ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9LS22 | MSDRVHERSMGMEEEGSTKNMKTKVLELPTKIKKILKNIWKVGKDDPRRVKHALKVGVSLTLVSLLYLMEPLFKGIGNSAIWAVMTVVVVLEFSAGATLCKGLNRGLGTLIAGSLAFFIEFVANDSGKIFRAIFIGAAVFIIGALITYLRFIPYIKKNYDYGMLIFLLTFNLITVSSYRVDTVIKIAHERFYTIAMGVGICLLMSLLVFPIWSGEDLHKSTVAKLQGLSYSIEACVNEYFEEEEKDEETSDLSEDTIYNGYKTVLDSKSADEALAMYASWEPRHTRHCHRFPWKHYVKVGSVLRQFGYTVVALHGCLKTE... | Function: Malate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60675
Sequence Length: 543
Subcellular Location: Membrane
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Q54SV3 | MNSENIIKVIKGKKVVINGEIKPASILIKNGIIIDIKDYSSEIKEEHEVLIEEEKLVIMGGLVDSHVHINEPGRTEWEGFLSATSAAASGGVTTIIDMPLNSSPVTTTFENLQTKIESMPGKLRVDVGLLGGIIPGNSSEISRMVLEGGVVGFKSFLVHSGIDEFPHVKEDDIQEAMNVMKKLKDEQGGRDVVMMFHAEIEEPIKEATERLQRENADPKLYDTFLKSRPRVSENIAIDKVIELTKKNMIKTHIVHLSSSDAIEAIHEAVHNDGVPITAETTYHYLYFESEQVPYGNTLYKCCPPVRESENKDLLWKAVTN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
Catalytic Activity: (S)-allantoin + H2O = allantoate + H(+)
Sequence Mass (Da): 72476
Sequence Length: 649
Pathway: Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1.
E... |
Q55C91 | MEIWKVIFSIWFLLFQNFVLSAKNDDNKLKVIRGRNVIYNGNVIPLSILIRNGKTIGIKDYSFNPKKLNENYEILYDDRECNNNEDFIIMGGLVDSHVHVNEPGRTEWEGFESATSAAAAGGVTTIVDMPLNSSPVTTSFKNLLDKIESMKGKLRVDVGLLGGIVPGNSKEIKKMVLQGGVLGFKSFLLPSGIDEFPPVNENDIQEAMNEMKLLKCQYNNSDVIMMFHAEVEEPIKEATVRLKNENADPKLYKTYLDSRPKISENQAISKLIDITRQNQIVSTHIVHLSSSESIEQIREAMDQGVPISAETTYNYLHLTS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
Catalytic Activity: (S)-allantoin + H2O = allantoate + H(+)
Sequence Mass (Da): 57323
Sequence Length: 510
Pathway: Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1.
E... |
C8VJR6 | MPKILCLHGYGTSASILQHQLGPFMAAADPSYEFVFLEGEIECQKAQGLGPFVKGPFLCYNESFAPADIQESCDLIDEMIQAAGPFDGIIGFSQGGSVALSYLLQRQIDGHPPPFRWAVFFSTVIAFAPNDTFGSNILANLTDHEIRLLDGYPATDLSSLHPLTRALCETTAQTFYSAKTGGFISPNTPIAEFSKRDDPSQPRVFHPALLGDRIPIPTVHITGRKDNSLMVGLSVLVQGLCDQRLIRSLTHSGGHNVPRSADDVRAAWAAVDWAIQHSQKQHIW | Function: Esterase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities . The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA... |
C8VJR5 | MASPASITLAEVARHSSPNDLWIVIEGNVYDVAEYREDHPGGDEILRQFAGKDATTEFQDAGHSNDAYVKLKTLLVGSLQSKTLPENQPEESSRIVSIAVSDRGKIPTKRQARNGNDTSKYGQLPSLVLAGGLALLFFTLKQHPWQSIQGYLSQAQVSRVQSSGWVGFLGGFLTATTLNTAAATFVGLTAKKTLLLRHRELEEYPRVKQHYLPLPPKKPGISGENTQQFLTLVDRQCIAPNVYKVRLQGDGLVIGLGQHLKVLAEIDGRKIQRSYTPVSPVGNSPKVDLIIKVYPKGQLGNYLLNLPLQSRVEIRGPFGR... | Cofactor: Binds 1 FAD per subunit.
Function: NADH-cytochrome b5 reductase-like protein; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities . The first step of the asperlin biosynthesis is the production of the intermediate 2,4... |
A0A1U8QFC3 | MTVQTFYLIGEKERSTRELDVGDPKTVNALRQGLAEVFNILSAEGIDFHDCHGPISTIESILRSESVGITVNGHPVRYPQQPQGIPIFGNHFEIYPDHLGNHERLFNKYGSVIRTNNMGRVTYLTNDPDIAALAFRDNDYFTKAPSSASHPLYGIRDQTALFLCDTESPAWKEAHKFIPPSMTPRAVRHYTPLLQQSVDTVFNVLDKFDNNGQAFNVYHLTAKLASQVICQLVLGVDLHHFDAVDSPVHPIIVLLQRYLTLNRRVQTKGAWYSYLPFGDPVALKNTRRELYGLIEEAVITCQKKNGGTTGDLPIQTAALH... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities . The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing pol... |
A0A1U8QYH7 | MSSDDTVKQEHSCSADSEKQDSSCASDNEQPKEPQSPRNIHGLLWVVTILAIYSSTFLFALDNTIVANIQPAIISSLNGIEKLAWSGVAFVMASSATVLTWLQIFNQFNIKWMYIFSIAVFMGGSAICGAAQSMDMLIGGRVICGIGGVGQYVGVMNFLPRLTTMQERPMYVSAMGLTWGAGTVLGPIIGGAFTDSSAGWRWSFYINLVVGGLFAPVYIFLLPSLEPQPAGTTVSSRLKRMDLVGTLILFAAFAAGVIGINFAGAMYPWSEPGIIVAITLGGVLFIVFGIQQTYCILTTEETRLFPVELVSWRQPLLSLL... | Function: Efflux pump; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities . Is probably involved in the efflux of asperlin (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59134
Sequence Length: 5... |
A0A1U8QYW8 | MADYVIQNLTSNLQAMQYAYSSREEMPVWATKLLTPIFMAVAVLTTLPPPGPLRVIVGLTAFTSLWLHVLTHWVSGPAFFMDAIFMISITVRWLLMFVAGTPEIDYHQTTQSGTTITHKGTKDSSTLRQGLTKLRWSVELWSCWRGQGWNFVDQHLPRGAERTQSRWEFLVSNAGRVLLNQYISDLVRKYAFCALWPAQVDAHVDFSSLPLLNRHGLVALQLIRDSLMLDSEYRKASILFVGLHLSTPDRWPSLFGNMRDLYTVRNFWGRVWHQIFRQIFTRCGDIVANALNAQKGTLLYKYSRLYVGFLVSGVQHYACA... | Function: Acetyltransferase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities . The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synt... |
P0CU77 | MTRQIPLLALSWLELIFFSCYYGGLAGLGYHSLWRIALRRRNVAPAIKSVLQTGRFADGTPLTRRYTNLEFLDKKLVPAVIFYDGLLTGACPLYRLLLVDIHSTMQAMALCMLVSTRSKSLSTISLLLPTFWNVFNQFYGAAFVYPLYLLLEAVTTGFNPLYPVETETSRSALLVSAMIGSFLPFTFLWPAFLRSGTESRQRAIALYRFAPVVFSLLQIVGEKVLGAQMIPQPTSQASPYLVAGCAATVGHWYALGGALGLAMRLSHRKGRLGALTLVLKRLYLPRSAEETTRLDASVLARAAHEFLQYDVLVLIAAYIP... | Function: Part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities . The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA with clea... |
C8VJR0 | MTMAALDVFNVPYSVPLLGSTVVILIGFIAIKALRVGSRPKGLPPGPPTEFIWGNTKQIDLFYPQYQYRKWAQQYGPVYTVMLGDTAHVVVSGLRDVRDIFIKQGASSQNRPPSRFQLLMRDGFFPGLNNGEKWRQSRRMWQAVLNNSAAKQYLPYQELETRQLLFDLLRAPTEWRDHIERYSNSVAMTMVNGRRIIDAADPRVKETIQDLYDLAETGVRGAFLDSWPFLWKLPEWMFPVCRQARKIAAKHREYIWRNYSDVAKRTSQGEVLPSVNHAIQEKLKQGWPGVSEIEGAEIGHHLLTGTTDTTASTLINWVAA... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities . The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing pol... |
Q9RVE3 | MLPRAVAHISAAALDHNLSALAQRSGTRLLLPVKADAYGHGMELVGRLAAAHPDVWGLAVATPQEAETLARLDLGKPLLLLTPPAPEELGALADLGVRLPVSTLAEVEALPAHAQAHLKVDTGMNRLGARPADAVAVGRALAERGQLEGVYTHFATADEPDLSFALTQLVRFRSVLDALPPVLAHCANGGGVLSFGRIEGMSLARPGLAAYGYVPEHLRHVCALRPVMTVRARVNQLHTAYPGETVSYGALWRAERETGVAVVGMGYADGYPRNATGRAAVLIGGERRPVLGRICMDQMMVDVTGLDVGVGDWAELWGEG... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 37193
Sequence Length: 351
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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B8J2K3 | MVSFDRPVWAEIDLSAFRHNMRQIKSLLQPGTIFCPIIKADGYGHGAVPLAHEAVAMGAGYLGVAILDEAAALRAAGITLPILILGYTPPQAAAFVVSNHITQTIFSKEQADALSAAASNLGITVKVHVKVDTGMTRIGVRPEEAAAFCSYVAGLENVHLEGMFTHFASSDSADHAYCLEQFGRFTAAIAAVEASGIRLGIRHCANSAAILSLPEGHLDMVRAGIILYGLKPSDECPMPIDLRPVMRLKARLAMVKQVPPGVGVSYGSIYHTQKESSLATIPIGYADGYTRMLSRKAQVLLRGQRAPVVGRICMDQCMVD... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 39627
