The aldo-keto reductase AMT2 catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV), one of the precursor residues incorporated by AMT1 during AM-toxin biosynthesis, by reduction of its ketone to an alcohol . The cytochrome P450 monooxygenase AMT3 and the thioesterase AMT4 are also important for AM-toxin production, but their exact function within the AM-toxin biosynthesis are not known yet . Up to 21 proteins (including AMT1 to AMT4) are predicted to be involved in AM-toxin biosynthesis since their expression ishighly up-regulated in AM-toxin-producing cultures .
Sequence Mass (Da): 98347
Sequence Length: 900
Domain: NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase (By similarity). AMT10 is composed of only one module and misses a condensation (C) domain (Probable).
Pathway: Mycotoxin biosynthesis.
EC: 6.3.2.-
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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 | MRLLPSSCAGALSLLCSLAIAAPTELKARDLSSFIASERAIALQGALNNIGPDGSAVPGAGAGFVVASPSKANPDYFYTWSRDSALTLKMIIDEFILGNTTLQTIIEQYIHAQAVLQTVSNPSGTFLPDGVGLGEPKFMVDGTRFNGPWGRPQRDGPALRAIALMTYSNWLIKNGQFAEAKTKIWPIIANDLSYVGQYWNQSGFDLWEETYASSFFTIQNQHRALVEGAQLAHDLGVTCTGCDQAPEVLCFLQSFWNGKYIVSNINVNNGRTGLDGNSILGAISTFDIDAYCDSPTLQPCHSQSLANFKVLTDTFRNLYTINAGIPEGQGVAVGRYAEDVYMGGNPWYLITTAAAEFLYDAVAQWKARHVLTVDETSLAFFKDIYPEVTVREYKSGNANSPFAQIMDAVTAYADSYVAIAEKYIPSNGSLSEQFNRDTGTPLSAIDLTWSYAAFITMSQRRAGQYPSSWGSRNALPPPTTCSASSTPGIYTPATAAGAPNVTSSCQVSITFNINATTYYGENLYVIGNSSDLGAWNIADAYPLSASAYTQDRPLWSAAIPLNAGEVISYQYVRQEDCDQPYIYETVNRTLTVPACGGAAVTTDDAWMGPVGSSGNC | 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 | MKLLSKVFVTALGLTSIVNAAPTSSSSAEEAQKTVPVELSIGVKQLPNIHNDSAVDANAVAKGYSLVNVSLTARGLTGILKLKEATNIYGYDFEYLNLSVEYQSDTRLNVHIEPTDLTDVFVLPEELVVKPKLEGDAKTFNFENSDLVFEYDEEDFGFEVLRSSTREVLFSTKGNPLVFSNQFIQFNTTLPKGHSITGLGESIHGSLNEPGVVKTLYANDIADPIDGNIYGVHPVYYDQRYNTNTTHAVYWRTSAIQEVVVGETSLTWRALSGVIDLYFFSGPDPKDVIQQYVSEIGLPAMQPYWALGYHQCRWGYDTVESLETVVENFKKFDIPLETIWSDIDYMDGYKDFTNDPYRFPTDKFRKFLDDLHNNSQHYVPIFDAAIYVPNPNNATDNDYEPFHLGNESDVFLKNPDGSLYIGAVWPGYTVFPDFLANNTQEYWNKMFKDWYERIPFDGIWTDMNEVSSFCVGSCGTGRYFDNPVHPPFEVGYSGSDYPLGFDKSNASEWKSISEAAAATKTTTTTSSSTSTSIDGKNTLAPGKGNINYPPYAINNNQGDHDLATHAISPNATHADGTVEYDIHNIYGLIQERAIYEALLEIHPNKRPFIIGRSSFAGSGKYMGHWGGDNYADYYMMYFSIPQALSMGLSGIPFFGVDACGFNGNTDMELCSRWMQLASFFPFYRNHNVLGAIPQEPYVWEGVMNATKTSINVRYSLLPYYYTLLHESHVTGIPIMRAFNWQFPYSKELAGVDTQFFVGDALLVTPVLEPGVNHTKGVFPGENAVYYDFYTHKKQKFTAGKNETLAAPLGHIPLHIKGGNIIPTQEPGYTTTESRKNPFGLLVALDAEGTASGKLYLDDGESVDVEEALYVDFVASKNKLVASVFGEYEVRQPLANVTILGVDSEPKKVLFNNETVSHNYENGAVYLTDLEKFTKEGAFAEEFSIQW | 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: Secreted
EC: 3.2.1.3
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P29761 | MSRKLIKYLPLLVLASSVLSGCSNNVSSIKIDRFNNISAVNGPGEEDTWASAQKQGVGTANNYVSKVWFTLANGAISEVYYPTIDTADVKEIKFIVTDGKSFVSDETKDTISKVEKFTDKSLGYKLVNTDKKGRYRITKEIFTDVKRNSLIMKAKFEALEGSIHDYKLYLAYDPHIKNQGSYNEGYVIKANNNEMLMAKRDNVYTALSSNIGWKGYSIGYYKVNDIMTDLDENKQMTKHYDSARGNIIEGAEIDLKKNSQFEIVLSFGNSEDEAVKASIETLSENYDSLKSAYIDEWEKYCNSLNNFNGKANSLYYNSMMILKASEDKTNKGAYIASLSIPWGDGQGDDNTGGYHLVWSRDLYHVANAFIAAGDVDSANRSLDYLAKVVKDNGMIPQNTWISGKPYWTGIQLDEQADPIILSYRLRRYDLYDSLVKPLADFIIKMGPKTGQERWEEIGGYSPATMAAEVAGLTCAAYIAEQNKDYESAQKYQEKADNWQKLIDNLTYTEHGPLENGQYYIRIAGLPDPNADFTISIANGGGVYDQKEIVDPSFLELVRLGVKSPDDPKILNTLRVVDSTIKVDTPKGPSWYRYNHDGYGEPSKTELYHGAGKGRLWPLLTGERGMYEIAAGKDATPYLKAMENFANEGGIISEQVWEDTGLPTDSASPLNWAHAEYVVLFPSNIEHKVLDMPDIVYKRYVAK | 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 beta-D-glucose.
