ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q554S6 | MECGDVQALVIDNGSSISKAGFAGDDAPRAVFPSIVGRQRYRDVMVGMGQKDSYVGDEAQSKRGILNLKYPIERGIITNWDDMEKIWHHTFYNELRVAPEEHPIHLTLSPSSSKANREKMTQIMFETFSNPAMYISIQSALSLYASGLTTGIVIDSGDGVSHTVPILEGHSINHAISRLDLAGNDLTDYLGKLLSGRGYPFISIDETEIVRDIKEKLSYITLDFQNEIKIVSSALEKSYELPDGKVISIGNELFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYDNVVLSGGTTMFPGIADRMNKELTALA... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction (By similarity... |
P07828 | MEREEVQAIVIDNGSDMCKAGFAGDDAPRAVFQSIVGRPRYTGVMDVMGQKDSYIGDEAHSRKGFLTLKYPIERGIVTNWDDMEEIWHHTFYNELGVAPEEHPVLLTEQPLNPKKNREKMTQIMFETFNTPAMYVAIQAVLSLYSSGRTTGIVMDSGDGVSHAVSIYEGHALPHAILRLDLAGRDLSDYMMKILTKRGYSFTTTAEKEIIKDIKEKLSYVALDFDAEMLTAASSTTLEKSYELPDGKVITIGNERFRCPEALFQPSLLAMESAGIHETIYNSIMKCDVDIRRYLFGNVILSGGSTMFPGIADRMNKELTA... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction (By similarity... |
P49128 | MCDEDAAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGNKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETVYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
PTM: Oxidation of Met-45 to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not kn... |
P07836 | MCDDDVRALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGLMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETVYNSIMKCDVDIRKDLYANTVMSGGTTMYPGIADRMQKEITA... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
PTM: Oxidation of Met-45 to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not kn... |
A0A2Z5Z9X0 | MNRLIILCLVAATIYSTIALPMKEDISNEERPTSVNEKPVKKSVAVAGAVIQGAALAFQVLDKILTSLGGIGRKIAIGVDNESGMKWAARNVYFYSGTSDTVLPYSVPHSKAFLYGARKTRGSVRGAVGVLAYSMSDGNTLGILFSVPYDYNWYSNWWNIKVYRGYKRANKWMYHDLYYYARPHKGNNEWHEKSLGYGLKSKGFMTSSGQTKLEIRVSRA | Function: Probably acts in predation . Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region... |
P30168 | MADVEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHAGVMVGMGQKDAYVVDEAQSKRGILTLKYPXEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTEYMVKILTERGYSFTTTAEKEIVRDVKEKLAYLALDFEQELETTKTGSAVEKNYELPDGQVITIGAERFRCPEVLYQPSLIGMEAAGIHETTYNSIMKCDVDIRKDLYGNHVLSGGSTMFPGIADRMSKEIQ... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension... |
Q96293 | MADADDIQPIVCDNGTGMVKAGFAGDDAPRAVFPSVVGRPRHHGVMVGMNQKDAYVGDEAQSKRGILTLKYPIEHGVVSNWDDMEKIWHHTFYNELRIAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGFSLPHAILRLDLAGRDLTDYLMKILTERGYMFTTTAEREIVRDIKEKLSFVAVDYEQEMETSKTSSSIEKNYELPDGQVITIGAERFRCPEVLFQPSFVGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFSGIADRMSKEIT... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension... |
P62736 | MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEIT... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 pro... |
P33379 | MGLNRFMRAMMVVFITANCITINPDIIFAATDSEDSSLNTDEWEEEKTEEQPSEVNTGPRYETAREVSSRDIKELEKSNKVRNTNKADLIAMLKEKAEKGPNINNNNSEQTENAAINEEASGADRPAIQVERRHPGLPSDSAAEIKKRRKAIASSDSELESLTYPDKPTKVNKKKVAKESVADASESDLDSSMQSADESSPQPLKANQQPFFPKVFKKIKDAGKWVRDKIDENPEVKKAIVDKSAGLIDQLLTKKKSEEVNASDFPPPPTDEELRLALPETPMLLGFNAPATSEPSSFEFPPPPTDEELRLALPETPMLL... | Function: Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton.
Location Topo... |
P0C1H0 | SVAVAGAVIEGASLTFNVLQ | Function: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and ... |
P81662 | SELAGTIIDGASLTFEVLDKVLGELGKVSRKIAVGIDNESGGTWTALNAYFRSGTTDVILPEVVPNTKALLYSGRKSSGPVATGAVAAFAYYMSNGNTLGVMFSVPFDYNWYSNWWDVKIYPGKRRADQGMYEDMYYGNPYRGDNGWYQKNLGYGLRMKGIMTSAGEAKMQIKISR | Function: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and ... |
Q76CA2 | MKRNILALVVVVALISQSRPAESAGGTIIATLSKIPLSTLASALNTALETGASVASAAAAATSSDYSVTCVIEVENWTKHLMKYPVVQIANSGGLLTVAKNVLPAEIQSFAMRKAWGANGVYGTVSWVLGQTNRRVVIMWSAPYNFDFYSNWLAVGMSRPGLAVPSSRSTWFDLMYYGNSNADISFVRGEYYHSVDPIYFKNSEWEIEGSMNNIHKARVRATVKPIKTMDLASSILTKLEALAGANGKRAIQQELARRAEEEKQRKRKALDEMLK | Function: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and ... |
P20360 | MSEEENAKEAIVVDNGSGVVKAGFAGENQPCSVFPSVVAKPKTKQVIVGGAGNKDCFVGDERQQKRGVCTLSYPIKSGMIKDWDGMQKIWDYTFYNELRIETENHPVLLTEAPLNPKQNRENMCRIMFEEYDFPSMYIQIQAVLSLYSAGRTTGIVVDSGDGVTHVVPIFEGYQIPHAIEKILLAGRDLTDYMCRILKDDDYHFETTAEKETVRDIKEKLCYVADDYEAELKKAGEGGELEESYALPDGRPLKISTQRFQCPEFLFQPDLGGRECKSVHQLTYDSIMTCDLDVRKDLYANIILSGGTTMFPGLGERLYKE... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 42624
Sequence Length: 379
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
Q39758 | MADEDVQALVVDNGSGMCKAGFARDDAPRAVFPSIVGRPKHPGIMVGMDQKDAYVGDEAQSKRGVLTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANKERMTQIMFETFNVPAMYVNIQAVLSLYASGRTTGCVLDSGDGVSHTVPIYEGYALPHAINRLDLAGRDLTDNLMKVLTERGYSFTTTAEREIVRDIKEKLTYVALDFDQEMKTAAESSQLEKSYELPDGNVIVIGNERFRCPEVLFQPSFIGMESSGIHDCTFKTIMKCDVDIRKDLYGNIVLSGGTTMFPGIGERMTKELTA... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 41890
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
P51775 | MTDDNPAIVIDNGSGMCKAGFAGDDAPRAVFPTVVGRPKRETVLVGSTHKEEYIGDEALAKRGVLKLSYPIEHGQIKDWDMMEKVWHHCYFNELRAQPSDHAVLLTEAPKNPKANREKICQIMFETFAVPAFYVQVQAVLALYSSGRTTGIVIDTGDGVTHTVPVYEGYSLPHAVLRSEIAGKELTDFCQINLQENGASFTTSAEFEIVRDIKEKLCFVALDYESVLAASMESANYTKTYELPDGVVITVNQARFKTPELLFRPELNNSDMDGIHQLCYKTIQKCDIDIRSELYSNVVLSGGSSMFAGLPERLEKELLDL... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 41586
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
Q99023 | MEEEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIDGRSRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINPKSNREKMTQIMFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTTVVPIYEGFALPHAIRRVDMAGRDLTDYLMKILAERGYTFSTTAEREIVRDIKEKLCYVAHDFEQEIQTAAQSSSLEKSYELPDAQVITIGDRFRAPQALFHASVLGLESAGIDVTTFNSIMKCDVDVRKELYGNIVMSGGTTMFPQGISDRMQKEITAS... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 41745
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
P91754 | EVTALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFDQEMGTAASSSSLEKSYELPDGQVITIGNERFRCPESMFQPAFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVMSGGTTMFPGIADRMQKEITSMAPS... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 41323
Sequence Length: 372
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
P49871 | MCDDDVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETVYNSIMKCDVDIRKDLYANTVMSGGTTMYPGIADRMQKEITA... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
PTM: Oxidation of Met-45 to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not kn... |
P56544 | MATHNVHSCEFEVFGRVQGVNFRRHALRKAKTLGLRGWCMNSSRGTVKGYIEGRPAEMDVMKEWLRTTGSPLSSIEKVEFSSQRERDRYGYANFHIKPDPHENRPVHEGLGSSSSHHDSN | Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 13697
Sequence Length: 120
Subcellular Location: Cytoplasm
EC: 3.6.1.7
|
P14620 | MSTLGKAPGALKSVDYEVFGRVQGVCFRMYTEEEARKLGVVGWVKNTSQGTVTGQVQGPEDKVNAMKSWLTKVGSPSSRIDRTNFSNEKEISKLDFSGFSTRY | Function: Its physiological role is not yet clear.
Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 11389
Sequence Length: 103
EC: 3.6.1.7
|
P07033 | MSTGRPLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTGQVQGPEEKVNSMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSSFNIRY | Function: Its physiological role is not yet clear.
Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 11178
Sequence Length: 99
EC: 3.6.1.7
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P35744 | MSAAAQLKSVDYEVFGRVQGVCFRMYTEGEAKKIGVVGWVKNTSKGTVTGQVQGPEEKVNSMKSWLSKVGSPSSRIDRTNFSNEKSISKLEYSNFSIRY | Function: Its physiological role is not yet clear.
Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 11007
Sequence Length: 99
EC: 3.6.1.7
|
P00818 | MSTARPLKSVDYEVFGRVQGVCFRMYAEDEARKIGVVGWVKNTSKGTVTGQVQGPEEKVNSMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSVRY | Function: Its physiological role is not yet clear.
Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 11148
Sequence Length: 99
EC: 3.6.1.7
|
P14621 | MSTAQSLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTGQVQGPEDKVNSMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY | Function: Its physiological role is not yet clear.
Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 11140
Sequence Length: 99
EC: 3.6.1.7
|
P00821 | MSALTKASGALKSVDYEVFGRVQGVCFRMYTEEEARKLGVVGWVKNTRQGTVTGQVQGPEDKVNAMKSWLSKVGSPSSRIDRTNFSNEKEISKLDFSGFSTRY | Function: Its physiological role is not yet clear.
Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 11448
Sequence Length: 103
EC: 3.6.1.7
|
P00820 | MSTAGPLKSVDYEVFGRVQGVCFRMYTEGEAKKIGVVGWVKNTSKGTVTGQVQGPEDKVNSMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY | Function: Its physiological role is not yet clear.
Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 10992
Sequence Length: 99
EC: 3.6.1.7
|
P35745 | MAEPLKSVDYEVFGTVQGVCFRMYTEGEAKKRGLVGWVKNTSKGTVTGQVQGPEEKVNSMKSWLSKVGSPSSRIDRADFSNEKTISKLEYSNFSIRY | Function: Its physiological role is not yet clear.
Catalytic Activity: an acyl phosphate + H2O = a carboxylate + H(+) + phosphate
Sequence Mass (Da): 10863
Sequence Length: 97
EC: 3.6.1.7
|
Q9R1V4 | MRRLRRWAIAALLLLPLLPPPGLGALGPRGALHWRSSAHVGSPESPEGSEVTEPSRLVRQSSGGEVRKPQLDTRVRQDPPRGTPVHLAQVSFVIPAFDSNFTLDLELNHHLLSSQYVERHFSREGTRQHSTGAGDHCYYHGKLRGNPQSFAALSTCQGLHGVFSDGNLTYIVEPKEIAGPWGPPQGPLPHLIYRTPLLPAPLGCREPGCLFAVPAQSALPNWPKLRRKRQVRRGHPTVHSETKYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYR... | Function: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Required for localization of the potassium channel subunit proteins KCNA1/KV1.1 and KCNA2/KV1.2 at cerebellar cortex basket cell distal terminals, is thereby involved in ephaptic inhibitory synchronization of Purk... |
Q9PSZ3 | RRHHSPLLVSLIGGQTFKSSHSGAAYFGGICSPTHGGGVNEYGNIGAMAITLAQTLGQNLGMMWNKPRTTTGDCKCPDLWRGCIMEDTGFYLPQKFSRCSVDEYSKFLQDGGGSCLFNKPLKLLDPPSCGNGFIEIGEECDCGSPAECNKSRAGNCCKKCTLSHDAMCSDGLCCRGCKYEPRGTVCRESLNECDVPEACPGDSSACPANLHKQDGYFCDNEQGRCFGGRCKTRDRQCHALWGRGASDRFCYEKLNIEGTEKGNCGRDRQNWIQCSKQDVLCGYLLCSNISGIPQIGELNGDITSMSFYHQNRYLDCRGGQ... | Function: Probable ligand for integrin in the brain. This is a non-catalytic metalloprotease-like protein.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48577
Sequence Length: 452
Domain: A conserved motif [AVN[ED]CD] within the disint... |
O43184 | MAARPLPVSPARALLLALAGALLAPCEARGVSLWNQGRADEVVSASVGSGDLWIPVKSFDSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTVILGHCYYHGHVRGYSDSAVSLSTCSGLRGLIVFENESYVLEPMKSATNRYKLFPAKKLKSVRGSCGSHHNTPNLAAKNVFPPPSQTWARRHKRETLKATKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMAP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors (By similarity).
PTM: The precursor is cleaved by a furin endopeptidase.