Sequence Length: 371
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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A8ZRV0 | MNDFSAWAEIDLDAVAHNVAALKALTRPACRLMAAVKADGYGHGMCEVASVALESGASALGVSRIDEALDLRNHGITAPILVLGHTPAHRCREMVDQNLIQTVCALAEAQALSRAATAIGATVSVHLKVDTGMGRLGINTVVPGRTAPQEAAVKEALAVLDLPGLAAEGVFTHFACADSADKTHANAQFKRFSTLIQELEAAGRPVAVRHAANSAALIDMPETHLDMVRAGIAIYGLYPSAEVDRQKVALKPAMAFKTRVAQVKKVPAGFTVSYGATYTTPKPTVLAVVSVGYADGLNRLLSSRGFMLVRGCRVPLVGRI... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 40872
Sequence Length: 390
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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A4J8G6 | MKEPIWAEINLEAIRHNIKEIRKMVGPNREIMAVVKANGYGHGAVPVARVALEAGATRLAVARLSEAQELRRAGLKVPILLLGYISPDQIGDALEYNVTLTVFRFDLAKKIAAIAQGRGQRATVHLKVDTGMGRIGFTPDEEGLAEITAVCALNGLDVEGIYTHFATADEQDKSYTRWQFKRFMLVLNRLEEQGITFSLRHCANSAAIMEFPETYLDLVRPGIILYGLYPSEEVDKGKLLLQPAMTLKARITHVKKVNSGTKISYGCTYTVPQETDIASLPLGYADGYPRLLSSKGQVLVKGKRARVVGRVCMDQCMVDV... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 40808
Sequence Length: 370
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q72DH4 | MPISYNKASVVVSLQSIIANYRRIRTVAQRPMPVIKSDAYGHGLEAVGMALEAEGARECAVGTVGEGAKLRKAGFGADIVALLGALDREDAQLAASSGIIPTVLDIAGLERLAAQGTPERPVRVALKFDTGMARLGFTEHDVSALCERLRTLPSVRPVMAVSHLAVADDPTQSAFTMAQGAAFARIMAGLRSNFPDIMGSLSNSAATLAHPQLHWDVQRPGIALYGSNPLRGTALARHGEGLLPAMSVSVPVLQVHPLPAGRSISYGRTYTATKDATVAIIAAGYADNYSRALSGRGVAVAGGRRVPVLGRVCMQTTAID... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 39406
Sequence Length: 376
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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A5EW54 | MRALKKIINLNALRHNWALIKQRSLPATPMVVLKADAYGHGMTTVAKTLDDARYFAVSCIEEAIALRHLGIDTPVVLLEGVYRADELLLCEYYQFDTLVHNFRQMQWLKEFNGSVKAWLKVDSGMHRLGFTQDEIAEAFAQAHSLPVNIQWQGVITHFACSDEDDLTHAKKQLACMDRLVLPAHWKRCYANSAAIFALPQAHYDYTRSGIMLYGLSPFMHGDGSAYGLQPVMTVITEILAVRHLEKNETAGYGQGFTAPESGWLATIALGYGDGFARTITSGAVPVLIAGQRYPLVGRVAMDMAMVWLGSDRYAEGTIVE... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 39491
Sequence Length: 357
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q2JFD6 | MTEQRAGSPAGNDLRSCAVIDLDAVRTSVTALVARAGDAATMAVVKADGYGHGMIPCARAALEGGATWLGTAFLEEALALRAAGFTVPVLSWLAAPGESFAAAIAADVDLSASAGWALEEAAAAARRTGRTARVHLKADTGLGRAGATEADWPALCDAGAALEAEGVIEVIGVWSHFAFADAPGHPTVQGQIGRFRDAIDIATKAGLHPSVRHLANSAATLVSPEAHFDLVRPGVSVYGLSPGPEIGPPAAFGLRPAMTLTTHAALTKRVPAGTGVSYAHRYTTTRETTLAVVPLGYADGIPRSATNTAEVLFGGRRRRI... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 39581
Sequence Length: 384
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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B0TYB0 | MNILKISKQTLTNNIKIIREYVGNAKICFPVKANAYGHGIEEIVENTHDLVDFFAVANSLEAFRVTAITKKPVLVFGVIYYEYLERMVSENIRVSIQDYDDIEKLEQIAKELNKKIYVHINVNTGMNRMGVCYNDVCRTIKRAYNSKWIILEGVYSHLACADNRDHPTNAKQKKRFSEIVEYAKELSQDIICHLSNSYGFLGDKEICYDMVRPGILIYGFLPEFYVERSIREIKPIARLLSKVVKIIELEEGDGVGYSMIYRGFDGEKVAVIPIGYGDGFPRELGDRGFVNIDNVMYPMAGRMSMDGLTVSLGHNEHNVK... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 41664
Sequence Length: 365
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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P02760 | MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGC... | Function: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments . Intravascularly, plays a regulatory role in red cell home... |
Q07456 | MQGLRTLFLLLTACLASRADPASTLPDIQVQENFSESRIYGKWYNLAVGSTCPWLSRIKDKMSVSTLVLQEGATETEISMTSTRWRRGVCEEITGAYQKTDIDGKFLYHKSKWNITLESYVVHTNYDEYAIFLTKKSSHHHGLTITAKLYGREPQLRDSLLQEFKDVALNVGISENSIIFMPDRGECVPGDREVEPTSIARARRAVLPQESEGSGTEPLITGTLKKEDSCQLNYSEGPCLGMQERYYYNGASMACETFQYGGCLGNGNNFISEKDCLQTCRTIAACNLPIVQGPCRAFIKLWAFDAAQGKCIQFHYGGCK... | Function: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeo... |
P04172 | MRALAFAAALAAFSATAALAAGALEAVQEAPAGSTEVKIAKMKFQTPEVRIKAGSAVTWTNTEALPHNVHFKSGPGVEKDVEGPMLRSNQTYSVKFNAPGTYDYICTPHPFMKGKVVVE | Cofactor: Binds 1 copper ion per subunit.
Function: Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
Sequence Mass (Da): 12609
Sequence Length: 119
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Peri... |
P22365 | MISAKTLRPAIAAIALFAIGATGAWAQDKITVTSEKPVAAADVPADAVVVGIEKMKYLTPEVTIKAGETVYWVNGEVMPHNVAFKKGIVGEDAFRGEMMTKDQAYAITFNEAGSYDYFCTPHPFMRGKVIVE | Cofactor: Binds 1 copper ion per subunit.
Function: Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
Sequence Mass (Da): 14259
Sequence Length: 132
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Peri... |
P9WEP6 | MPRSWTDIVAEKRAIRDEKLTKCYGENVPSDPRIIAAKDIQALTKLLEARNVTAEAVVLAHIAKAKEAHQRTNCLTEICFDEALEHARELDAFQQEHGRLKGPLHGVPVSLKDQFNLKGLDSTLGYVGRAFHPAASDCVLVKVLKQLGAVILAKTNLPQCILWGETDNPLWGLTTHPMNPEYTPGGSSGGEGTLLALNGSMLGWGTDIGGSIRVPSHMNGLWGFKPSSGRFSYEAVAVSQDGQQQIPSVVGPMARTLSTITLASKAMIEAECWRLDPQLPPMPWRKDVFQEYLQKPLVIGIMVDDGTVKVHPPIERVFKE... | Function: Amidase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant . Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazi... |
Q07838 | MPEVVFSVDHSKSMRDQAVPGHNRWHPDIPAAATVKPGSEFRIECKEWTDGQIGNNDSANDVRDVDLAPCHMLSGPIKVEGAEPGDLLIVDILDIGPVPQTNGPNCGEGWGYSGIFAKVNGGGFLTDYYPDAYKAIWDFHGQQCTSRHVPGVRYTGITHPGLFGTAPSPDLLAKWNERERALIATDPDRVPPLALPPLVDGTLGGTASGDLLQAIANDGARTVPPRENGGNHDIKNFTRGSRIFYPVFVEGAMLSGGDLHFSQGDGEINFCGAIEMGGFIDMHVDLIKGGMETYGVTTNPIFMPGRVEPLYSEWLTFIGI... | Function: Allows acetamide to be used as a sole carbon or nitrogen source.
Catalytic Activity: a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+)
Sequence Mass (Da): 43964
Sequence Length: 406
EC: 3.5.1.4
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Q6J1Z6 | MQGEIIAGFLAPHPPHLVYGENPPQNEPRSQGGWEVLRWAYERARERLDAMKPDVLLVHSPHWITSVGHHFLGVPELSGKSVDPIFPNVFRYDFSLNVDVELAEACAEEGRKAGLVTKMMRNPKFRVDYGTITTLHLIRPQWDIPVVGISANNSPYYLNTKEGMSEMDVLGKATREAIRKTGRKAVLLASNTLSHWHFHEEPTIPEDMSKEYPATMAGYQWDIRMIELMRQGKTSEVFKLLPQFIDEAFAEVKSGAFTWMHAAMQYPELAAELFGYGTVIGTGNAVMEWDLRKAGLSMLGAADQKQRSAAVA | Cofactor: Binds 2 Fe(2+) ions per APD complex. The iron ions are bound to the beta subunit.