Location Topology: Lipid-anchor
Sequence Mass (Da): 78658
Sequence Length: 702
Subcellular Location: Cell membrane
EC: 3.2.1.3
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D8Q9M3 | MGLASTVSLALLGLCSLARAQTSAADAYVSAESPIAQAGILANIGPSGSKSHGAASGVIIASPSTSNPDYLYTWTRDAALVSRALVDEFIEGESSLQSVIDSYVSSQQKLQRVDNPSGSYTSGGLGEPKFNIDLTAFTGAWGRPQRDGPALRAITLITYGNHLLSSGNTSYVTDTIWPVVKADLDYVVSYWNQTGFDLWEEVSSSSFFTTAEQHTALRLGATFATAVGASASTYLTQADNVLCFLQSYWNSNGGYATANTGGGRSGIDANTVLTSIHTFDIEAGCDSVTFQPCSDRALSNLKVYVDSFRGLYSINPTGATDPILTGRYKEDVYYNGNPWYLTTFAVAEQLYDALNTWDKLGSLDVTSTSLAFFKQFDSSITAGTYASSTSEYATLTSAIRNWADGFLEVLADFTPADGGLTEQIDKSSGNPTSAADLTWSYASAITAFKARGGAIPASWGAAGLTVPATCSTGGGGGSGGDTVAVTLNVQATTVYGENIYVTGSVNQLANWSPDNAIALNADNYPTWSVTVNLPANTQIEYKYIRKNNGQVTWESDPNRSITTSASGSFTQNDTWR | 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 | MTVTISFEPYVGSSVDALSIPLYLRCQLVFKLSKPLAAVPLLESGVNRLVQALPFLSGEFTAVPASDGGKEILLVRPVLNFELSRILKIKYHETSLRHVCKQMNRPSSQGGDLPHEPYMPYPRLPDPSRPQPIVGFQVNVHTDGIILSVATHHCSFDATGMGSIVQNLAACCRSPPSDEPDLTTSPAQEAEARKVLSQVRETPFDPKMFPEYRPLDSMLSYYKGVQSALQGRQTTIVNRCFTIAADKINALKRRCNQLIPEMVKKYGLSTEDAIGSAWVSSNDVVAALLWTCINRARYPEIRERSVHQLPPDLLHATSSLGVPVNVRSRLSPPLPKSTLGNAVCLLREKVPLQFFALPSHANMEATSSVCADHSGDDEWALSFCRVAYGLRAKLNAIDDDYIRDYISYVQKSPCHLSVTLDTENLYLSNWREIGVYDADFGGMLGKPLRMRAPDGYTDGLIFVMAQRSEDKSAPWEFNISLEASTMKRIVHDPLWCKYVELDAFWHGEE | 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 peptide synthetase anaPS . The prenyltransferase anaPT then converts (R)-benzodiazepinedione to aszonalenin in the presence of dimethylallyl diphosphate (DMAPP) via C3-prenylation . The last step in the biosynthesis of acetylaszonalenin via acetylation of aszonalenin at position N1 catalyzed by anaAT .
Catalytic Activity: (2R,3S,11R)-aszonalenin + acetyl-CoA = (2R,3S,11R)-acetylaszonalenin + CoA
Sequence Mass (Da): 56729
Sequence Length: 509
Pathway: Alkaloid biosynthesis.
EC: 2.3.1.-
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P54802 | MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKPGLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGELTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYLALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTPVLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELIKEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQFWGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGALEAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAARRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAWRLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAYELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYANKQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPRGDTVDLAKKIFLKYYPRWVAGSW | 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 | MTSKVQLVFLFLFLCVMWASPSAASCDEPSDPMMKQFEEWMAEYGRVYKDNDEKMLRFQIFKNNVNHIETFNNRNGNSYTLGINQFTDMTNNEFVAQYTGLSLPLNIKREPVVSFDDVDISSVPQSIDWRDSGAVTSVKNQGRCGSCWAFASIATVESIYKIKRGNLVSLSEQQVLDCAVSYGCKGGWINKAYSFIISNKGVASAAIYPYKAAKGTCKTNGVPNSAYITRYTYVQRNNERNMMYAVSNQPIAAALDASGNFQHYKRGVFTGPCGTRLNHAIVIIGYGQDSSGKKFWIVRNSWGAGWGEGGYIRLARDVSSSFGLCGIAMDPLYPTLQSGPSVEVI | 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 tripeptide for cleavage is Pro-Leu-Gln, with cleavage occurring after the Gln residue . Another optimal tripeptide is Val-Leu-Arg, which may imply that a hydrophobic residue at the P3 position of substrates is preferred .
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg-|-NHMec, but broader specificity than fruit bromelain.
Sequence Mass (Da): 38248
Sequence Length: 345
EC: 3.4.22.31
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A1DN10 | MSPLSMQTDSVQGTAENKSLETNGTSNDQQLPWKVLGKSLGLPTIEQEQYWLNTAPYFNNLLIQCGYDVHQQYQYLAFYHRHVLPVLGPFIRSSAEANYISGFSAEGYPMELSVNYQASKATVRLGCEPVGEFAGTSQDPMNQFMTREVLGRLSRLDPTFDLRLFDYFDSQFSLTTSEANLAASKLIKQRRQSKVIAFDLKDGAIIPKAYFFLKGKSLASGIPVQDVAFNAIESIAPKQIESPLRVLRTFVTKLFSKPTVTSDVFILAVDCIVPEKSRIKLYVADSQLSLATLREFWTLGGSVTDSATMKGLEIAEELWRILQYDDAVCSHSNMDQLPLVVNYELSSGSATPKPQLYLPLHGRNDEAMANALTKFWDYLGWKGLAAQYKKDLYANNPCRNLAETTTVQRWVAFSYTESGGAYLTVYFHAVGGMKGNL | 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-ribosomal peptide synthetase anaPS . The prenyltransferase anaPT then converts (R)-benzodiazepinedione to aszonalenin in the presence of dimethylallyl diphosphate (DMAPP) via C3-prenylation . The last step in the biosynthesis of acetylaszonalenin via acetylation of aszonalenin at position N1 catalyzed by anaAT .