Locati... |
Q61824 | MAERPARRAPPARALLLALAGALLAPRAARGMSLWDQRGTYEVARASLLSKDPGIPGQSIPAKDHPDVLTVQLQLESRDLILSLERNEGLIANGFTETHYLQDGTDVSLTRNHTDHCYYHGHVQGDAASVVSLSTCSGLRGLIMFENKTYSLEPMKNTTDSYKLVPAESMTNIQGLCGSQHNKSNLTMEDVSPGTSQMRARRHKRETLKMTKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIKLLPRKSHDNAQLISGVYFQGTTIGMAPIM... | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Sin... |
Q13444 | MRLALLWALGLLGAGSPLPSWPLPNIGGTEEQQAESEKAPREPLEPQVLQDDLPISLKKVLQTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRGLVVLTPERSYTLEQGPGDLQGPPIISRIQDLHLPGHTCALSWRESVHTQKPPEHPLGQRHIRRRRDVVTETKTVELVIVADHSEAQKYRDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAHLLPRLPHDSAQLVTGTSFSGPTVGMAIQN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and m... |
O88839 | MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTLSGSMESRVVQDSPPMSLADVLQTGLPEALRISLELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLSPERGYTLELGPGDLQRPVISRIQDHLLLGHTCAPSWHASVPTRAGPDLLLEQHHAHRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and m... |
Q94316 | MKIQDRSLLIFLVLGILKSDAFNTRVKRHAPIRFQRSTRQSVVHFEFLDQEYVVDLEPNHSTFHENFKVFTQDGPQIVPRDEYIGTVREPRAGRAVLTQLEENVYIGSLYFVDDTLHLEPSYPHQLSDDLGPVVGYFESDLDLNLDLSAMPVRNQVSFRRANPFLKHRRAIAIPSDRRKDVLNVKRNRCTLKLVADYSFYSIFGKNNTGIVTKFLVNMIARVNEIYTPINWDVGKEDDISGRGRFQNMGFSIKEIKVLDRPNASDSHYNSYSRIWEVERLLREFAFAEGSKDFCLVHLVTARTFREVATLGLAYVSYKKW... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease (By similarity). Acts together with protease sup-17 to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision . By modulating glp-1/Notch signaling, plays a role in germlin... |
Q9VAC5 | MFTKCISCCGLAIISVFFACLFVENCAALQKTLRHYEIFHKDDVVHRVVKRGAKHSTNPFNTIKEVEFTTLGKNFRLILHPHRDVLHSKFRAYAVDADGNETVVHMDHDSFYSGRVFGELESSVRAHIEDGTMTMSIHLPEETYHIEPSWRHLPEAKKDTMVAYKASDVKVHKNEAGATPKTCGYIKEGLELEDKEHGDTLDNELHTREKRQSDQYEYTPTKTRCPLLLVADYRFFQEMGGGNTKTTINYLISLIDRVHKIYNDTVWQDRSDQEGFKGMGFVIKKIVVHSEPTRLRGGEAHYNMIREKWDVRNLLEVFSR... | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 83081
Sequence Length: 732
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion u... |
P78536 | MRQSLLFLTSVVPFVLAPRPPDDPGFGPHQRLEKLDSLLSDYDILSLSNIQQHSVRKRDLQTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQDFFTGHVVGEPDSRVLAHIRDDDVIIRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKNVSRLQSPKVCGYLKVDNEELLPKGLVDREPPEELVHRVKRRADPDPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form . Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface . Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-re... |
O77636 | MLREQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPIGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNE | Cofactor: Binds 1 zinc ion per subunit.
Function: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-rece... |
Q9Y3Q7 | MFLLLALLTELGRLQAHEGSEGIFLHVTVPRKIKSNDSEVSERKMIYIITIDGQPYTLHLGKQSFLPQNFLVYTYNETGSLHSVSPYFMMHCHYQGYAAEFPNSFVTLSICSGLRGFLQFENISYGIEPVESSARFEHIIYQMKNNDPNVSILAVNYSHIWQKDQPYKVPLNSQIKNLSKLLPQYLEIYIIVEKALYDYMGSEMMAVTQKIVQVIGLVNTMFTQFKLTVILSSLELWSNENQISTSGDADDILQRFLAWKRDYLILRPHDIAYLLVYRKHPKYVGATFPGTVCNKSYDAGIAMYPDAIGLEGFSVIIAQL... | Function: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization. This is a non catalytic metalloprotease-like protein (By similarity).
PTM: The prodomain and the metalloprotease-like domain are cleaved during the epididymal maturation of the spermatozoa.
Location Topology: Single-pass... |
Q9R157 | MPLLFILAELAMLFARLDSEGICLHITVPQKIEPRKGGDAEGKVTYVITIDGKPYSLHLRNHSFLSQNFLVYTYNETGSLYSDSSHFLAHCHYRGYVDEVPNSIVTLSICSGLRGFLQLENVSYGIEPLESSARFEHIVYQVKSDSSMLAGNDSHVWQIDQLDKGHFNEQDKNHSQLLPQSLKLHIIVGKFLFDYMGSDIMAITQKIFQIIGLVNAMLTQLKLSVVLASLELWSDKNHISTDGNATDILQRLLDWKRDYLTLQSNEITHLLIYRRRPKYIGAASPGEICSKSYVAGVGMYPEDIGLEGFSVVITQLIGLH... | Function: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization. This is a non catalytic metalloprotease-like protein.
PTM: The prodomain and the metalloprotease-like domain are cleaved during the epididymal maturation of the spermatozoa.
Location Topology: Single-pass type I membrane... |
Q9H013 | MPGGAGAARLCLLAFALQPLRPRAAREPGWTRGSEEGSPKLQHELIIPQWKTSESPVREKHPLKAELRVMAEGRELILDLEKNEQLFAPSYTETHYTSSGNPQTTTRKLEDHCFYHGTVRETELSSVTLSTCRGIRGLITVSSNLSYVIEPLPDSKGQHLIYRSEHLKPPPGNCGFEHSKPTTRDWALQFTQQTKKRPRRMKREDLNSMKYVELYLVADYLEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRKLLAQKYHDNAQLITGMSFHGTTIGLAPLMAMC... | Cofactor: Binds 1 zinc ion per subunit.
Function: Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteob... |
Q9QYC0 | MNGDTRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTASVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGSTNLGVNQAGFTLHSAVYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSLGDVAYHDYHGILVDEEEKILIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHN... | Function: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80647
Sequence Length: 735
Domain: Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular h... |
Q7MDL6 | MNYFDLPKIDLHCHLDGSVRPQTIIDLADEQNLTLPSRDINVIKEMMVAPETCPNLDEYLKRFELPGMVMQTAEALERISFELFEDAANENVKYLEVRFGPLLHQVKGLSLDDIMDSVVRGMKRAEAQYDIHGNYILSILRTMPKDQIKAVLEAGAKHLNDGIVAFDLAGSEIPGFCHEFVPYAQYAKELGYRITIHAGEQGAGQNVYDAISLLGAERVGHGIFIHNHPEAYQLVKGEEVALETCPSSNVQTKAVNSLSEHPIKAFYKDGIAVTINTDNRTVSNTTMTDEVRKVVEAFELTEAEYFDIYTISVNNAFTSD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
Catalytic Activity: adenosine + H(+) + H2O = inosine + NH4(+)
Sequence Mass (Da): 36997
Sequence Length: 331
EC: 3.5.4.4
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O15204 | MLRGISQLPAVATMSWVLLPVLWLIVQTQAIAIKQTPELTLHEIVCPKKLHILHKREIKNNQTEKHGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENMEHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHAVFTSNQEEQDPANHTCGVKSTDGKQGPIRISRSLKSPEKEDFLRAQKYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSNLGKKIHDHAQLLSGISFNNRRVG... | Cofactor: Binds 1 zinc ion per subunit.
Function: May play an important role in the control of the immune response and during pregnancy.
Sequence Mass (Da): 52775
Sequence Length: 470
Subcellular Location: Secreted
EC: 3.4.24.-
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P07327 | MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAIL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Alcohol dehydrogenase . Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate .
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 39859
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 1.... |
P25405 | GTAGKVIKCKAAIAWEIKKPLSIEQIEVAPPKAHEVRIKILATGICRSDDHVISGAFKMPLPMVLGHEAAGVVESVGEGVTCVKPGDKVIPLFVPQCGKCSSCRSTRGNLCTSNDLSAATGLMPDGTSRFTCKGKSLHHFISTSSFTEYTVVHENSVVKIDAAAPLEKVCLIGCGFSTGYGAAVETAKVEPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGVDINKDKFPKAKEMGATECVNPLDYKKPINEVLFDLTGGEGVDYSFEVIGRTDTMTAALASCHMDYGTSIIVGLPPSASEITFSPGLIFTGRTWKGSVF... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 39663
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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P00325 | MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICHTDDHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVY... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism . In vitro can also catalyzes the NADH-dependent reduction of all-trans-retinal and its derivatives such as al... |
P00328 | MSTAGKVIKCKAAVLWEQKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDDHVVSGTLVAPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFIPQCGKCSVCKHPEGNLCLKNLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLVGCGFSTGYGSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVAALSCCQEAYGVSVIVGVPPDSQNLSMNPMLLLSGRTWKGAIFG... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 39623
Sequence Length: 374
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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P30350 | ARGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINSDKFAKAKELGATDCINPKDHKEPIHKVLIGMTGYGVDYSFEVIGRIETMVAALASCHYNYGVSVIVGVPPAAQNITFDPMLLFSGRTWKGSVFGGWKSKDSVPKLVADYMKKKFVLDPLITHTLPFSKINEGFDLLRAGKSIRSVLTF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 19816
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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P06525 | MSTTGQIIRCKAAVAWEAGKPLVIEEVEVAPPQKHEVRIKILFTSLCHTDVYFWEAKGQTPLFPRIFGHEAGGIVESVGEGVTDLQPGDHVLPIFTGECGECRHCHSEESNMCDLLRINTERGGMIHDGESRFSINGKPIYHFLGTSTFSEYTVVHSGQVAKINPDAPLDKVCIVSCGLSTGLGATLNVAKPKKGQSVAIFGLGAVGLGAAEGARIAGASRIIGVDFNSKRFDQAKEFGVTECVNPKDHDKPIQQVIAEMTDGGVDRSVECTGSVQAMIQAFECVHDGWGVAVLVGVPSKDDAFKTHPMNFLNERTLKGT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Alcohol dehydrogenase mostly active on ethanol (EtOH), but exhibits broad substrates selectivity for primary and secondary alcohols (e.g. butanol, propyl alcohol, pentanol, isopentanol, ethylene glycol, isopropanol, methanol and tertiary butyl alcohol) . Converts all... |
O04619 | MASEDVKRTESAAVSTIVNLAEEAREGVKAPSYAFKSICKSLFAGGVAGGVSRTAVAPLERMKILLQVQNPHNIKYSGTVQGLKHIWRTEGLRGLFKGNGTNCARIVPNSAVKFFSYEQASNGILYMYRQRTGNENAQLTPLLRLGAGATAGIIAMSATYPMDMVRGRLTVQTANSPYQYRGIAHALATVLREEGPRALYRGWLPSVIGVVPYVGLNFSVYESLKDWLVKENPYGLVENNELTVVTRLTCGAIAGTVGQTIAYPLDVIRRRMQMVGWKDASAIVTGEGRSTASLEYTGMVDAFRKTVRHEGFGALYKGLV... | Function: Mitochondrial adenylate carrier that catalyzes specifically the transport of ATP, ADP and AMP by a counter-exchange mechanism across the inner mitochondrial membrane. Substrate preference in reconstituted proteoliposomes is ATP > AMP > ADP. May play a role in oxidative phosphorylation and be important for the... |
Q94BT6 | MEWDSGSDLSADDASSLADDEEGGLFPGGGPIPYPVGNLLHTAPCGFVVTDAVEPDQPIIYVNTVFEMVTGYRAEEVLGGNCRFLQCRGPFAKRRHPLVDSMVVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQFFIETDIDLGPVLGSSTKEKSIDGIYSALAAGERNVSRGMCGLFQLSDEVVSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVCQNAWGSETTRVLETVPGAKRLGWGRLARELTTLEAAAWRKLSVGGSVEPSRCNFSACAVGNRVVLFGGEGVNMQPMND... | Function: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(AD... |
Q5Z8K3 | MEWDSESDGAGSIGAGEEEEEEEEEEEGGFGGGGGGGGGGGGMFSFAIEGMLRASGPCGLVVTDALEPDCPIIYVNCGFEEATGYRAEEVLGRNCRFLQCRGPFAQRRHPLVDAMVVSEIRKCIDNGTEFRGDLLNFRKDGSPLMNKLHLTPIYGDDETITHYMGIQFFTNANVDLGPLPGSLTKEPVRSTRFTPDNFFRPISTGPGQSNFCREYSSLFQLTDEVLCQSILSRLSPRDIASVSSVCRRLYLLTRNEDLWRMVCQNAWGSETTRALETVPAAKRLGWGRLARELTTLEAVAWRKLTVGGAVEPSRCNFSAC... | Function: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex (By similar... |
Q8W420 | MQNQMEWDSDSDLSGGDEVAEDGWFGGDNGAIPFPVGSLPGTAPCGFVVSDALEPDNPIIYVNTVFEIVTGYRAEEVIGRNCRFLQCRGPFTKRRHPMVDSTIVAKMRQCLENGIEFQGELLNFRKDGSPLMNKLRLVPIREEDEITHFIGVLLFTDAKIDLGPSPDLSAKEIPRISRSFTSALPIGERNVSRGLCGIFELSDEVIAIKILSQLTPGDIASVGCVCRRLNELTKNDDVWRMVCQNTWGTEATRVLESVPGAKRIGWVRLAREFTTHEATAWRKFSVGGTVEPSRCNFSACAVGNRIVIFGGEGVNMQPMN... | Function: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(AD... |
Q67UX0 | MEWDSDSEGSGDEEEEEEEEEEEGVEVGGGGDGGVGVGVGGGFALAIEGVLGACGLVVSDALEPDFPIIYVNRGFEDATGYRAEEVLGRNCRFLQCRGPFAKRRHPLVDTTVVTDIRRCLEEGTVFQGDLLNFRKDGSPFMAKLQLTPIYGDDETITHYMGMQFFNDSNVDLGPLSVSTTKEIVRSTLITPDNTIRPSPMGKGFCSEHSDLFLLSDEVLCQKILSRLSPRDIASVNSVCKRLYHLTRNDDLWRMVCQNAWGSEATQVLETVAGTRSLAWGRLARELTTLEAVTWRKLTVGGAVEPSRCNFSACAAGNRVV... | Function: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex (By similar... |
Q9C9W9 | MAREHAIGEATGKRKKRGRVEEAEEYCNDGIEEQVEDEKLPLEVGMFYYPMTPPSFIVSDALEPDFPLIYVNRVFEVFTGYRADEVLGRNCRFLQYRDPRAQRRHPLVDPVVVSEIRRCLEEGIEFQGELLNFRKDGTPLVNRLRLAPIRDDDGTITHVIGIQVFSETTIDLDRVSYPVFKHKQQLDQTSECLFPSGSPRFKEHHEDFCGILQLSDEVLAHNILSRLTPRDVASIGSACRRLRQLTKNESVRKMVCQNAWGKEITGTLEIMTKKLRWGRLARELTTLEAVCWRKFTVGGIVQPSRCNFSACAVGNRLVLF... | Function: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(AD... |
Q2R2W1 | MFDAGDRGGGGGVVAVKRMKLCEEEEEEEEGMEVDEEEEEVGWVWRPPGGLAGEDEAAAWEGRAAAIVVSDAVEVDFPVIYVNAAFEAATGYRADEVLGRNCRFLQFRDPRAQRRHPLVDPMVVSEIRRCLNEGIEFQGELLNFRKDGAPLYNRLRLIPMHGDDGFVTHVIGIQLFSEANIDLSNVSYPVYKQQSNHRPNIQEINPASHEHIPKIQSSEYCCILQLSDEVLAHNILSRLSPRDVASIGSVCTRMHELTKNDHLRKMVCQNAWGRDVTVRLEMSTKMLGWGRLARELTTLEAASWRKFTVGGRVEPSRCNF... | Function: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(AD... |
P83736 | MTIAVTGSIATDHLMRFPGRFSEQLLPEHLHKVSLSFLVDDLVMHRGGVAGNMAFAIGVLGGEVALVGAAGADFADYRDWLKARGVNCDHVLISETAHTARFTCTTDVDMAQIASFYPGAMSEARNIKLADVVSAIGKPELVIIGANDPEAMFLHTEECRKLGLAFAADPSQQLARLSGEEIRRLVNGAAYLFTNDYEWDLLLSKTGWSEADVMAQIDLRVTTLGPKGVDLVEPDGTTIHVGVVPETSQTDPTGVGDAFRAGFLTGRSAGLGLERSAQLGSLVAVLVLESTGTQEWQWDYEAAASRLAGAYGEHAAAEIV... | Function: Catalyzes the phosphorylation of adenosine to adenosine monophosphate (AMP). Prefers dGTP and GTP to ATP as phosphate donors in vitro.