Function: Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCb seems to be the catalytic subunit of the complex. Also active ... |
Q9KWS5 | MKQYRNFVDGKWVESSKTFQDVTPIDGSVVAVVHEADRDLVDAAVKAGHRALEGEWGRTTAAQRVDWLRRIANEMERRQQDFLDAEMADTGKPLSMAATIDIPRGIANFRNFADILATAPVDSHRLDLPDGAYALNYAARKPLGVVGVISPWNLPLLLLTWKVAPALACGNAVVVKPSEDTPGTATLLAEVMEAVGIPPGVFNLVHGFGPNSAGEFISQHPDISAITFTGESKTGSTIMRAAAEGVKPVSFELGGKNAAVIFADCDFEKMLDGMMRALFLNSGQVCLCSERVYVERPIFDRFCVALAERIKALKVDWPHE... | Function: Involved in the modified meta-cleavage pathway for 2-aminophenol catabolism. The enzyme is also active toward 2-hydroxymuconic 6-semialdehyde, acetaldehyde, propionaldehyde, and butyraldehyde.
Catalytic Activity: 2-aminomuconate 6-semialdehyde + H2O + NAD(+) = (2Z,4E)-2-aminomuconate + 2 H(+) + NADH
Sequence ... |
Q9KWS2 | MVSKADNSAKLVEGKAKPMGSFPHVKRAGDFLFVSGTSSRRPDNTFVGAEPDDTGRPRPNIELQTREVISNIRDILQSVGADLGDVVEVCSYLVNMNDFAAYNKVYAEFFDATGPARTTVAVHQLPHPQLVIEIKVVAYKPL | Function: Involved in the modified meta-cleavage pathway for the 2-aminophenol catabolism. Only active toward 2-aminomuconic acid.
Catalytic Activity: (2Z,4E)-2-aminomuconate + H2O = (3E)-2-oxohex-3-enedioate + NH4(+)
Sequence Mass (Da): 15533
Sequence Length: 142
EC: 3.5.99.5
|
Q9KWS3 | MKISRIAQRLDEAAVSGKATPQLTGDDAVTVREAAEIQRLLIAHRIERGARQVGLKMGFTSRAKMAQMGVSDLIWGRLTSDMWVEEGGEIDLAHYVHPRVEPEICYLLGKRLEGNVTPLEALAAVEAVAPAMEIIDSRYRDFKFSLPDVIADNASSSGFVVGAWHKPETDVSNLGMVMSFDGRAVELGTSAAILGSPIRALVAAARLAAQQGEALEAGSLILAGAATAAVALRPGISVRCEVQNLGSLSFSTTGER | Function: Involved in the modified meta-cleavage pathway for the 2-aminophenol catabolism.
Catalytic Activity: (3E)-2-oxohex-3-enedioate + H(+) = 2-oxopent-4-enoate + CO2
Sequence Mass (Da): 27196
Sequence Length: 256
EC: 4.1.1.77
|
Q9KWS4 | MSEQNAKLAALLNEAELSEKPIEPVRGHIEGGIAQAYAIQQINVQRQLAAGRRVTGRKIGLTSAAVQKQLGVDQPDFGTLFDSMAVNDGEEIAWSRTLQPKCEAEVALVIERDLDHENITLIDLIGATAYALPAIEVVGSRIANWDINILDTVADNASAGLYVLGHTPVKLEGLDLRLAGMVMERAGQQVSLGVGAACLGHPLNAALWLARTLVKQGTPLKSGDVVLSGALGPLVAANPGDVFEARIQGLGSVRACFSPAS | Function: Involved in the modified meta-cleavage pathway for the 2-aminophenol catabolism.
Catalytic Activity: (S)-4-hydroxy-2-oxopentanoate = (2Z)-2-hydroxypenta-2,4-dienoate + H2O
Sequence Mass (Da): 27456
Sequence Length: 261
EC: 4.2.1.80
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Q6UKI2 | MGALGRALLWLQLCALARAAYKLWVPTTDFEAAANWSQNRTPCAGAVVQFPADKAVSVVVRASHGFSDMLLPRDGEFVLASGAGFGAADAGRDPDCGAGAPALFLDPDRFSWHDPRLWRSGDAARGLFSVDAERVPCRHDDVVFPPDASFRVGLGPGARPARVRSVQVLGQTFTRDEDLAAFLASRAGRLRFHGPGALRVGPGACADPSGCVCGDAEVQPWICAALLQPLGGRCPPAACPDALRPEGQCCDLCGAIVSLTHGPTFDIERYRARLLRAFLPQYPGLQAAVSKVRRRPGPHTEVQVVLAETGPQPGGAGRLA... | Function: Membrane-bound component of the endocytic receptor formed by AMN and CUBN. Required for normal CUBN glycosylation and trafficking to the cell surface. The complex formed by AMN and CUBN is required for efficient absorption of vitamin B12. Required for normal CUBN-mediated protein transport in the kidney.
PTM:... |
Q9VPN2 | MGLHWQWLIWALVGLHVALATKWYGGGMDFNDPTAWLDDHLPCAQDLVVFPEYYPALLPLPEDISIDGLVFPREGAILLAEESTITFGSDKQPSCESDENKAYLKPPKSSKWFDPGTWTDKSKEFSTFTPELERIPCDDEQVIIKGHGPLAFDLENVQYLRLGQLILAGSSISKTYLEQLISRDLGQFLFYNAEYVQVEYYRGELCGCHKDFERLLEPVCHNVQEQCETPHCLSPVRPLGSCCLICGAILSTPTTHCTEGSRKELVAQISNLISQESLKDQIGLHVEFVGSQKFGNCLQAVVTDRHKYSERSLEFLQQNE... | Function: Required in the nephrocyte for normal uptake of proteins and elimination of toxins, and for maintenance of endocytic trafficking structures. May function together with Cubn.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 56864
Sequence Length: 505
Subcellular Location: Cell membran... |
Q9BXJ7 | MGVLGRVLLWLQLCALTQAVSKLWVPNTDFDVAANWSQNRTPCAGGAVEFPADKMVSVLVQEGHAVSDMLLPLDGELVLASGAGFGVSDVGSHLDCGAGEPAVFRDSDRFSWHDPHLWRSGDEAPGLFFVDAERVPCRHDDVFFPPSASFRVGLGPGASPVRVRSISALGRTFTRDEDLAVFLASRAGRLRFHGPGALSVGPEDCADPSGCVCGNAEAQPWICAALLQPLGGRCPQAACHSALRPQGQCCDLCGAVVLLTHGPAFDLERYRARILDTFLGLPQYHGLQVAVSKVPRSSRLREADTEIQVVLVENGPETGG... | Function: Membrane-bound component of the endocytic receptor formed by AMN and CUBN . Required for normal CUBN glycosylation and trafficking to the cell surface . The complex formed by AMN and CUBN is required for efficient absorption of vitamin B12 . Required for normal CUBN-mediated protein transport in the kidney (P... |
Q99JB7 | MGALGRVLLWLQLCAMTRAAYKLWVPNTSFDTASNWNQNRTPCAGDAVQFPADKMVSVLVRDSHAISDMLLPLDGELVLASGAALSAAGGDSDPACNPGAPLLFRNPDRFSWLDPHLWSSGTQAPGLFSVDAERVPCSYDDVLFPRDGSFRVALGPGPNPVHVRSVSAVGQTFSRDEDLTAFLASREGRLRFHGSGALRVGSQACTDASGCVCGNAEMLPWICASLLQPLGGRCPQAACQDPLLPQGQCCDLCGAIVSLTHDPTFDLERYRARLLDLFLKQPQYQGLQVAVSKVLRDAHTEIQVVLVETEHATGAAGQLG... | Function: Membrane-bound component of the endocytic receptor formed by AMN and CUBN. Required for normal CUBN glycosylation and trafficking to the cell surface . The complex formed by AMN and CUBN is required for efficient absorption of vitamin B12 (By similarity). Required for normal CUBN-mediated protein transport in... |
Q96565 | MDKISAPFFSGTSPAAASVAGVDEDDRLCFQAQELMFAYNISMVLRAAIQLGLLDALSAAGGKALTPNELVENVETSSNKAEAAAAVDRILRYLSCFNVVTCSSEAAGPDGTLVRRYTTGPLCRWLTKDRGDGTLSPFAVFVVDPDHLFPWHHIAEAVTAGGPSAFERTQKWPYYEYMGKNQRLGTLFDNAMAQHSVILVTKMLERFKGFDGVQRLVDVGGGTGSTLGMITSKYKHMTGINYDLPHVIAQGLPLPGVEHVAGDMYESIPTGDAVLLQWITLMLNDDEFVKILSNCHNALPKDGKVIVVDGILPENPDSSL... | Function: Methylates 3-aminomethylindole (AMI) and N-methyl-3-aminomethylindole (MAMI), two substrates involved in gramine biosynthesis, a toxic indole alkaloid. Can use S-adenosyl-L-methionine (AdoMet) as a methyl donor. Unable to mediate caffeic acid O-methylation.
Catalytic Activity: 3-(aminomethyl)indole + 2 S-aden... |
P0AE13 | MNNKGSGLTPAQALDKLDALYEQSVVALRNAIGNYITSGELPDENARKQGLFVYPSLTVTWDGSTTNPPKTRAFGRFTHAGSYTTTITRPTLFRSYLNEQLTLLYQDYGAHISVQPSQHEIPYPYVIDGSELTLDRSMSAGLTRYFPTTELAQIGDETADGIYHPTEFSPLSHFDARRVDFSLARLRHYTGTPVEHFQPFVLFTNYTRYVDEFVRWGCSQILDPDSPYIALSCAGGNWITAETEAPEEAISDLAWKKHQMPAWHLITADGQGITLVNIGVGPSNAKTICDHLAVLRPDVWLMIGHCGGLRESQAIGDYVL... | Function: Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations.