Catalytic Activity: (R)-benzodiazepinedione + dimethylallyl diphosphate = (2R,3S,11R)-aszonalenin + diphosphate
Sequence Mass (Da): 48811
Sequence Length: 437
Pathway: Alkaloid biosynthesis.
EC: 2.5.1.-
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Q96K21 | MNYDSQQPPLPPLPYAGCRRASGFPALGRGGTVPVGVWGGAGQGREGRSWGEGPRGPGLGRRDLSSADPAVLGATMESRCYGCAVKFTLFKKEYGCKNCGRAFCSGCLSFSAAVPRTGNTQQKVCKQCHEVLTRGSSANASKWSPPQNYKKRVAALEAKQKPSTSQSQGLTRQDQMIAERLARLRQENKPKLVPSQAEIEARLAALKDERQGSIPSTQEMEARLAALQGRVLPSQTPQPAHHTPDTRTQAQQTQDLLTQLAAEVAIDESWKGGGPAASLQNDLNQGGPGSTNSKRQANWSLEEEKSRLLAEAALELREENTRQERILALAKRLAMLRGQDPERVTLQDYRLPDSDDDEDEETAIQRVLQQLTEEASLDEASGFNIPAEQASRPWTQPRGAEPEAQDVDPRPEAEEEELPWCCICNEDATLRCAGCDGDLFCARCFREGHDAFELKEHQTSAYSPPRAGQEH | 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 VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ZFYVE19/ANCHR and VPS4 and subsequent abscission.
PTM: Phosphorylated in vitro at Ser-22 by AURKB; however, phosphorylation at this site could not be confirmed in vivo.
Sequence Mass (Da): 51546
Sequence Length: 471
Domain: The FYVE-type zinc finger mediates binding to phosphatidylinositol-3-phosphate (PtdIns(3)P).
Subcellular Location: Cytoplasm
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Q9DAZ9 | MESRCYGCAVKFTLFKKEYGCKNCGRAFCNGCLSFSALVPRAGNTQQKVCKQCHTILTRGSSDNASKWSPPQNYKKRVAALEAKKKSSTSHSQSLTHKDQAIAERLARLRQENKPKSVPSQAEIEARLAALKDEVQGPIPSTQEMEDRLAALQGRVPPSHTVRPAHQAPDTRTQAQQTQDLLTQLTAEVAIDENCQPRASASLQNDLNKGAARSQRTNSQGQASQSLEEEKYKLLAEAAVELQEENTRQERILALAKRLAVLKGQDPSRVTLQDYHLPDSDEDEETAIQRVMQQLTEEAALDEASGFNIPEKPAPGSRAQPCKAEMEGPQAEEEELPWCCICNEDATLRCAGCDGDLYCARCFREGHDNFDLKEHQTSPYHPRRPCQEH | 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 VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ZFYVE19/ANCHR and VPS4 and subsequent abscission (By similarity).
Sequence Mass (Da): 43272
Sequence Length: 389
Domain: The FYVE-type zinc finger mediates binding to phosphatidylinositol-3-phosphate (PtdIns(3)P).
Subcellular Location: Cytoplasm
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Q84BZ0 | MSADPFVIVGAGHAARRTAEALRARDADAPIVMIGAERELPYDRPALSKDALLNDDGEQRAFVRDAAWYDAQRIALRLGTRVDAIEREAQRVRLDDGTTLPYAKLVLATGSRVRTFGGPIDAGVVAHYVRTVADARALRAQLVRGRRVAVLGGGFIGLEVAAAARQLGCNVTVIDPAARLLQRALPEVVGAYAHRLHDERGVGFQMATLPRAIRAAAGGGAIVETDRGDVHADVVVVGIGVLPNVELAQAAGLDVDNGIRVDAGCRTADRAIFAAGEVTMHFNPLLGRHVRIESWQVAENQPAVAAANLLGADDAYAELPWLWSDQYDCNLQMLGLFGAGQTTVVRGDPARGPFTVFGLGGDGRIVAAAAVNLGRDIGAARRLIAAGAMPDPQQLADPTVGLKTFL | 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: 406
Pathway: Aromatic compound metabolism; anthranilate degradation via hydroxylation; catechol from anthranilate: step 1/1.
EC: 1.18.1.3
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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(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25130
Sequence Length: 235
Domain: The pre-methyltransferase (preMT) region is responsible for mitochondrial localization.
Subcellular Location: Mitochondrion membrane
EC: 2.1.1.-
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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)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24740
Sequence Length: 229
Domain: The pre-methyltransferase (preMT) region is responsible for mitochondrial localization.
Subcellular Location: Mitochondrion membrane
EC: 2.1.1.-
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Q9GZV1 | MAKAPSWAGVGALAYKAPEALWPAEAVMDGTMEDSEAVQRATALIEQRLAQEEENEKLRGDARQKLPMDLLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLVQLWQADTRHALEHPEPGAEHNGLEGPNDSGRETPQPVPAQ | 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 translocation to the nucleus and negatively regulates myoblast differentiation.
Sequence Mass (Da): 39859
Sequence Length: 360
Subcellular Location: Cytoplasm
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Q9WV06 | MEGPEAVQRATELIEQRLAQEEETEKLRRSAPGKLSMDMLVLEEEKRLGVQSPALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAAAQEPPPEPEEITGPVNEETFLKAAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKLLSTPLHVAVRTGHVEIVEHFLSLGLDINAKDREGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTPTDLVQLWQADTRHALEHPEPESEQNGLERPGSGRETPQPIPAQ | 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 translocation to the nucleus and negatively regulates myoblast differentiation.