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 34472
Sequence Length: 324
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP fro... |
P07693 | MIFTKEPAHVFYVLVSAFRSNLCDEVNMSRHRHMVSTLRAAPGLYGSVESTDLTGCYREAISSAPTEEKTVRVRCKDKAQALNVARLACNEWEQDCVLVYKSQTHTAGLVYAKGIDGYKAERLPGSFQEVPKGAPLQGCFTIDEFGRRWQVQ | Function: Degrades the intracellular SAM pools of the host cell and inhibits the host S-adenosylmethionine synthase METK/MAT, thereby preventing methylation of the viral genome . Induces the polymerization of METK into filaments that are enzymatically inactive . Keeping the viral genome in an unmethylated state allows ... |
Q5CZR5 | MTYPTNLEIIGGQGGSSFSFTGENNGASLEKIWVWVGGWQIKAVRAWLSDGRDETFGVPSGSHQEYVFTPGECFTSLSLWGNGAGTRLGAIKFKTNKGGEFFAHMTSWGLKTEYPMDVGSGYCLGIVGRGGSDIDCMGFMFLNAVQSTVLTNVNYPTINQLIPKVATEEIKSVSFENKTSVKQEQKVETSKKVIKTSSWSMTKSFSSTFSVEVSAGIPEIAEVSTGFSISFGVESTHSLEQTDEKNETLTTTVEVPPKKKVDVHITIGRASFDLPYTGTVKITCKNGSVLQYETKGQYKGVAYTDIKVNTVEKDL | Function: Pore-forming protein which might play a role in host defense. Exists as an antiparallel dimer in solution. Can also assemble into an octameric pore-like structure spanning the cell membrane. Oligomerization may be triggered by binding of the jacalin-type lectin domain to high-mannose cell-surface proteoglycan... |
Q83M39 | MKPENKLPVLDLISAEMKTVVNTLQPDLPSWPATGTIAEQRQYYTLERRFWNAGAPEMATRAYMVPTKYGQVETRLFCPQPDSPATLFYLHGGGFILGNLDTHDRIMRLLASYSQCTVIGINYTLSPEARFPQAIEEIVAACCYFHQQAEDYQINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKIAGVLLWYGLYGLRDSVTRRLLGGVWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTREVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQFFTAQL | Function: Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose bin... |
O42470 | MMFPQSSSRHSGSSHMPQQLKFTTSDSCDRIKDEFQLLQAQYHSLKLECDKLAGEKSEMQRHYVMYYEMSYGLNIEMHKQAEIVKRLHGICAQVLPYLSQEHQQQVLGAIERAKQVTAPELNSIIRQLQVHQLSQLQALALPLTSLPMGLQAPSLPISASSGLLSLSALGSQGHLPKEDKNGHEGDRRPDDDGDKSD | Function: May act as a transcriptional corepressor. Has a possible role in the negative regulation of proteins containing WD-40 repeats. May be required for the initiation and maintenance of the differentiated state (By similarity).
PTM: Ubiquitinated by XIAP/BIRC4.
Sequence Mass (Da): 22035
Sequence Length: 197
Domain... |
P80197 | MAGALWEIEKELFTKLPAPSSAINSHLQPAKPKVPQKKPSKWDPPAEFKVDLSTAVSYNDIGDINWKNLQQFKGIERSEKGTEGLFFVETESGVFIVKRSTNIESETFCSLLCMRLGLHAPKVRVVSSNSEEGTNMLECLAAIDKSFRVITTLANQANILLMELVRGITLNKLTTTSAPEVLTKSTMQQLGSLMALDVIVNNSDRLPIAWTNEGNLDNIMLSERGATVVPIDSKIIPLDASHPHGERVRELLRTLIAHPGHESSQFHSIRDIITLYTGYDVGTEGSISMQEGFLATVRECASFDLDAFERELLSWQESLQ... | Function: Has a role in the regulation of microfilament formation. Phosphorylates the actin-fragmin complex on threonine residues, in vitro.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 80955
Sequence Length: 737
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q00278 | MNGSLSQHDQERLSTPYRDGPPEETVYLVTGASRGIGRGLIEAFLQRPKSTVVAWLRNVRTATPALSALTVAEGSRMIIVQLNSDSETDAQAAVQTLREEHGVTHLDVVVANAAMATNFGPASTMPLEHLQAHMMVNMYAPVLLFQATRLMLQQSKQQAKFVLIGAPISTITNMHDYSRAPLTAYGVSKLAANYMVRKFHFENKWLTAFIIDPGHVQTDMGDQGARLMGRPQAPTTVADSVAGICARIDEATKETTSGHFVIHTDGSQLPW | Function: Norsolorinic acid ketoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1),... |
Q00258 | MVLPTAPEPPTLLGYHRILSPSAGVRVSPLCLGTMSFGNGWKGVMGECDQATSFNMLDTFYESGGNFIDVANFYQGGDTERWVGEWMAQRQNRDEIVLSTKYTMGYTMFGPQKIKSNFQGNHAKSLRLSVKASLQKLQTDYIDLLYVHMWDFTTSVEEVMRSLNHLVANGKVLYLGVSDTPAWLVVKCNAFARANGLTPFSVYQGHWSSAFRDFERDILPMCESEGMGLAPWGVLGRGQFRSAEEFSREGRKMGPQDEKHRRLGEKLDQMAQQKNTKATSIAQAYVMHKAPYVFPVIGGRKVEHLKENIEALGLVLSEEE... | Function: Norsolorinic acid reductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), afl... |
Q12732 | MGGDGWPSDGHILLLIVLTVLTPPSLALYRLWIHPLRSYPGPRWWAIWRGPYILSNIRGNLVRDLQRLHQQFGPVVRIAPNELSFIVPEAASPIYTSNPEFPKDPMHLPPFHNGTPGILAADHAHHRRYRRLLAFSFSDKGLRHERSLIERSIDLLITQLHENCGQGPLDLALWFNWATFDIIGDLAFGDSFGCLENVQTHPWIASIQGNVKLIPILNAFRRYRLDGLLRLLGSRKLLEQRRRNAQFTTDQVDRRLKNSSTPRGDIWDAVLAQKPDGEPPMTRDEMISNASAIVLAGSETSATLLSGCTWLLLKNPSHLH... | Function: Averantin hydroxylase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin... |
P87017 | MEVLDTTVDLGTLQGKSALITGGASGIGLATARAWAAAGMYVTIADIQPLETGQNILADLAGGHVHYVCCDVTSWESQITAFKEAIQFTPSKALDIVAAFAGVSFAGGNQVDHVLAAGDPRLDVNPSPPDIRNIQVNLIGVYYTSWLGLYYLRLSPTNKAANPSPDKSLILMGSIGSYMDSPKASTYPASKFGVRGLFRSTRARTRELGVRCNLLAPWFIDTPLIAPMKKAMAARGIDMAQRLTFASVDACVEAATTCAANPQLHGTPPIRYAYCLKT | Function: 5'-hydroxyaverantin dehydrogenase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1... |