Catalytic Activity: AMP + H2O = adenine + D-ribose 5-phosphate
Sequence Mass (Da): 53995
Sequence Length: 484
EC: 3.2.2.4
|
Q07121 | MTLNAESEALVGVSHPLDPLSRVEIARAVAILKEGPAAAESFRFISVELREPSKDDLRAGVAVAREADAVLVDRAQARSFEAVVDLEAGTVDSWKLLAENIQPPFMLDEFAECEDACRKDPEVIAALAKRGLTNLDLVCFEPWSVGYFGEDNEGRRLMRALVFVRDEADDSPYAHPIENFIVFYDLNAGKVVRLEDDQAIPVPSARGNYLPKYVGEARTDLKPLNITQPEGASFTVTGNHVTWADWSFRVGFTPREGLVLHQLKFKDQGVDRPVINRASLSEMVVPYGDTAPVQAKKNAFDSGEYNIGNMANSLTLGCDC... | Cofactor: Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity).
Function: The exact function of MaoXI is not known.
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Catalytic Activity: an aliphatic amine + H2O + O2 = an alde... |
Q2YB18 | MKFNIKNGTPEKQRSACVVAGIFEQQKLTPAAEALDKSANGYITGILSRGDMKGKAGATLMLHNVPNSACERVLLVGLGKEQELGDKGYRDAVRAVFKALSDTGAADATLFLLEAPVKNRDLSWKVLQIAVGGLESMYRFDRLKSKVEEAEPKLQKITLGIIKSLTEEEQTASEEALQQGLAVGDGMSLAKDLGNLAPNICTPTYLAEQAMNMAKTYKLKVTVLEQKDMEDLGMGALLAVARGSRQPPKLIALEYWGGAKKGKPVVLVGKGVTFDTGGISLKPAGEMDEMKYDMCGAASVLGTVHAVAKMGLPINVVGII... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q3JEC8 | MNFHVTSGTPEKQRTAALVVGIYEDEKLSSYAQRIDKASEGYVSRLIKQGDFTGKKGQALLLFALPGVKAERVLLMGCGQKDKVTAKNLRQSWSGAVKALQACGATEAMICPLEAKPKDEELTQWARLIVETAEQALYRYEHTKSKKESLKKPLAKLTLLLDQRSQQPLAEQGIQQGQAIAKGVNLARDLGNLPGNICTPTYLADEARRLAKEYKSLKAKILEQAEMEKLGLGALLAVSRGSRQPPKLITLEYKGAPGKQKPIVLVGKGLTFDAGGISIKPGERMDEMKYDMCGGAGVLGTMQACAELELPLNVIAVVPS... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q8Z064 | MAIQLSDKPLLEWAGDTLAIALFEDAVELTGELGSLDEKFAGILKELITEEEFTGKANSTVFTRVSSNIPVRKIILVGLGKTEAFKIETLRRAAAAVGKVGKKQKSKVIGLSFPLWNNDPTASAQAIAEGLQLALYQDNRFKSDPEDKGSQVETVELLGFAGQEAAINRANQIVSGVILARQLVAAPANSVTPITMAETAQQIAQDYGLQIEILEQEDCEKLGMGAFLGVALASDLPPKFIHLTYKPEGTPKRKLAIVGKGLTFDSGGLNIKGAGSGIETMKIDMGGAAATLGAAKAIAQIKPNVEVHFISAVTENMISG... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q6MC72 | MEFALTLHIEKRKKADVLVLPFWKGTSQPEAAIALHPLKLSLDSVFNTGDFKGKEGETLFLYVEGLVEMRVALLGLGEKNKVSTEALRKSYGCLAKACLGKKLKTLNILMPEFNKTEEDAFIKAITEGLLLPNYVYDRLKSKQEEDDEVTLLQKINFISSNKHVLALAEEVAAICDGVYYTRDLINGNADEITPQYLAKCAQGLSQEYPQIKTTVFDKKRLEKEQMGLLLAVNRGSNLDPTLIIMEYKGNPKSKDHTVIIGKGVTYDTGGLNIKPTGGIETMKCDMSGGAACFGTMLAACHLDLKVNLTAIIPATENSVD... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
C0QSL9 | MNIKITSGHLKNARVRAVISFSFKEDRKLSPEIEDLDRILDGAISQLKREQKFDGSDGKILVVPTFGKGKMDYVILIGAGSRRKADLDKVRRLGNISVKTTKKLKIDRFLIDAEPLSVIKEGEDSIAQAVVEGVILGNYRFDKYLSKKDEYRIKELQIRVKRRFKNKAEQSVKVGKILAESQNFTRDIVNEPGNVITPEKLAQIAQDLAREYGFEVKIYDEEEIEKMGMNAYLAVAKGSANPPRFIHIIYRPEKPKKKIALIGKGLTFDSGGLNIKPGDYMRWMKADKSGACAVLGIFKAIGQLKPDVEVHGIIAAAENM... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q73QZ3 | MKFNIAKKGGVVAQLVFEEKIEGGYLNHLKEKELFSGKAEDVYYTLDSNLKAQLFIGLGKEEKIDLEVLRKTFFKAASELLKNKVEEVELNIPKLNNLCNYKTAEAIAEGMLHATYKYDKFKSDRKEQTEITVNYNPEKGKEDRAEKGINEAVKLMEAVFLTRDLVNQPANVIYPETLAKIAKEKLEAKGVKVTVHGKKEIEALKMEAFLNVARASTKEPKLIVMEYYNNPGSNEKIALVGKGLTYDSGGYAIKPATSMVDMFTDMGGSGTVIGAMHALADLKAKVNVVAVVASCENMISGDGYRNGDIIGSMSGKTIEI... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q83I32 | MSDYTNTVTVEITSDDSLVADVIVVPVASGAVPRLPEDSKFRAYEDILQKLGVTGSKDELTRIPLDGSKHVVLAFIGVGKAFSATELMFAAGSAVRQIGARCIQIDFSVTQKDKLSAIVEGAFLGAYRFDKYRSKKSECPEVIRVSHNINGITDSECRQIIARAKVIAGSVGLAKDLVNTTGDDLYPAQFASFVAKDLEGIDHISVESWDEKRLQEKSCGGILGVGRGSNFPPRLVKISYTPGQYKKHLSLVGKGITFDTGGLSLKPASAMLGMKYDMTGAANVFAVLRIVALLRLSVRVTGWLCLAENMLSGSAIRPGD... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
A5CXK2 | MKFTLINEIIQHFKGDAVVVFSNSNTVFNDDNIQQLIKLNHFDSKPGKVLLLNLVSGFKSKQVIVSGLGDAPISAKNYVKALNAVIVILVEIKAKNLMVQHVGIKGFNELWVHEITAKVMCNATYKVQKVGNYKKQNSGIERITIQSTMDSVYGLMKGQAIADGMSLTRHLGDLPSNVCTPSYLAGTAISLAQEFNLECEVLEEVDMEKLGMGSLLAVSKGSSEPPKLISLSYRGNGNEKPIVLVGKGVTFDSGGISLKPGTGMDEMKYDMCGAASVLGVMRVIAQIKPNINLVVVLPAVENMPAHNASKPGDVVKSMSG... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q8D295 | MKFSIADKSIKQTKDILLILGIFYKDCYQKTLKYISDENKKNIIQVVKNIKIKDNIGSTYFISNTNKVGSNPILLIMLGSKVNINSRIYKKLIINTISSIKNIKYKKSIFFLLNLNFNNSNLYWKIRRSIEYIYESLYEFNNFKSKTKSYKIYMKEIMFYIHDENEIKQANIAISHSVSISKGIIITKNLGNMPSNFCDPHYLSHQSYILKDKYSEKISVEIMDHKKIKNIGMNAYLHVSKGSSKNPYLSIIKYNENKFNGKSPIILIGKGLTFDSGGISIKPSNNMDEMKFDMCGAAAVLGVMHAISELNLNLYVIGIL... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
C5K105 | MGPVDTSQRLARLRELMQERKVDVYIVPSEDSHQSEYIAPCDGRREFISGFTGSAGCAIVSMSKAALSTDGRYFNQAAKQLDNNWMLLKRGFENMPTWQEWTAEQAEGGKVVGVDPSLITASEARSLSETIEKSGGSLQGVQENLIDLVWGKKRPARPSEKVALHPIEFAGKSFEEKISDLRKELQKKKSAGFVISMLDEIAWLFNLRGNDIPYNPVFFAYAIITPTTADLYIDDEKLPAEVKKYLGDQVSVKPYGSIFEDAKALSQSAQKKSDGDASTSPSEKFLISTKASWSLSLALGGEKNVEEVRSPITDAKAIKN... | 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): 68558
Sequence Le... |
Q2H8T2 | METVNTTARLTTLRSLMKENGVDIYGIIVPSEDSHASEYIAPCDGRRAFISGFTGSAGTAVVTQDKAALATDGRYFNQAGKQLDGNWHLLKTGLQDVPTWQDWTAEASAGGKTVGVDPSLISSPIAEKLDESIKKSGGAGLKAVSENLVDPVWGSDRPARSSNPVKLLIGKYSGKDTAAKLTELRKELEKKKAAAFVLSMLDEVAWLFNLRGSDITYNPVFYSYAIVTQDSATLYVDVSKLDDESRSYLDQNKVTIKPYDTLFEDAKALASAAEAKGTSEAPRKYFVSNKGSWALKLALGGDKFVEEVRSPVGDAKAVKN... | 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): 68186
Sequence Le... |
A8P5H7 | MGARGNHTVDTSKQLAALRELMKKENVDVWVVPSEDQHYSEYLAHCDERRAFISGFNGSAGCAVITLDKAYLFTDGRYFLQAEKQLDSNWTLMKQGLPDVPTWQDFLHKTLDGSLKIGIDATIITEEDAAGLRKNLAPKKSELVPSKKNLVDIVWGSERPARPQNPVFHLDEKYSGQSFKEKVKKVREEIAKEKGKAFVVTMLDEVAWLFNLRGSDIDYNPVFFAYAVVTPDEVVLFINEKQLDDAARDYLGQDVKIRGYDELYDYLKELPKSLSLTGDKDGEKILVTSRTSLAITETITPPSSPESTTFHKVVRSPVGD... | 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): 69966
Sequence Le... |
Q5AVF0 | MLFSRPPARLSWILAFQPSQKLPRYSPRFFSISVSRFAIDMEAVDTTKRLSSLRQLMREHKVDVYIVPSEDSHQSEYIAPCDGRREFISGFSGSAGTAIISLNEAALSTDGRYFNQAAKQLDNNWTLLKRGVEGVPTSQEWITQQAEGGKVVGVDPALITGAAARSLSDALQKSGASLIGVSQNLVDLVWGNDRPAPPREKVRVHPEKYAGKSFQEKVSDLRKELENKKAAGFVISMLDEIAWLLNLRGSDIPYNPVFISYCIVTPTKVELYIDDEKLTPEVKAHLGDDVIIKPYDSIFADAKALFEAKKKDPDAPSSKF... | 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): 72691