Sequence Mass (Da): 36707
Sequence Length: 328
Subcellular Location: Cytoplasm
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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 rate-limiting enzyme in GTP biosynthesis or protects IMPDH2 by stabilizing IMPDH2 filaments assembly . Implicated in different cellular processes, like copper homeostasis and cell proliferation .
Sequence Mass (Da): 34295
Sequence Length: 317
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasmic vesicle
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C5BV64 | MRVLGMISGTSHDGIDVAVVRFTLDAGGAQLRGVVEHATTVPYPTALRARVAGALPPAQVGMAEVCALDADLGHAFADAAAEAAAAPDVPEPPDLVCSHGQTMYHWVAEGSALGTLQLGSPAWIAERLGVPVVADVRIRDVTAGGQGAPLVPLLDELLLAGASGRTAVLNLGGIANVTVVGDGADPVAYDVGPANALIDAAVAAAGRGAYDADGALAAAGRVHAPLLDALLTEPYYARRPPKSTGKELFDPGYVDRVRRGAGGAAAADLSLEDLVSTLTELTARVVAQDVRRLDVARLVVSGGGVRNPVLLGALTAAVPGVEVVPSDAFGVSVDHKEAVAFALLGWFTAHGLPASVPSATGASGARVLGSVTPGAGPLRLPTPLSTAPSRLRLTS | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 39695
Sequence Length: 395
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q7VUW3 | MDSTTHGPRTHVPGRLFIGLMSGTSMDGADGVLVRLDGPRPEVLASASLPMPAALRDELFALNHAGANELERAALAANGLARLYARAVRQLLDQAGLQPGDVAAIGAHGQTVRHRPDLGYTLQLNAPALLAELAGIDVVADFRSRDVAAGGQGAPLVPPFHAALFAGGQARAVLNLGGIANVTLLEPGRPPRGFDTGPANVLLDAWCQRHTGQPYDADGRFAAQGQVLADLLEHLIASEPWFALAPPKSTGRDLFNLDWLLARLQAFDGPAPQPQDVQATLQRLTARTVANAIDASAAAPRDVLVCGGGARNPGLMRELAYCLQRPVRPTDDAGVPAQWVEALAFAWLAQACLDRIPAGLPTVTGARAARVLGALYPA | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 39576
Sequence Length: 378
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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A6X3N5 | MQPIWAVGLMTGTVLDGNIDVALLKTDGETIAEFGAYALKPYPRWIRDLLEQAQAEARVWNFEGAEPAIFAEAEEALTRAQSAAVRELVEESGLSMADIGVVGFHGQTVLHRAPQAGRLGDTRQLGDGRLMSQLLATKVAYDFRTADIRAGGQGAPLAAVYHAALLRSADASGNTAILNLGGVGNITWWDGDDALVAFDTGPANAPINDFMKKRGLGEMDRDGALAAKGKVDEDRLAELLKHPYLIAPYPKSLDRFDFTEMMADGLNEENGAATLTAFTTSAVGKALDILPRRPKRLAVSGGGRRNPTMMHMLVERAEVELVPVEALGWRGDAVEAECFAFLAVRVLRGLPISFPSTTGVPEPMTGGELVG | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 39683
Sequence Length: 371
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q46HU0 | MRVLGLMSGTSADGIDAVLVDFTGDPSRPKWQILNTFSYEYPSSIREKIIQVGQGLKISSKDWLELAEEITELNAFAARTCDPDSTAEVVGCHGQTLFHRSVKKSKRGGSLQILLGPLLANLLDQIVIYDFRSKDIASGGHGAPLVALVDEALVGRLYGWRGVLNLGGIANLTIIPPKTGIDKTSQCLGWDCGPANSLVDLAVKESTNSSLTFDENGSLASLGIPKLEIIDKWLRDPFFYLEPPRSTGREQFGFQYLQKRKKELGDISKEDLISTLTTFTASIISQDLDNLFKLKQIRLIELLVAGGGSKNLFLMRQLQKQCCGVHVRPIHEIGVPSQYREALVFATLSWWNFLGKKVHPKYITGANKPILYGVRVDP | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 41702
Sequence Length: 378
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q15RS7 | MNKHIEQLYRSAKKRSRLIIGLMSGTSLDGLDVALCRIEGHGTDTQIELVAFCTVDYDDGYKQKIKSVFAKRQVDLQQVTLLNPWVGVLHGQMVNQCLEKWNIAATDIDAIASHGQTIYHCPLGQHGQSEFGNATLQIGDADHLAVTTGILTIGDFRQKHIAAGGEGAPLAVYGDYLFFTSKQENRILLNMGGIANLTFLPCSADASAVFSSDIGPGNTIMDAYVQRHFSPLHYDKDSAMASQGKVHLGLLDSLLEHAFFALDFPKTTGPEVFNLDYLSVAQAHSATRQLAHEDVLATLNLFSARTIANAINDAAIELEEFNVYASGGGIHNPLLMEHILRLCPNVTAIQDTSKLGIDPDAKEAVLFAILANECLVGGQQPFGNLEQGIPNITMGKISFPD | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 43490
Sequence Length: 401
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q9I5Q5 | MPRYLGLMSGTSLDGMDIVLIEQGDRTTLLASHYLPMPAGLREDILALCVPGPDEIARAAEVEQRWVALAAQGVRELLLQQQMSPDEVRAIGSHGQTIRHEPARHFTVQIGNPALLAELTGIDVVADFRRRDVAAGGQGAPLVPAFHQALFGDDDTSRAVLNIGGFSNVSLLSPGKPVRGFDCGPGNVLMDAWIHHQRGEHFDRDGAWAASGQVNHALLASLLADEFFAARGPKSTGRERFNLPWLQEHLARHPALPAADIQATLLELSARSISESLLDAQPDCEEVLVCGGGAFNTALMKRLAMLMPEARVASTDEYGIPPAWMEGMAFAWLAHRFLERLPGNCPDVTGALGPRTLGALYPA | 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 plays a role in cell wall recycling. Contributes to intrinsic fosfomycin resistance in P.aeruginosa .