Q12437 | MVTYALLGATGATGSSILRHLLQKSPDSLHIQVLVRSKVKLLQAFPDLETTRRPQVHVIQGMSTDSDALSECLRNASIVFMCVAQNGSPIGTTLCQDSARPIISVLQQQQQSEGASYQPCTIVQLRSASLNPALAAQVPAFVHRIVSFCLFANYADIKQACQYYSEAQKQGTLEYILVDPPTLHDANGTHPTGYRLISTEPQATALSYADLGAAMCEIAHRESEFHGRAVGVTATGRVRQTWGVLLRHLLEGGSSRLRETIAKEAVVVRVLCIFLVILACLMSSL | Function: Averufin oxidase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (... |
Q6UEG5 | METPFAGPWHQFVEDLGQTPCLPGKDLDSILAGWGQLAGTLATRYGFPPPDESVATEDVQLDGLWLRCYTPANATGQEPVGLYFHGGGWVMGGVKEEDGFCRVISRQCQMRLVSVEYRKAPETRYPGALNDGVSAALWAQSRYENQPLVLMGTSAGGNLAFGTALRLIDQDMADKVSGVVALAPITVHPDAVPEHLKEQYTAYEENAELTVNSRAAMQVFFDCYKAPVDDVYTSCLLHPRLLALPKVYIAELGLDTLRDDARLMKGALDTAKVPVMYDAYPGYPHCSFMFPFKSLGEHQRTFLGGVAKAVRWMS | Function: Versiconal hemiacetal acetate esterase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 ... |
Q12062 | MGRNWFQVTAMAVVPVVGIMAAVNPTILSSAASSLPSLGAMFTSDDFASQMDGRIQAQGLLSSHFGMYGWPGQSFDYVIVGGGTAGLAMARRLSQDGTASVAVIEAGGFYETDAGNATEVPMYLFNYFFDNGKVKNPLFDWYQYTTPQPGLAQREMFYMQGKTLGGSTARGAMLYHRGSKGAYDMWADHVGDDSYRWDKWLPYFQKSVHFSGPETNPRPANATALNDNTAFTASGGPVHVGYPFQVNAISSWVDRALAKMGFPEAQGFSNGNLLGRSYITHTINPYTRRRETASSSYLREALMESNNLNIFTRTLVKRVL... | Function: Dual cyclase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2... |
Q9UQY0 | MTGLDMEIIFAKIKEEYARTDDVGKRQIQGHIRELQVGFYSDWDVVMRLSSGPLQVALTKVGIDLGIFRSLKESDTPITLAEIVKKTGASPRLLGRILRTQAAFGLIKETGPQEYTSSAFTDVFANSDAAGAVVQLFDISGPCTQILPDFLAERNYQDITSNKDCVFQKAFGSDLTMFEWMPQHPKHMESLGHLMALERPVSWVDHYPVLEELGGFPAPDKVLMVDIGGGFGQQSKALRAKFPDLPGRLIVQDIPQTLANAQPAAGIEFMEHNFFEPQPIQNAKFYYLRHVFHDWPDEQCVLILKQIIPAMGPESQILID... | Function: Demethylsterigmatocystin 6-O-methyltransferase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflat... |
Q12120 | MALPSKAALVGLANTLSEQVKRYLATAGETKSPEDHKLCIESERTPSSNEHAQAWEIVRTCDRIGSLVHGPVPWLLSNALSHLDSACLAAATHLNLQDIIVDGPSPTSLDTIVAATGVSEDLLRRILRGCAQRFIFEEVAPDQYAHTDASKMLRVTGIHALVGFSCDEVMRSGASFSDFLQQTKGKPPSWNVPSPFSLAFDPTKGLFDYYSTVDEVRGRRFDLGMGGTEATKPLVEEMFDFSSLPEGSTVVDVGGGRGHLSRRVSQKHPHLRFIVQDLPAVIHGVEDTDKVTMMEHDIRRPNPVRGADVYLLRSILHDYP... | Function: Sterigmatocystin 8-O-methyltransferase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 ... |
O13345 | MIYSIIICAGALLGFLILQKLLAPKDTRPPLPPGPWRKPIIGNLTDFPPKGTPEWLFWAKHHERYGPMSSLEVMGQTIIMINDAHLGIEIMHKKSALSQMIPDAPFAHMAGWGMSLATERNKQAWKTIRANMKQEIGTRRAIATFHPKMEIGIRRFLLRTLDNPDDLRFHIRKEANAFMMDVAYGYTIAPHGKDELYDLTQQSVRQFSHIFSPGEWSVNFFPILRYVPSWFPGASFQIKAAEYKRTIERMTMVPYLWIKDQVARGCTRPSILLRLLQKGHYESGSHQEQVLVWTNAEFVMGGSDTTVSAVSSFFVAMALY... | Function: O-methylsterigmatocystin oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1... |
Q8XAC2 | MPENYTPAAAATGTWTEEEIRHQPRAWIRSLTNIDALHSALNNFLEPLLRKENLRIILTGAGTSAFIGDIIAPWLASHTGKNFSAVPTTDLVTNPMDYLNPAHPLLLISFGRSGNSPESVAAVELANQFVPECYHLPITCNEAGALYQNAINSDNAFAVLMPAETHDRGFAMTSSITTMMASCLAVFAPETINSQTFRDVADRCQAILTSLGDFSEGVFGYAPWKRIVYLGSGGLQGAARESALKVLELTAGKLAAFYDSPTGFRHGPKSLVDNETLVVVFVSSHPYTRQYDLDLLAELHRDNQAMRVIAIAAESSDIVA... | Function: Catalyzes the isomerization-deamination of galactosamine 6-phosphate to form tagatofuranose 6-phosphate and ammonium ion.
Catalytic Activity: D-galactosamine 6-phosphate + H2O = D-tagatopyranose 1-phosphate + NH4(+)
Sequence Mass (Da): 41729
Sequence Length: 384
EC: 3.5.99.-
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A0KYQ7 | MLTSPLSPFEHEDSNLLLSAEQLTQYGAFWTAKEISQQPKMWRKVSEQHSDNRTIAAWLTPILAKPQLRIILTGAGTSAYIGDVLAAHIQQHLPLATQQVEAISTTDIVSHPELYLRGNIPTLLISYGRSGNSPESMAAVELAEQLVDDCYHLAITCNGQGKLANYCADKSHCYLYKLPDETHDVSFAMTSSFTCMYLATLLIFAPNSQALMQCIEMAEHILTERLADIRLQSEQPSKRVVFLGGGPLKAIAQEAALKYLELTAGQVVSAFESPLGFRHGPKSLVDSHTQVLVMMSSDPYTRQYDNDLIQELKRDNQALS... | Function: Involved in the pathway of N-acetyl-D-galactosamine degradation. Catalyzes the conversion of D-galactosamine 6-phosphate (GalN-6-P) to D-tagatofuranose 6-phosphate (Tag-6-P). It can also catalyze the conversion of D-glucosamine 6-phosphate.
Catalytic Activity: D-galactosamine 6-phosphate + H2O = D-tagatopyran... |
O50523 | MTTPPGTLPVDDSAVHTVREIAQQPALWREVDRIVGASREALDAFLDPLVARGDLRVVLTGAGTSAFAGQVLQPSLARHLGRRVDAVPTTDLVADPRGCLAEDLPTLLVSFARSGDSPESVAATALADQVLSEVHHLVITCNEQGRLAREHTRRPRSHVLLMPAASNDRGFAMTSSFTCMTLAALLALGKDARDGVAERLARAAESIIEDGAADRTAGALVDRAPERIVFLGSGPLKGLAEESALKVLELTGGTLMAVAESSLGFRHGPKAVLNERSVAVVYVSNDPYTRRYDHDIVAELRGNLPVGSVVAVSAESGAGT... | Function: Catalyzes the isomerization-deamination of galactosamine 6-phosphate to form tagatofuranose 6-phosphate and ammonium ion.