Sequence Le... |
Q3IP82 | MELTVEPIDIGTERPVVLLNCADAETLGVHSLDRVEIDWDGTTEVGIVKVTDELVAAGRIGASHGFPEITDGTVVAVTPAGQPESVESIRRKLDGRELDSDELGAIVADIEADRLSDLELSAYVCASHANGLSLEETKQLTERMAEVGKQLSWEQPVVADKHSIGGVAGNRVTPVVVAIVAAAGLTIPKTSSRAVTSPAGTADTMEVFCPVEFSREEIRDIVTETGGCLVWGGAVDLSPVDDKVIRAQRPLSLDPPGQVIASVLSKKQSAGSSHIVVDIPYGAGAKVTSLSEARDLADDFRRVGDHLGLTIECALTRGSD... | Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Catalytic Activity: AMP + phosphate = adenine + alpha-... |
Q5JCX3 | MKAKIRILDMFSGRYTVLINEEDAKEAKLHPDDLVKIEAGKKAVYGSVALSNLVGKGEVGISRDVLDLHNFSEGETVSVIPAGTPESVRYIKKKMHGEKLRKVEIEAIVRDIVDRKLRDIEISSFVTALEINGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFADVSFSLDEIKRIVEKVGACLVWGGALNLAPADDITIKAERALSIDPTGLMLASIMSKKYAMGSQYVLIDIPTGKGVKVETVEEARSLARDFIELGKRLGQYVEVAITYG... | Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP, dCMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Catalytic Activity: AMP + phosphate = adenine + ... |
A1RWC3 | MKLKTRILPFESAHYTVVLDQSVAKKLDVRPSDRVLVRFNGKTVVAIANIAKEFSHEHVGVYVNIAKALGISDGDEVEVEATSPPASLQAIRKKLQGLSLESDEIYQVVKDIVDGKLSELELAAFVTAVHFQGMTPSEIYSFTLSMVETGQRLRLKRKPILDKHSLGGVPGDKTSLLVVPIIASLGFTIPKTSSRAITSAAGTADRMEVLAPVNLSIDEIERIVEKTNACLVWGGALNLAPADDIIIRVEYPLGIDPFYIPSILAKKLAVGSTHVVLDVPTGRGTKVKTLEEAKRISQSFFEIARMFGMNLQAVATYAEE... | Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Catalytic Activity: AMP + phosphate = adenine + alpha-... |
P15034 | MSEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSEYPYRQNSDFWYFTGFNEPEAVLVLIKSDDTHNHSVLFNRVRDLTAEIWFGRRLGQDAAPEKLGVDRALAFSEINQQLYQLLNGLDVVYHAQGEYAYADVIVNSALEKLRKGSRQNLTAPATMIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAMEKCRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENECEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTQAQREIYDIVLESLETSLRLYRPGTSILEVTGEVVR... | 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): 49815
Sequence Length: 441
Subcellular Location: Cytoplasm
EC: 3.4.11.9
|
P44881 | MELAYMAKLPKEEFEERRTRVFAQMQPNSALLLFSEIEKRRNNDCTYPFRQDSYFWYLTGFNEPNAALLLLKTEQVEKAIIFLRPRDPLLETWNGRRLGVERAPQQLNVNEAYSIEEFATVLPKILKNLTALYHVPEIHTWGDTLVSESAVNFSEILDWRPMLSEMRLIKSPNEIRLMQQAGQITALGHIKAMQTTRPNRFEYEIESDILHEFNRHCARFPSYNSIVAGGSNACILHYTENDRPLNDGDLVLIDAGCEFAMYAGDITRTFPVNGKFSQPQREIYELVLKAQKRAIELLVPGNSIKQANDEVIRIKTQGLV... | 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): 49261
Sequence Length: 430
EC: 3.4.11.9
|
P47566 | MISELQQKITVLKDLLKTNKADAILIGSDQNRFWLTNFPSSAGWLIITSNKAKLFIDGRYYEAARNFINPIVEVELFVSFKQVKAFCESNGINHLLIEGDYLTFNYQDWIQAICKQYTVINAQEIRRVKLPSEIQAIEKAVDITRKVAVKLKRFIKPKMTELFISQWITNELVKQGGAKNSFDPIVATGKNGANPHHKPTKTIVKEGDFITCDFGTIYNGYCSDITRTFLVGKKPKSAKLLSAYKKVEEANLAGINAVNTTLTGSQVDKVCRDIIENSEFKDFFVHSTGHGVGIDIHEMPNVSQSYNKLLCENGVVTIEP... | 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): 39815
Sequence Length: 354
EC: 3.4.11.9
|
A0A144A2H0 | MQLNFLLFVFIFLMVFHLNIFNKGKRQNLVSAYLNHFKKSYFSGVTSGSDCVNKSEVSSDNNNNNNNNNNKIAHNFFSKKYQRNFENNNLSENQENNKNIIYSGSNIFKNIYNTEMMSNNNTVDVNMMDNNPAARLEELRTIMKKNKIDVYILINSDEHNSEIINEKDKKIVKITNYSGADGILIVTKDKPILYVNALYELQAMNELDQNLFTLRISRIDNRDEIFETISSLEFNTIAFDGKNTSVVFYEKLRKALLNAYPKKKIVEKIIYNNNFDDVNKKDDENVLNFLVLEKSLVEIKDYPVNNKTLYIHDRKYNGAC... | Cofactor: Binds 2 Mn(2+) ions per subunit.
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides . In the food vacuole, involved in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides . In the cytoplasm, may be involved in the last steps of... |
Q6Q4G3 | MGPPSSSGFYVSRAVALLLAGLVAALLLALAVLAALYGHCERVPPSELPGLRDLEAESSPPLRQKPTPTPKPSSARELAVTTTPSNWRPPGPWDQLRLPPWLVPLHYDLELWPQLRPDELPAGSLPFTGRVNITVRCTVATSRLLLHSLFQDCERAEVRGPLSPGTGNATVGRVPVDDVWFALDTEYMVLELSEPLKPGSSYELQLSFSGLVKEDLREGLFLNVYTDQGERRALLASQLEPTFARYVFPCFDEPALKATFNITMIHHPSYVALSNMPKLGQSEKEDVNGSKWTVTTFSTTPHMPTYLVAFVICDYDHVNR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA.... |
Q2KHK3 | MSRPFSSGVYVSRGVALLLAALTAVLLLVLVALASLYGSCAHVQPSEQGNSRVKNTSLWPPGGQEWALPTPAQEPTVGTSQDLGPPSGPWDHLRLPPWLVPLHYDLELWPWLQPDKLSPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVWGPLAQDTRNATVGRVQVEKVWFAPDMQFVVLDLGQSLEPGSRYELSFHFSGQVLQVGLEGLFLNLYHDEDELRALVATQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALSNMPQLGQSERIDVNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRTER... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA.... |
P06547 | MLHSQKRIWKKIGLCLLSFILGITVFTGSFGSKAEAAVAGDFQVSVMGPLAKVTDWNSFKNQLTTLKNNGVYAITTDVWWGYVESAGDNQFDWSYYKTYADTVKQAGLKWVPIISTHRCGGNVGDDCNIPLPSWLWSKGSADEMQFKDESGYVNNESLSPFWSGVGKQYDELYASFAQNFSAYKDMIPKIYLSGGPSGELRYPSYYPAAGWSYPARGKFQVYTETAKSAFRTAMTTKYGSLDKINAAWGTNLTSMSQISPPTDSDGFYTGGGYNITYGKDFLSWYQSVLENHLGVIGAAAHKNFDPVFGVRIGAKISGIH... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
Sequence Mass (Da): 62899
Sequence Length: 575
EC: 3.2.1.2
|
P19584 | MIGAFKRLGQKLFLTLLTASLIFASSIVTANASIAPNFKVFVMGPLEKVTDFNAFKDQLITLKNNGVYGITTDIWWGYVENAGENQFDWSYYKTYADTVRAAGLKWVPIMSTHACGGNVGDTVNIPIPSWVWTKDTQDNMQYKDEAGNWDNEAVSPWYSGLTQLYNEFYSSFASNFSSYKDIITKIYISGGPSGELRYPSYNPSHGWTYPGRGSLQCYSKAAITSFQNAMKSKYGTIAAVNSAWGTSLTDFSQISPPTDGDNFFTNGYKTTYGNDFLTWYQSVLTNELANIASVAHSCFDPVFNVPIGAKIAGVHWLYNS... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
Sequence Mass (Da): 60548
Sequence Length: 551
EC: 3.2.1.2
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Q0JMV4 | MQVPIEHNGGEQTLLVPFRAHRPPRPLLQLGSRASPVSGFQLGVVEGEWRVVQPAYGQARWTTSPPPASPTSGSLRRPTLSASKATCWGGCTIWTRPIIEAFHGKGVQVIADIVINHRTAEHKDSRGIYCRLPPRLGPAHDLPRRPLRRRHRKPGHRRRTSTTSTSASSGSSSAGSTGSRWTSASTRGASTSPRATPPTWQRSTSMPPSRASPWPRYGRRWRTAGTASRTTTRTRTGRSWSTGSIVSAAPTAMPRRSTSPPRASSTSPWRAIELWRLRGEDGKAPGMIGWWPAKATTFVDNHDTGNPCIFYDHFFDWGLK... | Cofactor: Binds 3 Ca(2+) ions per subunit.