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 39120
Sequence Length: 363
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q3K5W7 | MALYIGVMSGTSLDGLDIALIEQSSAINLVATHYIPMPDTLRAELLGLCAGGPDEIARSAIAQQNWVKLAAQGIHTLLEQQQLKPEAIRAIGSHGQTIRHEPARGFTVQIGNPALLTELTGITVVSDFRSRDVAAGGQGAPLVPAFHEALFEERTGNRAVLNVGGFSNLSLIEPNKPVAGFDCGPGNVLMDAWIHQQRGENYDRNGQWAASGKVEPTLLKALLSDPFFVTQGPKSTGREVFNLPWLEQQLSCLPGFAAENVQATLLELTALTIVESLQSAQSNTEELLVCGGGAHNVTLMKRLADLLPNAKVASTATHGVDPDWVEAMAFAWLAHCCLEGIAANRPSVTGAKGLRVLGAIYPN | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 38607
Sequence Length: 363
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q88QQ4 | MALYLGVMSGTSLDGLDIALVEQGEQLELLATHYLPMPPDLRQDLLALCSSGPDEIARAALAENRWASLAGEGIRQLLARQGLKPEAVRAIGSHGQTIRHEPARGFTVQIGNPALLAELTGISVVADFRRRDVAAGGQGAPLVPAFHETLFSQLGRRLAILNVGGFSNLSLIEQDKPVHGFDCGPGNVLLDAWIEREHGHPYDADGAWAASGVAQPGLLSALMADPFFAGSGPKSTGREVFNLPWLDRHLANLPAYRAQDVQATLLELTARSIIDSLGKAQQGTEALLVCGGGARNGALMARLGQLLPAARVASTGAYGVDPDWVEAMAFAWLAHCCLEGIAANRPSVTAAKGLRVLGAIYPA | 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 plays a role in cell wall recycling. Contributes to intrinsic fosfomycin resistance in P.putida .
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 38236
Sequence Length: 363
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q3ICY1 | MHPHISKLYNSALKPSRLIIGLMSGTSLDGLDVALCKITAAGVHTQIEVLKFTTVDYSDDYKTKIKQVFAKRECNLEYLTLLHPWVGKFHGDMVNQCLNSWQVNPANIDVIASHGQTIYHCPKSQHQYNDFNNGTLQIGDSDQIAVTTGITTIGDFRQKHIAAGGEGAPLAVYGDYLFFSSSDENRILLNMGGIANLTFLPQNGDSNAVFSSDIGPCNTIMDAYVQRYFNNMHYDENAAIAKAGFINTALLTALCDNHFLTLKMPKTTGPEVFNLAYLEAAQQASNTQKLSHQDVMATLNRFTAEVIANALNTCVKMAPNSVVYASGGGIHNLLLMQHLVTLCPAIKGFKNTHALGVDPDAKEAVLFAILANECLAGEQLHLDNKAQGIAGVTMGKVSFAD | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 43557
Sequence Length: 401
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q4FQ90 | MDDLNYATLTEALEQTVFENFDDGLYIGMMSGTSLDGMDAILCQFSNHTNSSNISNEDNTQQPMHLLATYSQDFPPRLREVLLALCQPNGINQLTPTAGEPDSELEWFGWASKAYAEFASDVVNTLLQQSNTDIESVLAIGCHGQTVRHRPQMGFSLQLVDANIIAERTGISVVSDFRRRDMAVGGQGAPLVPAFHQALFAVPDSTRILLNLGGIANIAVLPAISDDLSDFNEHSDNQPSDSVVGYDTGPANLLLDAWTALHTDKDYDAGGTWAQSGQVVEPLLNQLLEHPFFVKAYPKSTGREDFNLAWLQDELQKFDQAAADIRYSSADVQATLTELTAISASAQINIFINASSNNAVYVCGGGALNDYLMMRLQAHLPRCKVETTASLGLEPTWVEAVAFAWLARQTLMGETGNLPAVTGASKGVVLGQVCFA | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 47228
Sequence Length: 436
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q8Y241 | MTTLASSISERYIGLMSGTSLDGVDGVLVDFSGPRPMLLTDAYVPFPPALRQAFFDLQSAGHNEIHREALAANALADLYAECVAQLLHESGCDPREVRAIGAHGQTIRHQPGEHDGIGYTRQTQHAAVLAERTGIDVIADFRSRDIAAGGQGAPLVPAVHRALFALPDAWRVVCNIGGIANLTVLPPQQSDARDRVLGFDCGPGNALLDYWVHAHRGEAYDRNGEWARSGWIDAALLETLRSEPFFARMPPKSTGRDLFNPTWLQQQAGDTLERIRPEDVQATLLALTADTIADAVRTHAPRTASLVVCGGGARNGALMQRLAAQLPGTLVAASDDFGVPAHQVEALAFAWLARQCVRREPGNVYHATGAAGPRVLGTIYPA | 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 cell wall recycling.
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Mass (Da): 40965
Sequence Length: 382
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 2.7.1.170
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Q6P6B7 | MAQPGDPRRLCRLVQEGRLRALKEELQAAGGCPGPAGDTLLHCAARHGHRDVLAYLAEAWGMDIEATNRDYKRPLHEAASMGHRDCVRYLLGRGAAVDCLKKADWTPLMMACTRKNLGVIQELVEHGANPLLKNKDGWNSFHIASREGDPLILQYLLTVCPGAWKTESKIRRTPLHTAAMHGHLEAVKVLLKRCQYEPDYRDNCGVTALMDAIQCGHIDVARLLLDEHGACLSAEDSLGAQALHRAAVTGQDEAIRFLVSELGVDVDVRATSTHLTALHYAAKEGHTSTIQTLLSLGADINSKDEKNRSALHLACAGQHLACAKFLLQSGLKDSEDITGTLAQQLPRRADVLQGSGHSAMT | 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 Ser adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent peptides.