Catalytic Activity: D-galactosamine 6-phosphate + H2O = D-tagatopyranose 1-phosphate + NH4(+)
Sequence Mass (Da): 40446
Sequence Length: 385
EC: 3.5.99.-
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A8W969 | MKGFTKHSILMACSIGLAINATAADWDNIPIPAELDAGQSWELQQNYSDSFNYSGKNSTFTGKWKDSYFHSWTGPGLTHWSSDESWVGDGNLIISASRRQGTNKVNAGVITSKTKVKYPIFLEASIKVSNLELSSNFWLLSENDQREIDVLEVYGGARQDWYAKNMSTNFHVFFRNNDNSIKNDYNDQTHFTPTWGNYWRDGFHRFGVYWKSPTDVTFYIDGQKTTKGAWSQVVMKDKDYTGAILDKSRYNMDQEAFIIIDTEDHSWRSEAGHIATDADLADSDKNKMYVDWIRVYKPTGGSTTPPTGDITPPSGYTNLQ... | Catalytic Activity: Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
Sequence Mass (Da): 50998
Sequence Length: 453
Subcellular Location: Secreted
EC: 3.2.1.81
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P64293 | MRFVVTGGLAGIVDFGLYVVLYKVAGLQVDLSKAISFIVGTITAYLINRRWTFQAEPSTARFVAVMLLYGITFAVQVGLNHLCLALLHYRAWAIPVAFVIAQGTATVINFIVQRAVIFRIR | Function: Required for arabinosylation of arabinogalactan (AG), an essential component of the mycobacterial cell wall. Probably acts as an anchor protein recruiting AftA, the first arabinosyl transferase involved in AG biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13377
Sequence Lengt... |
Q9CDA3 | MLRFIVTGSLATAVDFSVYVTLYRGGGLQVDLAKFTSVVIGTITSYMINRRWTFQMSPSTTRFAAVMALYGITFAVQMGLNHLCLFLFHYQEPWAIPIAFVIAQGLATVINFIVQRVVIFRIR | Function: Required for arabinosylation of arabinogalactan (AG), an essential component of the mycobacterial cell wall. Probably acts as an anchor protein recruiting AftA, the first arabinosyl transferase involved in AG biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13861
Sequence Lengt... |
Q9LTW5 | MDLASKKNTANVGSKEIDPIKPKSPRSSLSPFSLKLGDNVPRNPHFDPKKMDPLVKHQPPKSLEPPPSTRGTNSEGDLKHNTYSSDGDSLAMRKNAPKNLHYDPKKIVPLTTSETYSPSARNHHHHRTKSPDKKRAPRHNGDYAYGDNLVGPSAQPFKPHTGGDVRWDAINSIASKGPQIGLDNFRLLKRLGYGDIGSVYLADLRGTNAVFAMKVMDKASLASRNKLLRAQTEREILSLLDHPFLPTLYSYFETDKFYCLVMEFCSGGNLHSLRQKQPSRRFTEEAARFYASEVLLALEYLHMLGVVYRDLKPENILVRD... | Function: Functions redudantly with AGC1-7 as signaling component in the pollen tube. Required for polarized growth of pollen tubes.
PTM: Autophosphorylated and phosphorylated by PDPK1/PDK1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 63768
Sequence Length:... |
Q1PFB9 | MLTKPGKKLDSSESTHHTTSSNYPPLDIVHQTPQPRKEMQQKPLFDPKKMDNLIKPEPAGFTNHHRPNPSPKIPSSPGSNMTESQSNLNTKPNNNNSNNNSNMSSRSNSIESTSSNPSKPHTGGDIRWDAVNTLTSKGVQLGISDFRLLKRLGYGDIGSVYLVELRGTITYFAMKVMDKASLASRNKLLRAQTEREILSQLDHPFLPTLYSHFETDKFYCLVMEFCGGGNLYSLRQKQPNKCFTEDAARFFASEVLLALEYLHMLGIVYRDLKPENVLVRDDGHIMLSDFDLSLRCSVSPTLVKSSSVHAAGGGSGSSRP... | Function: Functions redudantly with AGC1-5 as signaling component in the pollen tube. Required for polarized growth of pollen tubes.
PTM: Autophosphorylated and phosphorylated by PDPK1/PDK1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 61069
Sequence Length:... |
Q12482 | MEQINSNSRKKKQQLEVFKYFASVLTKEDKPISISNGMLDMPTVNSSKLTAGNGKPDTEKLTGELILTYDDFIELISSSKTIYSKFTDHSFNLNQIPKNVFGCIFFAIDEQNKGYLTLNDWFYFNNLLEYDNYHLIILYEFFRKFDVENLKAKQKKELGSSSFNLKAADDRIKSINYGNRFLSFDDLLLNLNQFKDTIRLLHESIDDNFVKDNKLLLDWNDFRFLKFYKCYHENEEYLSLNSLVTILQNDLKNEKIFIGFDRLAQMDSQGHRLALSKNQLTYLLRLFYSHRVSADIFSSLNLSNTELLKADNNSIPYNVF... | Function: Calcium-dependent mitochondrial aspartate and glutamate carrier. Transport of glutamate in mitochondria is required for mitochondrial transamination reactions and ornithine synthesis. Plays also a role in malate-aspartate NADH shuttle, which is critical for growth on acetate and fatty acids.
Location Topology... |
Q6LX42 | MDFVSLVNTVNSFVWGPYMLVLLLGTGIFLTLRLGFMQIHTLPYALKLAFSKHQDETSEGDISHFQALMTALAATIGTGNIAGVATAYVLGGPGAIFWMWVTAFFGMATKYAEAVLAIKYRTVDDNGEMAGGPMYFLEKGLPDHGLGKILGVAFAFFGAFAAFGIGNMVQTNSVADAVASNFGVDPLITGFVLAIFTAAVILGGIKSIGKATGIIVPFMAVFYILAGLVILAMNIGYIIPAFGTIFSSAFNFSAGFGALIGTAIMWGVKRGVFSNEAGLGSAPIAAAAAKTDHPGRQALVSMTGTFLDTIVVCTITGLVL... | Function: Catalyzes the sodium-dependent uptake of extracellular D-alanine and L-alanine . Can also transport glycine . Binds glycine and both enantiomers of alanine, while strictly excluding other amino acids .
Catalytic Activity: D-alanine(in) + Na(+)(in) = D-alanine(out) + Na(+)(out)
Location Topology: Multi-pass me... |
A9ZPJ6 | MKITVHSSKAVKPEYGACGLAPGCTADVVPLTVLDKANFDTYISVIYAFHAPAPPNAVLEAGLGRALVDYREWAGRLGVDASGGRAILLNDAGARFVEATADVALDSVMPLKPTSEVLSLHPSGDDGPEELMLIQVTRFACGSLVVGFTTQHIVSDGRSTGNFFVAWSQATRGAAIDPVPVHDRASFFHPREPLHVEYEHRGVEFKPCEKAHDVVCGADGDEDEVVVNKVHFSREFISKLKAHASAGAPRPCSTLQCVVAHLWRSMTMARGLDGGETTSVAIAVDGRARMSPQVPDGYTGNVILWARPTTTAGELVTRPV... | Function: Involved in the synthesis of hordatines (antifungal hydroxycinnamoylagmatine derivatives). Specific for agmatine as the acyl acceptor, inactive towards tyramine and putrescine. Has activity with the acyl donors 4-coumaroyl-CoA, cinnamoyl-CoA, caffeoyl-CoA, feruloyl-CoA, and to a lesser extent sinapoyl-CoA.