Function: Important for breakdown of endosperm starch during germination.
Catalytic Activity: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Sequence Mass (Da): 38478
Sequence Length: 348
EC... |
P37729 | MRKVHVQKYLLTFLGIVLSLLWISPFYIILVNSFKTKLELFTNTLSLPKSLMLDNYKTAAANLNLSEAFSNTLIITVFSILIIAIFSSMTAYALQRVKRKSSVIIYMIFTVAMLIPFQSVMIPLVAEFGKFHFLTRSGLVFMYLGFGSSLGVFLYYGALKGIPTSLDEAALIDGCSRFRIYWNIILPLLNPTTITLAVLDIMWIWNDYLLPSLVINKVGSRTLPLMIFYFFSQYTKQWNLGMAGLTIAILPVVIFYFLAQRKLVTAIIAGAVKQ | 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): 30994
Sequence Length: 274
Subcellular Location: Cell membrane
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I1BYW6 | MFIGYLLLILAIFGFYYSIQQINGSSIFKKKNLLDDWISKQNTISFNSILKNINPSGTPRGFVAASLSTSYPDYFYTWTRDAALVVRVLSDLPETDDDVLKDYIDFQIHIQNTPTVCHCLGEPKFNPDGTGYTGSWGRPQNDGPAERAITFIKIANRLKNSAYVSQKIVPALEKDLDYILQVWEQPCFDLWEEVDGVHFYTLMAMQRALLDAFDFFNLSKYRSTAYRIQEKIERFWSSEENYIRVTHEVREGANKPSGLDVSVLMAANMFATTREGFFTPGSDKVLATAAAIEKSFSSIYPINKNLQPDLGVAIGRYPED... | Function: Consecutively hydrolyzes alpha(1-4) glycosidic bonds from the non-reducing ends of starch, resulting in the production of glucose. It also has a limited ability to produce glucose through the hydrolysis of amylopectin alpha(1-6) linkages.
Catalytic Activity: Hydrolysis of terminal (1->4)-linked alpha-D-glucos... |
Q9V895 | MEKRIELERRARKVNQITELNLDNCRSTSIVGLTDEYTALESLSLINVGLTTLKGFPKLPNLKKLELSDNRISSGLNYLTTSPKLQYLNLSGNKIKDLETLKPLEEFKNLVVLDLFNNDATQVDNYREKIFKMLPSLNFLDGFDCNDEEVQSDGDDDDEVNGNDSDEVGVSDEDDDSDDSDEEANGEVSLSEVYNDDLEEDNSDWEGEDEAGEEDEEEDSDIDDADGDANESAASVNAKDKDGEKEADESQVRGKKRKHDG | Function: Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability, and inhibition of acetyltransferase... |
P39687 | MEMGRRIHLELRNRTPSDVKELVLDNSRSNEGKLEGLTDEFEELEFLSTINVGLTSIANLPKLNKLKKLELSDNRVSGGLEVLAEKCPNLTHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLDGYDRDDKEAPDSDAEGYVEGLDDEEEDEDEEEYDEDAQVVEDEEDEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEELGEEERGQKRKREPEDEGEDDD | Function: Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription . Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation . In addition, plays a role in the modulation of hi... |
P49911 | MEMDKRIYLELRNRTPSDVKELVLDNCRSIEGKIEGLTDEFEELEFLSTINVGLTSISNLPKLNKLKKLELSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNAYRENVFKLLPQVMYLDGYDRDNKEAPDSDVEGYVEDDDEEDEDEEEYDEYAQLVEDEEEEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEDAAEEEGSQKRKREPDDEGQEDD | Function: Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription. Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation. In addition, plays a role in the modulation of hist... |
Q3SZC6 | MDMKRRIHLELRNRTPAAVRELVLDNCKSNDGKIEGLTAEFVNLEFLSLINVGLISVSNLPKLPKLKKLELSDNRICGGLDMLAEKLPNLTHLNLSGNKLKDISTLEPLKKLECLKSLDLFNCEVTNLNDYRESVFKLLPQLTYLDGYDREDREAPDSDAEVDGVDEEEDDEEGEDEDKEEDEDGEEEEFDDEEDDDEDEDVEGEEDEDEVSGEEEEFGHDGEVDEDDEDEDEDEDEDEEEEESGKGEKRKRETDDEGEDD | Function: Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription. Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative... |
Q92688 | MDMKRRIHLELRNRTPAAVRELVLDNCKSNDGKIEGLTAEFVNLEFLSLINVGLISVSNLPKLPKLKKLELSENRIFGGLDMLAEKLPNLTHLNLSGNKLKDISTLEPLKKLECLKSLDLFNCEVTNLNDYRESVFKLLPQLTYLDGYDREDQEAPDSDAEVDGVDEEEEDEEGEDEEDEDDEDGEEEEFDEEDDEDEDVEGDEDDDEVSEEEEEFGLDEEDEDEDEDEEEEEGGKGEKRKRETDDEGEDD | Function: Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription . Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negativ... |
Q6A1I3 | MDMKRRIHLELRNRTPAAVRELVLDNCKSNDGKIEGLTAEFVNLEFLSLINVGLISVSNLPKLPKLKKLELSDNRICGGLDMLAEKLPNLTHLNLSGNKLKDIGTLEPLKKLECLKSLDLFNCEVTNLNDYRESVFKLLPQLTYLDGYDREDREAPDSDAEVDGVDEEEDDEEGENEDKEEDEDGEEEEFDDEEDDDEDEDVEGEEDEDKVSGEEEEFGHDGEADEDDEDEDEDEDEDEEEEESGKGEGRKRETDDEGEDD | Function: Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity. Exhibits histone chaperone properties... |
Q6P1U7 | MEMKKRLMLELRNRKAADVKELVLDNCRSDDGKIIGLTSEFENLEFLSMINVNLLSVANLPKLPKLKKLELSDNRISGGLEVLAERTPNLTHLNLSGNKIKEINTLEPLKKLPHLMSLDLFNCEVTMLNNYRESVFELLPQLTFLDGFDADDQEAPDSDPEAEDLEENGEDGEDDEEDEEEFEDELDDEEDDEEGEDEEGEEEEEGDEEDEDDEDVPQGEKRKRDLEDDGDEEDDDDEEDDE | Function: Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity. Exhibits histone chaperone properties... |
Q5F4A3 | MEMKKRINLELRNQAPEEVTELVLDNCKSSNGEIEGLNDSFKELEFLSMANVQLTSLAKLPTLSKLRKLELSDNIISGGLEVLAERCPNLTYLNLSGNKIKDLGTVEALQNLKNLKSLDLFNCEITNLEDYRDSIFDLLQQITYLDGFDQEDNEAPDSEDDDDEGDEDDNDEDEDEAGPPGEYEEEDDEDDGGSDLGEGEEEEEVGLSYLMKEEIQDEDDDDDYVEEGGDEEEEAEGIRGEKRKRDPEDEGEEEDD | Function: Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1 from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the nucleosome. May stabilize the evicted H2A.Z... |
P03950 | MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP | Function: Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs) . Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the... |
P31346 | KDEDRYTHFLTQHYDAKPKGRDGRYCESIMKQRGLTRPCKEVNTFIHGTRNDIKAICNDKNGEPYNNFRRSKSPFQITTCKHKGGSNRPPCGYRATAGFRTIAVACENGLPVHFDESFIITSQ | Function: Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs) (By similarity). Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and tran... |
P31347 | QDDSRYKHFLTQHYDAKPFGRNDRYCETMMKRRDLTSPCKDTNTFVHGNKGSIKDVCEDKNGKPYGKNFRISKSSFQVTTCKHVGGSPWPPCRYRATSGSRNIVIACENGLPVHFDESVFQQKVH | Function: Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs) (By similarity). Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and tran... |
Q9UKU9 | MRPLCVTCWWLGLLAAMGAVAGQEDGFEGTEEGSPREFIYLNRYKRAGESQDKCTYTFIVPQQRVTGAICVNSKEPEVLLENRVHKQELELLNNELLKQKRQIETLQQLVEVDGGIVSEVKLLRKESRNMNSRVTQLYMQLLHEIIRKRDNALELSQLENRILNQTADMLQLASKYKDLEHKYQHLATLAHNQSEIIAQLEEHCQRVPSARPVPQPPPAAPPRVYQPPTYNRIINQISTNEIQSDQNLKVLPPPLPTMPTLTSLPSSTDKPSGPWRDCLQALEDGHDTSSIYLVKPENTNRLMQVWCDQRHDPGGWTVIQ... | Function: Induces sprouting in endothelial cells through an autocrine and paracrine action.