Sequence Mass (Da): 39284
Sequence Length: 361
Domain: Side chains of Lys-102, Lys-135 and Lys-165 capture Ser that is misactivated by AARS/AlaRS.
Subcellular Location: Cytoplasm
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A2AS55 | MALPGDPRRLCRLVQEGRLRDLQEELAVARGCRGPAGDTLLHCAARHGRQDILAYLVEAWSMDIEATNRDYKRPLHEAASMGHRDCVRYLLGRGAVVDSLKKADWTPLMMACTRKNLDVIQDLVEHGANPLLKNKDGWNSFHIASREGHPVILRYLLTVCPDAWKTESNIRRTPLHTAAMHGCLEAVQVLLERCHYEPDCRDNCGVTPFMDAIQCGHVSIAKLLLEQHKACSSAADSMGAQALHRAAVTGQDEAIRFLVCGLGIDVDVRAKSSQLTALHYAAKEGQTNTVQTLLSLGADINSTDERNRSVLHLACAGQHVACTRLLLQSGLKDSEDLTGTLAQQLTRSVDILQDFDHDVKS | 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 Ser adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent peptides .
Sequence Mass (Da): 39776
Sequence Length: 361
Domain: Side chains of Lys-102, Lys-135 and Lys-165 capture Ser that is misactivated by AARS/AlaRS.
Subcellular Location: Cytoplasm
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Q499M5 | MAPPGDPRRLCRLVQEGQLRALREELEVAGGCWDPEMFRGSQGPAGDTLLHFASRHGRQDILAYLVEAWSMDIEAANRDYKRPLHEAASMGHRDCVRYLLGRGAVVDSLKKADWTPLMMACTRKNLEVIQDLVEHGANPLLKNKDGWNSFHIASREGDPVILRYLLTVCPDVWKTESKIRRTPLHTAAMHGCFEAVQELLERCHYEPDCRDNCGVTPFMDAIQCGHVSIAKLLLENHEACSSATDSLGAQALHRAAVTGQDEAIRFLVCGLGIDVDVRAKSSQLTALLYAAKEGQTSTVQTLLSLGADINSTDERNRSALHLACAGQHAACARFLRQSGLKDSADLTGALAQQLTRGVAILQDFDPGVKS | 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 Ser adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent peptides.
Sequence Mass (Da): 40560
Sequence Length: 370
Domain: Side chains of Lys-111, Lys-144 and Lys-174 capture Ser that is misactivated by AARS/AlaRS.
Subcellular Location: Cytoplasm
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Q945B4 | MGSCSPQLPLICLSDQTLKPGSSKWVKVRSDVRKALEDYGCFEAKIDQVSMELQGSVLKAMQELFALPTEAKQRNVCPKPFAGYFSHNGLSESFGIKDANILEKAHEFTQQLWPEGNKSIKMIQLYAEKLAELDMMVRRLILESYGIEYFIDEHLNSTYYRMRLMKYIARPDNDITAAVGANVDNGANDNADGDANVNDDGASIGVKVNVDVGDDVNDNDSVNIGVGVDINVETNVNGDLDAEANGDATAWVVGAVSGNASVGAKEANVDAELGLPSHTDKSLSGIIYQHQIDGLEVKTKEGKWIRVKPAPNTVIVIAGDALCALMNGRIPSPYHRVRVTERKKTRYAAALFSYPKEGYIIDSPKELVDEKHPRAFKPFDFVDLFNFYHTEAGRRAPSTLQAFCGVSAGK | 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 | MRPLSHLSFFNGLLLGLSALSAATSVVHERREATSSNWVKRARVNPSDKHVVRIGLTQSSLEEAHDLLMDVSNPSSPNYARFYSADEVAAKFAPSTETVNEVQNWLTEKGINASRVAQTQNHGWLVFHATSKEIENLFDTTYYEYHNRKTGKKAIACEQYHVPASVQKHIDYVHPGVNLNPSSGKPSSIRRRAAASKKTKLPARGPRPIQQHDVKGLNVTNCDQLITPECIRALYKIPSARAAPHPNNSLGIFEEGDYYAQEDLDLFFKTFAKDIPQGTHPIPAFIDGAEAPVPVTKAGGESDLDFELAYPIVHPQSITLYQTDDANWASNTTGFLNTFLDALDGSYCTYCAYGECGNDPSLDPVYPDDAGYDGQLMCGVFKPTNVISVSYGEQENDLPANYQQRQCMEFLKLGLQGVSVLFASGDNGVAGPPGDGNSVNGCLNNGTVFSPAFPNSCPYITNVGATKVYPGYTVSQPESAVYDPDGLYSYASGGGFSNIYPIPDYQAEAVATYFKDHNPPYPYYEGAENLGKNGGLYNRLGRGYPDVAANGDNIAVFNGGEFGSSGGTSASTPIFASIINRIIDERLAVGKGPVGFINPVLYKNPSVLNDITNGTNPGCGTDGFSTAPGWDPATGLGTPNYPKMLKLWLDLP | 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 to trypsin.
PTM: N-glycosylated.
Sequence Mass (Da): 70501
Sequence Length: 652
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9ZUC1 | MNAALATTTATTPVLRRETPLLHYCSLTTKSPVYQINRVRFGSCVQTVSKKFLKISASSQSASAAVNVTADASIPKEMKAWVYSDYGGVDVLKLESNIVVPEIKEDQVLIKVVAAALNPVDAKRRQGKFKATDSPLPTVPGYDVAGVVVKVGSAVKDLKEGDEVYANVSEKALEGPKQFGSLAEYTAVEEKLLALKPKNIDFAQAAGLPLAIETADEGLVRTEFSAGKSILVLNGAGGVGSLVIQLAKHVYGASKVAATASTEKLELVRSLGADLAIDYTKENIEDLPDKYDVVFDAIGMCDKAVKVIKEGGKVVALTGAVTPPGFRFVVTSNGDVLKKLNPYIESGKVKPVVDPKGPFPFSRVADAFSYLETNHATGKVVVYPIP | 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 .