PTM: N-glycosylated.
Sequence Mass (Da): 57104
Sequence Length: 493
Subcellular Location: Secreted
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A2Z0C0 | MDQRKGSGSDANGGLAEATASRLRFEDPDEVMEENPAAAAATVGAEEEGGEGGGGEEVIGSDKTSADYYFDSYSHFGIHEEMLKDVVRTKSYQNVITQNSFLFKDKIVLDVGAGTGILSLFCAKAGAKHVYAIECSQMADMAKEIVKTNGYSNVITVIKGKVEEIELPVPKVDVIISEWMGYFLLFENMLNTVLYARDKWLADGGVVLPDKASLHLTAIEDAEYKEDKIEFWNNVYGFDMRCIKKQAMMEPLVDTVDANQIVTNCQLLKTMDISKMTPGDASFTVPFKLVAERNDYIHALVAYFNVSFTKCHKMMGFSTG... | Function: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (can methylate histones).
Sequence Mass (Da): 43014
Sequence Length: 387
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q63009 | MAAAEAANCIMEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMR... | Function: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, FMR1, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP and MAP3K5/ASK1 . Constitutes the ma... |
Q9URX7 | MPGNTKKSADSGLTAKDYYFDSYSHWGIHEEMLKDDVRTLSYRDAIMQNPHLFRDKIVLDVGCGTGILSMFCARAGAKHVYGVDMSEIIHKAVQIVEVNKLSDRITLIQGKMEEIQLPVEKVDIIVSEWMGYFLLYESMLDTVLVARDRYLAPDGLLFPDRAQIQLAAIEDADYKSEKIGFWDDVYGFDFSPIKKDVWKEPLVDTVDRIAVNTNSCVILDLDLKTVKKEDLAFSSPFEITATRNDFVHAFLAWFDIEFSACHKPIKFSTGPFSRYTHWKQTVFYTHKDLTVKAGEYIRGTITCKPAEGNHRELDIDISYT... | Function: S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that catalyzes both the mono- and asymmetric (type I) dimethylation of the guanidino nitrogens of arginine residues in target proteins (By similarity). Asymmetrically dimethylates the polyadenylate-binding protein pab2, modulating pab2 oli... |
Q54HI0 | MTDDYSKLKSEIMDLVSEEFLKTKDDIISVMIENNKLKRAELVVGNDSLPPPPPTPSIVKIEHTTTTSNIDDLPLPPPIQEVEEEEPTQQNIEQQQQTQDESDDYYKTVHPLGVQDTYEDEEYFSSYSKISLHHEMVFDKRRTAAYYHAISKSKNIFKDKVVLDVGCGTGILSCFVAKAGAKKVYAVDASDMAHRAELIVQQNGLADIVTVFKGKLEHIAFPEYVDVIVSEWQGAFLIFESMIESVIYARDNLMRPGGIILPSKASIYLSPINVDSFYNQYINQWSNVFNLDMSPLIPFAQEELLEEKTIRNYYVDNQDS... | Function: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in some proteins such as histones.
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 58871
Sequen... |
P55345 | MATSGDCPRSESQGEEPAECSEAGLLQEGVQPEEFVAIADYAATDETQLSFLRGEKILILRQTTADWWWGERAGCCGYIPANHVGKHVDEYDPEDTWQDEEYFGSYGTLKLHLEMLADQPRTTKYHSVILQNKESLTDKVILDVGCGTGIISLFCAHYARPRAVYAVEASEMAQHTGQLVLQNGFADIITVYQQKVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDAWLKEDGVIWPTMAALHLVPCSADKDYRSKVLFWDNAYEFNLSALKSLAVKEFFSKPKYNHILKPEDCLSEPCTILQLDMRTVQISDLE... | Function: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation... |
Q9R144 | MEAPGEGPCSESQVIPVLEEDPVDYGCEMQLLQDGAQLQLQLQPEEFVAIADYTATDETQLSFLRGEKILILRQTTADWWWGERAGCCGYIPANHLGKQLEEYDPEDTWQDEEYFDSYGTLKLHLEMLADQPRTTKYHSVILQNKESLKDKVILDVGCGTGIISLFCAHHARPKAVYAVEASDMAQHTSQLVLQNGFADTITVFQQKVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDTWLKGDGIIWPTTAALHLVPCSAEKDYHSKVLFWDNAYEFNLSALKSLAIKEFFSRPKSNHILKPEDCLSEPCTILQ... | Function: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. May inhibit NF-kappa-B transcription, and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). Has a negative regulation effect on G1 to S trans... |
D9IVE5 | MESSSECSSISDFQDSTEGDDANTLPENLCMREYVVICDYVATDNTQLSLCSGDKVLLLNAVSQDWWWVNHNGTCGYVPASHLHDALNEQEDTEVNDPWQDEEYYGSYKTLKLHLEMLSDVPRTMTYQNVILKNSSSLCGKHILDLGCGTGIISFFCAKFAQPEAVYAVEASKIAEQTCRLVEQNGISSLVHVIRQQAEELDLPTKVDVLVSEWMGTCLLFEFMLESVLQARDRWLKEDGVMWPSTACIHLVPCSAYKEYSNKVLFWDNPYQLDFSLLKPPATKEFFAKPQPDYILQPEDCLSEPCTLFHLNLKTLQVAE... | Function: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as histones. Involved in growth regulation (By similarity). Involved in embryonic dorsal development.
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethy... |
B3DLB3 | MSTSGCSSEKSDFQDSTEGEEEEDTQSENLCMREYVVIRDYMAADATQLSLCFGDKVLLLSAVTQDWWWVKHNGICGYVPASYLHDALNDQEDTEVDDPWQDEEYYGSYKTLKLHLEMLSDVPRTTAYKEVILRNSSSLCGKHILDLGCGTGIISFFCAKLAQPEAVYAVEASEIAEQTRRLVKQNGISNLVHVIRQRAEELQLPTKVDILVSEWMGTCLLFEFMLESVLQARDRWLKEDGVMWPSTACIHLVPCSASKEYANKVLFWDNPYQLDFSLLKPLAAKEFFARPKPDYVLQPEDCLSEPCILLHLNLKTLQLA... | Function: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as histones. Involved in growth regulation. Involved in embryonic dorsal development.
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[pro... |
Q0WVD6 | MAATMVKHEILNYSEDEEENYSDEGDWGDWKADDNGIEGGEEEEEDDGDDSESDFLCLFCDSHFVSCDLLFEHCRLSHGFDFHGVRKELKLDFYSSFKLINYIRSQVAENMCFSWKIEADDYKDVKFPWDEEKYLKPFWQEDSLLYSFADDEEDEEVTFDREEVMEELQKLGDLSIDVEALGESSMSNSDKCNINGSKDVTSLSNCNGLKQSSADDLIVNGKDAEPKVCDGRLVNRNIRKVNENYFGSYSSFGIHREMLSDKVRTEAYRDALLKNPTLLNGSVVMDVGCGTGILSLFAAKAGASRVVAVEASEKMAKVAT... | Function: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.
Sequence Mass (Da): 67344
Sequence Length: 601
Domain: The zinc-finger is responsible for substrate specificity.
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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O60678 | MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPV... | Function: Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (Probable). May regulate retinoic acid synthesis and signaling by inhibi... |
A3BMN9 | MATREHELRPEQERLGEDREEYEDGEEEEEEGEEGWDDWESDGDDAGGGGGGGGLLCLFCSARFDSESSLFSHCASEHRFDFYRVVKETGMDFYGCIKLINFVRSKVAENKCWSCGQVFSSNSELCGHLHALEIPQLEGKVPWGDDVYLKPFLEDDSLLHSLSVFDDDDEDDCGMPMEKGGCSAGNGSLAETCESNLKSIINDGSDVIDRFERTCTIESTDGECSGSLAQEPSDKQLKIARASAAARGIKSVDESYFGSYSSFGIHREMLGDKVRTEAYRDALLGNPSLMNGATVLDVGCGTGILSLFAAKAGASRVIAV... | Function: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.
Sequence Mass (Da): 67943
Sequence Length: 620
Domain: The zinc-finger is responsible for substrate specificity.
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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O70467 | MCSLAAGNGQGAELGPEPLELSDSGDDAGWEDEDADAEPAQGRQHTPCLFCDRLFRSAEETFSHCKLEHQFNIDGMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWDKDEYLKPVLEDDLLLQFDVEDLYEPVSAPFTYPNGLSENTSAVEKLKLMEARALSAEAALARAREDLQKMKQFAQDFVMNVDVRTCSSTTTIADLQEDEDGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKV... | Function: Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases . May regulate retinoic acid synthesis and signaling by inhibiting ALDH1... |
O13648 | MLVKPMACYFEIWTRKVTTIEDFSLAIANRFKQMGSHSDSEVDWDNEEEVWEDEVHEFCCLFCDSTFTCLKDLWSHCKEAHNFDFYQVKQQNNLDFYACIKLVNYIRSQVKEGKTPDLDKLSDILRSDEYMISVLPDDSVLFSLGDELDSDFEDDNTLEIEVENPADVSKDAEIKKLKLQNQLLISQLEEIRKDKMNELTSQTTDQLSVTPKKADNDSYYFESYAGNDIHFLMLNDSVRTEGYRDFVYHNKHIFAGKTVLDVGCGTGILSMFCAKAGAKKVYAVDNSDIIQMAISNAFENGLADQITFIRGKIEDISLPV... | Function: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in ribosomal protein rps2.