Sequence Mass (Da): 40986
Sequence Length: 386
Subcellular Location: Plastid
EC: 1.3.1.-
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Q9V035 | MFGYWGKILRVNLTDGTIKEETFNEEFAKKWLGTRGFGIYFLLKEMDPKVDPFSPENKLIFATGPLTGTSAPTGGRYMVITKSPLTGYIAMANSGGYFGAELKFAGWDAIIIEGKADHPVYLYIHDENVEIRDASKVWGKLVSETEKALKEEVGDKHVQIASIGPAGENKVRFAAVMNNGHRAAGRGGVGAVMGSKNLKAIVVRGHKRVEVADKGKFMEVIREKIEKLKKDPVAGGGLPKYGTAVLVNIINEHGLYPTRNFQTGVFEYAYEQSGEAMAAKYLIRNKPCFACPIGCGRVNYLPSIGETEGPEYESTWALGANLGINDLASIIEANHFADEYGMDTISLGGTLATAMELYERGLIKQEDIGGENEPPFRFGNTEVLHYWIHKIAKREGFGDILAEGGYRLAERFNGTEYFMGVKKQELPAYDPRGAEGHGLGYATNNRGGCHIKQYMISPEILGYPYKMDPHDISDEKVKMVILFQDLTALIDAAGLCLFTTFGLGADDYRDMLNAALGWDFSTEDYLKIGERIWNAERLFNLKAGLDPLKEDTLPKRLLEEPMPEGPNKGHVVRLKEMLPRYYKLRGWTEDGRIPEEKLKELGLEEFI | 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 | MYGNWGRFIRVNLSTGDIKVEEYDEELAKKWLGSRGLAIYLLLKEMDPTVDPLSPENKLIIAAGPLTGTSAPTGGRYNVVTKSPLTGFITMANSGGYFGAELKFAGYDAIVVEGKAEKPVYIYIKDEHIEIRDASHIWGKKVSETEATIRKEVGSEKVKIASIGPAGENLVKFAAIMNDGHRAAGRGGVGAVMGSKNLKAIAVEGSKTVPIADKQKFMLVVREKVNKLRNDPVAGGGLPKYGTAVLVNIINENGLYPVKNFQTGVYPYAYEQSGEAMAAKYLVRNKPCYACPIGCGRVNRLPTVGETEGPEYESVWALGANLGINDLASIIEANHMCDELGLDTISTGGTLATAMELYEKGHIKDEELGDAPPFRWGNTEVLHYYIEKIAKREGFGDKLAEGSYRLAESYGHPELSMTVKKLELPAYDPRGAEGHGLGYATNNRGGCHIKNYMISPEILGYPYKMDPHDVSDDKIKMLILFQDLTALIDSAGLCLFTTFGLGADDYRDLLNAALGWDFTTEDYLKIGERIWNAERLFNLKAGLDPARDDTLPKRFLEEPMPEGPNKGHTVRLKEMLPRYYKLRGWTEDGKIPKEKLEELGIAEFY | 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]
Sequence Mass (Da): 66631
Sequence Length: 605
EC: 1.2.7.5
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Q8GZP5 | MANTKDSYHIITMDTKESSIPSLPMKEIPGDYGVPFFGAIKDRYDFHYNQGADEFFRSRMKKYDSTVFRTNVPPGPFNARNSKVVVLVDAVSYPILFDNSQVDKENYFEGTFMSSPSFNGGYKVCGFLGTSDPKHTTLKGLFLSTLTRLHDKFIPIFTTSITSMFTSLEKELSEKGTSYFNPIGDNLSFEFLFRLFCEGKNPIDTSVGPNGPKIVDKWVFLQLAPLISLGLKFVPNFLEDLVLHTFPLPYILVKRDHQKLYNAFYNSMKDILDEAEKLGVKRDEACHNFVFLAGFNSYGGLKVFFPSLIKWIGTSGPSLHARLVKEIRTAVKEAGGVTLSAIDKMPLVKSVVYETLRMDPPVPFQTVKARKNIIITNHESSFLIKKDELIFGYQPLATKDSKVFKNAEEFNPDRFVGGGEKLLKYVYWSNGKEIDNPSVNDKQCPGKDLIVLMGRLLVVEFFMRYDTFEVEFGKLLLGSKVTFKSLTKATS | 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 hydrolysis and cyclization . The first step is the synthesis of (12Z)-9,10-epoxyoctadeca-10,12-dienoic acid (9,10-EOD) and the final products are (9R)-alpha-ketol and the racemic cis-10-oxo-11-phytoenoic acid . The cyclase activity possesses regiospecificity and (9Z)-12,13-epoxyoctadeca-9,11-dienoic acid (12,13-EOD) is significantly less efficient as a substrate for cyclopentenone production than 9,10-EOD . Has no hydroperoxide lyase activity . May play a defensive role against soil-borne pests that affect roots or juvenile tissues as they emerge from the germinating seed .
Catalytic Activity: (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
Sequence Mass (Da): 55514
Sequence Length: 491
EC: 4.2.1.92
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Q3SYW1 | MSASAVFILDVKGKPLISRNYKGDVAMSEIDHFMPLLMQREEEGALTPLLSHGRVHFLWIKYSNLYLVATTLKNANASLVYSFLYKIVEVFSEYFKELEEESIRDNFVIVYELLDELMDFGFPQTTDSKILQEYITQQGNKLETGKSRVPPTVTNAVSWRSEGIKYKKNEVFIDVIESVNLLVNANGSVLLSEIVGSIKLKVFLSGMPELRLGLNDRVLFELTGRSKNKSVELEDVKFHQCVRLSRFDNDRTISFIPPDGDFELMSYRLSTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANGVEISVPVPSDADSPRFKTSVGSAKYVPEKNTVIWSIKSFPGGKEYLMRAHFGLPSVEKEEVEGRPPIGVKFEIPYFTVSGIQVRYMKIIEKSGYQALPWVRYITQSGDYQLRTS | 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.
PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its affinity for sorting signals.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 48150
Sequence Length: 423
Subcellular Location: Cytoplasmic vesicle
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P35602 | MATSAMFILDLKGKTIISRNYRGDIDMTAIDKFIHLLMEKEEEGSAAPVLTYQDTNFVFIKHTNIYLVSACRSNVNVTMILSFLYKCVEVFSEYFKDVEEESVRDNFVVIYELLDEMMDFGFPQTTESRILQEYITQEGQKLISAPRPPMAVTNAVSWRSEGIKYRKNEVFLDVIESVNMLASANGTVLQSEIVGSVKMRVYLTGMPELRLGLNDKVLFEGSGRGKSKSVELEDVKFHQCVRLSRFDTDRTISFIPPDGAFELMSYRLTTVVKPLIWIETSIERHSHSRVSFIIKAKSQFKRRSTANNVEIIIPVPSDADSPKFKTSIGSVKYTPEQSAFVWTIKNFPGGKEYLLTAHLSLPSVMSEESEGRPPIKVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGEYEMRMK | 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 and behavior, including negative regulation of vulval differentiation . Required for the dendritic localization of potassium channel kvs-4 in the cholinergic motor neuron DA9 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 48229
Sequence Length: 422
Subcellular Location: Golgi apparatus
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P47795 | MIHSLFLMNGGGAVFLEKHWRSVVSRSVCAYLLEAQLKAGQPENVAPVLATPHHYLVSTHRHGISFVAVIQAEVPPLFVIEFLHRVAETLQDYFGECSEASIKDNVVIVYELLEEMLDNGFPLATESNILKELIKPPTILRSVVNSITGSSNVGDQLPTGQLSNIPWRRVGVKYTNNEAYFDVTEEIDAIIDKSGSTVFAEIQGVIDACIKLTGMPDLTLSFLNPRLLDDVSFHPCVRFKRWESERVLSFIPPVGNFRLMSYHVNSQNLVAIPVYVKHNINFRDDGSTGWFDITIGPKQTMGKVVENILVIIHMPKVVLNMTLTAAQGNFTFDPVTKVLIWDIGKIILPKLPTLKGLINLQSGEAKPEENPTLNIQFRIQQLAVSGLKVNRLDMYGERYKPFKGVKYVTKAGKFQVRT | 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 by phosphorylation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46772
Sequence Length: 418
Subcellular Location: Golgi apparatus
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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 molecules (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18759
Sequence Length: 161
Subcellular Location: Golgi apparatus
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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 cargo molecules.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18733
Sequence Length: 158
Subcellular Location: Golgi apparatus
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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 cargo molecules.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18615
Sequence Length: 157
Subcellular Location: Golgi apparatus
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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 cargo molecules. Involved in TLR3 trafficking .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18280
Sequence Length: 154
Subcellular Location: Golgi apparatus
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O94669 | MSTIEAIYLVDTNGALLLQLESRGRTSPITLEHIKNELFRYKLRNEEPPFILHNKNFLIFQELEEDVRLCIPTTCDTEPLYIHDIMRRIVDVVKTFFGGFNASKVEKNVCVIVQLLAEMIDYGYATCMEPNALQDIVPLPSFMNKFMAVTGLQTNTPTLARDTVPWRTAKAKYATNEFFIHVLERVSAVYQPNGKLAFGTVKSDMECKCQISGMPLLLLSLRPGTKLGNVRFHQSVNLKRWKQHPDQIEFIPPDGKFTLASFQTDFATQKSLPVVVEAKNKLDGRFEVRIRNTGKKSVENLKILITIPQALKSVTVTEGNYIFRASKYTHMEEGILEWSVKKLAWTSPALVLTGFLAPLKKDANSTEESSSYSKLEHLDLQYKLQGSTLHNFKVESLKMLNHPDKKSYKGVKHTIIAQNVSFRFR | 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).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 48422
Sequence Length: 425
Subcellular Location: Cytoplasm
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P38153 | MYLSFYITDTKNKLIFQYLLGATAPSFKHLWTRVQSTCPQLLEDSSSDDYLDHSMVGRDLEVYKYFSVINKLNYWCLASTSKSKGPLDCFTFLETIDRILLEYFDKDKLSIKKIVNNYDRISLIFNCCVEAGEPNVSDMLYVNKIKEAVPERSDLSKFISSTAHNLQQAVQLPQQRQQQLQQNQISRGSNSLIENEEIVPWRTSRASKHENNELYVDLLETFHVVFEKKKSHLRLLTGSIHGIVDVRSYLNDNPLVAVKLNTMGNDIGIPSLHDCVEINDGVFSPSNITFIPPDGKFRLLEYSVDLSSQVKQSGVRMNSIGLMSLHFQNGLGKDSDEFELSLNIENFKKVSQVDDLKIDLQFNVENADPNEIAYKIKILRNTHGRFENSIIMGQGQWIFDKSTATGTVPVLRGCIEYENTGPNFTKKVDLQTVSLEYSYIGQSASGIYVEAIDIVSGLTIGKNTKLYKGAKYKTQTGNFQVRL | 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 the transport via the ALP pathway, which directs the transport of the cargo proteins PHO8 and VAM3 to the vacuole.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54837
Sequence Length: 483
Subcellular Location: Golgi apparatus
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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 the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21732
Sequence Length: 193
Subcellular Location: Golgi apparatus
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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 the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22035
Sequence Length: 193
Subcellular Location: Golgi apparatus
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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 the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22017
Sequence Length: 193
Subcellular Location: Golgi apparatus
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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 function in maintaining the identity of lytic vacuoles and in regulating the transition between storage and lytic vacuoles (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18729
Sequence Length: 166
Subcellular Location: Cytoplasm
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