Sequence Mass (Da): 61761
Sequence Length: 543
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P46580 | MSNRTYADNLFPQQVAEQHEEQMSSGSSPKSNSPSRSISSVEAANSRIHIGWMATTLDVAENLDRHVATFCTRLGEFKYNFVVYPIGGVVRAFWTPNGSAENHPPVIDLPDVQLRNDLWESYVVGKISPWIDCDSSDPAFASLSEEHLLKELSYICYLGLQTMAIELTRISSPRTAAILKKWIWTRNSRFTVWVQLPSAIEKCKDYDAFTIEHVDLWTIWADFRKNCGNFSGVYFQVALTISSELPDELTELKLVDRWKAEPLAAFVIESGLFISGRNGEASIPSAHINLLKHLWTTDALRIVLRATTDTFKYNTSIKSE... | Function: Catalyzes the symmetrical dimethylation of arginine residues in targets such as small nuclear ribonucleoproteins, histone H2A/H4 and cbp-1 . Dimethylation occurs in a distributive manner where the protein is released after the addition of the first methyl group prior to rebinding for the addition of the secon... |
Q54KI3 | MINSAQYEFSCGVELESVDIQLDIERAYDLEYQFIMTSISHPRFNRDFTKASIGNSFSNKVAFTRSDTLLQSNYWRSSIVGKTSTNGIDLDSIDPTIRSNSVKTLKQEISWAAHLSLPSILLPTPSFNSTNYAQVVNQSLQSLSYMKVWIRIPLVSPKSQLLNKFDYYQDHNTSGGSGNNLVDNDNPWEWWNNFRLLCNQHPNLSAVLEMTSDLPSKEQLQQWLGEPVKCVIIPTSVFLTNKAGFPTLSKAHQQFLLQLFNYNIQFVVSGASMDTLKDYKTYLKFLHTNQNPLTQEEYFEMPYLDFLQAPLQPLMDNLES... | Function: Methylates arginine residues in proteins such as small nuclear ribonucleoproteins or histone H2A/H4.
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 73499
Sequence Length: 642
EC: 2... |
Q82UQ3 | MYYVGIMSGTSLDGIDAVLVDFSGPSFSLLHTCYIPYDQSLRAALLGLNQAGENELHRAAILSNQLSGWYAQAVGRLLEKSGIDPGEIIAVGCHGQTIRHCPQPENGYSIQLVNGALLAELTGMTVVTDFRSRDIAAGGQGAPLVPAFHHEMFAHRDIHRLIINIGGITNITSLPVSGGVNGFDCGPGNMLMDAWCLKHTGMTYDHNGSWAESGRVINPLLENLLNFPYFSLPPPKSTGREMFSLDWLQPCLRGDEATQDVQSTLLQLTVRTITDSVETYYPAVRELYLCGGGAHNGTLVTRLQQQLPGRRINLTDALGI... | 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 ... |
Q3JCM5 | MAQRYIGLLSGTSMDAVDAALVELEPLRILATHSIPISLALRQQLFAVIERSTTSLGELGALDIRLGRLFAETALELLAKAKCSVTEVQAIGSHGQTIYHWARGPDPFTLQLADPNTIAEITGITTIADFRRRDLAAGGQGAPLAPAFHAAFLRSPHYHRAVLNIGGIANISFLPADHRTPIWGFDTGPGNTLMDGWISRHLNQSIDREGRWAASGRVNKTLLRYLLTDPYFSLPPPKSTGREYFNLVWLDHILSKTGIKLSPPDVQATLCALTIASVKLAIQSSSPHTEELLICGGGANNETLMEGLRKQLAFCRVTTT... | 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 ... |
Q9CK07 | MKEATMYYIGVMSGTSLDGVDLALMDFSCAQPQLIHADFYPMPPAIRQQISTLCNSGTTTLQALGELDHQLGLLYTDCIQQFLQKHRLSPEQITAIGCHGQTVWHSPNSHYPFTMQIGDANLIAAKTGITTVADFRRKDMAFGGQGAPLVPAFHQALFRKPNQATVVLNVGGISNISRLLPNEEVIGYDTGPGNTLLDAWIEKHQGKAYDKNAEWAKSGKVNTDLLADLLDEPFFALPAPKSTGRELFNLAWLNKKLQKHTALLPQDVQATLVELTAQSIVDQLNQIETELDRHLLVCGGGVKNCLLMARLTALLPQWQV... | 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 ... |
Q6D5V5 | MRSGRYIGVMSGTSLDGVDVVLAAIDEHTVAQQARYCHPIPQDIKMAILGMCQGQAVTLSALGQLDTRLGILFAEAVLTLLKETGLRAQGITAIGCHGQTVWHEPTGEAPCTLQIGDNNRVAALTGITTIGDFRRRDLAYGGQGAPLVPSFHHALLLHPVERRIVLNIGGIANLSLLVPGAPVRGYDTGPGNMLLDAWIWRHCAQPYDKDALWAINGQANPLLLRRMLTDPYFALRAPKSTGREYFNLGWLERMLAGLPPIAPQDVQATLVELTAISIADQVLLVGGCERLLVCGGGAHNPLIMARLSALLPGIEVSTTD... | 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 ... |
Q4FMN4 | MEKFYTSLGLMSGTSMDGVDASIIRSDGESNYEPIFDKYFEYDGVIYSNLLNLRDKINSIKDLQDNSYQINELERKITLFHAKISKEIIKNAGVDVDIVGFHGQTIFHNAQEKISKQIGDGNLLSSLLKKNVVYNFRENDIHNGGQGAPLAPIFHNLLINQNKIEKPACVLNIGGIANITLVISKNNEDLKSFDVGPGNCLLDEWVRRHTQMKYDENGKASNLGKTSEVILNQAIDNFDNISNQKKLSFDIKDFDLSFVKGLTYEDGLSTLVDFTAIIIYQSILKSINSEENKKLLIIVCGGGRKNLSLMESIRKRLPKN... | 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 ... |
B4RCQ8 | MRVLGFMTGTSLDAVDMAVLETDGEGISAFGPAGERKLTDATREILLEATEAALKWERGEPEPQIFAKAAVTVAEEHFAAAEAFLAEHGLVWSEFDLLGMHGQTVLHERPQDGVPGRTVQLGDAGLLASLTGRPVAHDFRSADVAAGGEGAPLAPIYHLARARASGLEPPLAVLNVGGVANVTFWSGPGDFAAFDTGPGNGMIDLLVQARKAGRYDAGGRYASVGRVDEAVVRALLAHPYFEAPAPKSLDRYDFSLEPLEPLQLEDACATLVAFTAEAVGRGFELMGEVPREVVVTGGGRHNPEIMKALAARLPAPVKTA... | 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 ... |
Q9F7Q9 | MSKKIYIGAMTGTSHDAIDISFLSIGTKIHLEYFHSIKFPKSLRLKVKKLIENNESSLSDLGTINKEIGFLFSKSINEAIGFSKIKKSSIECVAISGQTIRHEINKRFPFSMQIGDPNIVAKETGLLVVSDFRNMHIALGGEGAPLVPEFHNQLFYKARNPRIILNIGGISNYSFVKNRNDIWGTDVGPGNAILDAYCSDFLQIPFDKNGAIAAKGKVDHIELGRLLQNNFFKRKCPKSTGKELFNIKILSKKFLKKKAEDILCTLVEFSAKSIINSIHKNGHNNCDIVICGGGAHNKYLVKRISEMASNDIVLSSDLGH... | 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 ... |
Q7VEB3 | MYVLGLMSGTSADGVDAVLVDFRGNLNKPRWKLLNSVSLKYSVDLQKAIIDAGQGSKLSGCDWLELSEAITEAHFSAASRCDPDGISTVVGCHGQTVCHRPPKPSFRGASWQLIQAPLLATLLGKNVIYDFRSKDLALGGQGAPLAPFLDYALIGRGKTWRGVLNLGGIANLSLIPPLKGPHRKCHLLGWDCGPANTLIDLAVQKITNGQMNFDCDGLMASKGKPDLDAIKKWLKEDFFQQPPPKSTGREYFGSLDLAKRFSEINSANVNDLVATITCFTACVVAQDLNNLFKKSWIKPAELFVAGGGSRNIFLMKEITN... | 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 ... |
B1P0S1 | MALSLFTVGQFIFLFWTISITEANIDPAARAAAAAAASKAAVTAADAAAAAATIAASAASVAAATAADDAAASIATINAASAAAKSIAAAAAMAAKDTAAAAASAAAAAVASAAKALETINVKAAYAAATTANTAAAAAAATATTAAAAAAAKATIDNAAAAKAAAVATAVSDAAATAATAAAVAAATLEAAAAKAAATAVSAAAAAAAAAIAFAAAP | Function: Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point by about 1.1 degrees at a concentration of 0.1 mg/ml, and by about 1.5 degrees at a concentration of 0.2 mg/ml. Binds to nascent ice crystals and prevents further growth.
Sequence Mass (Da): 1930... |
P17342 | MPSLLVLTFSPCVLLGWALLAGGTGGGGVGGGGGGAGIGGGRQEREALPPQKIEVLVLLPQDDSYLFSLTRVRPAIEYALRSVEGNGTGRRLLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARGAKPDLILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDSEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEDIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTSGDYAFFNIELFNSSSYGDGSWKRGDKHDFEAKQAYSSLQ... | Function: Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May ... |
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