Ca... |
Q9FNP9 | MALKVIKISRVSPATASVDPLIVPLSFFDLQWLKLNPTEQVFFYKLTESSSSRDVFYSSILPKLERSLSLILTHFRLFTGHLKWDSQDPKPHLVVLSGDTLSLTVAETDADFSRISGRGLRPELELRPLIPELPIYSDSGAVVSLQVTLFPKQGFCIGTTAHHVVLDGKTAEKFNKAWAHTCKHGTIPKILPTVLDRSVVNVPAGLEQKMLELLPYLTEDDKENGRTLKLPPVKEINAKDNVLRITIEISPENIEKLKERAKKESTRAELHLSTFVVTFAHVWTCMVKARSGDPNRPVRFMYAADFRNRLEPPVPVTYFG... | Function: Involved in the biosynthesis of hydroxycinnamic acid amides, which play a role in defense against pathogens. Agmatine is the preferred acyl acceptor, lower activity is observed towards putrescine. The preferred acyl donor is p-coumaroyl-CoA, lower activity is seen towards feruloyl-CoA.
Catalytic Activity: 4-c... |
O82171 | MASENLNDKISVFKKLKAKSDNKICFDCNAKNPTWASVTYGIFLCIDCSAVHRSLGVHISFVRSTNLDSWSSEQLKMMIYGGNNRAQVFFKQYGWSDGGKTEAKYTSRAADLYKQILAKEVAKSKAEEELDLPPSPPDSTQVPNGLSSIKTSEALKESNTLKQQEKPDVVPVSPRISRSVKKPLGAKKTGKTGGLGARKLTTKSSGTLYDQKPEESVIIQATSPVSAKSARSSFSSRFDYADNVQNREDYMSPQVVSHVAPPKSSGFFEEELEMNGGRFQKKPITSSSKLQIQETDEARKKFTNAKSISSAQYFGNDNNS... | Function: GTPase-activating protein (GAP) for ADP ribosylation factor (ARF). Activates ARF1 and ARF2. Required for female gametophyte development. Involved in root hair and pollen tube growth.
Sequence Mass (Da): 43097
Sequence Length: 395
Domain: The C-terminal domain (317-395) is responsible for the Golgi localizatio... |
Q8U3P6 | MKIDKRLMVIVAIATLFRMIPFRLKYLVGSDPYFHLAYIEEALKAGEWFNFFTYAGGPWGLQVRLFHPLGLWATPAYIYKLFSFLGISLYTAFRVTPVIFGVLTVVFFYLSLKKLYNRDVAFIVGLFLGVNYGHIFRSMANYYRGDNYMLFWYSVALLGIALGLKTRSKYRYLFYLLPGIATGFASAFWQAYYPIFVFVLAGGLLLGVYAYLKSPKLFLDSILIVLSTGLGVLIANILGDKVGYGMLGYTDWMGKKVAETFGLEFGFIKDAYLLIHVKYLLPLSLVFLGFLIITKKLNPKIKVGVLVGGSILAFIVMLVK... | Function: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in P.furiosus) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycos... |
O58981 | MKRRYSILIILLVAIFYRMITFRFKYLLGYDPYFHLAYIEEVNKVGKWINFLTFAGGPWGYQVKLFHPLGLWMTPLYLYKLLKVFGVSLTTTFKITPVIFGVLTVIFLYLSLLKLYDEKRAFFGGFFLAISYGHVFRSMANYYRGDNYMLFWYSVALLGISLALGIKKGKWKYKRLIFYTLPVLASGFSAIFWQAYYPIFAFLLSNALLLAVGAFILKKDKYLLDSIILILSTAFGVLLANYLGGIFGYGMLGYAKWLGKSVAKKLGLEFGYLKDVYLILHLKYLVPISLSFVLVLILLGFLTKDIRIRSLFLGIASFIG... | Function: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in Pyrococcus) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycos... |
O29867 | MQNAESWFKKYWHLSVLVIAALISVKLRILNPWNSVFTWTVRLGGNDPWYYYRLIENTIHNFPHRIWFDPFTYYPYGSYTHFGPFLVYLGSIAGIIFSATSGESLRAVLAFIPAIGGVLAILPVYLLTREVFDKRAAVIAAFLIAIVPGQFLQRSILGFNDHHIWEAFWQVSALGTFLLAYNRWKGHDLSHNLTARQMAYPVIAGITIGLYVLSWGAGFIIAPIILAFMFFAFVLAGFVNADRKNLSLVAVVTFAVSALIYLPFAFNYPGFSTIFYSPFQLLVLLGSAVIAAAFYQIEKWNDVGFFERVGLGRKGMPLAV... | Function: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a glucose-linked heptasaccharide composed of 3 Glc, 2 Man, 2 Gal and a sulfate for A.fulgidus AglB-L) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nasc... |
Q58920 | MYIKVKLMSNALEKINNFFKEKSWIKVFLIILMLMFVSFQLRAQTADMKFAQDNEFLKDMFSDEHGRMYLLALDPYYYLRLSENLYNNGHCGDTIKVVDGKETPYDLYQYAPPGHPLPWEPPVICLATLAIYYIWHSIDLTVTIMNAAFWVPAVLGMLLGIPIYFVVRRVTNSNIGGIAGAIALISAPGLLYKTCAGFADTPIFEVLPILFIVWFILESIHSQEKTALFKKDLKNPISLFVIAALIIELIIGAYLNIASGESVVIASILFYTVSLAFILAGLIIAGIKKLKGNELEFELFALLAVILTAVSPKMWGAWWY... | Function: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcGlc-2,3-diNAcAGlcNAc in Methanococci) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycos... |
Q2EMT4 | MTENNEKVKNSDSANNQSSKNSKFNFNFEDKKVKCAKTILIIIFLAFLSFQMRAQTADMGFTTNEQYLDVFSDDNGRMYLTALDPYYYLRMSENYLENGHTGDTLKNIDGQQVPWDSYKYGPTGARATFNLLSVVTVWVYQVWHAMDSTVTLMNAAFWVPAILSMFLITPIFFTVRRITSSDIGGAVAAILASLSPSIFVKTVAGFSDTPILEILPLLFIVWFIIEAIHYSKEKNYKSLIYGLLATLMLALYPFMWSAWWYGYYIVIAFLVIYAIYKGISYNSIAKYTKSKNNNHKDKIESEKLEMLNILKISGLFIIGG... | Function: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcGlc-2,3-diNAcAGlcNAc in M.voltae) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylat... |
Q9X2F4 | MMYPMPSWVYDSVVYQIFPDRFFIGKGKTVEDKKDLYLKRGGVIEKWGVPPRKLPGAQHVKIFYGGDLWGIAEKVDYFEELGINVLYLTPIFLSDTNHKYDTIDYFRVDPQFGGKRAFLHLLRVLHERSMKLILDGVFNHVGSQHPWFKKAKKNDPEYVNRFFLYKDRHRSWFDVGSLPELNVEVEEVKEYILKVVEHYLKLGIDGWRLDCGHDLGPTVNLWINMKVKEFSAEKYLVSEIWTYPAGWDMVDGLMNYNFRNLVLSYVNGETDSIGFHLERAYRETKNIFGCWNMLDSHDTPRLATMVPDRDLRKLAVVLQF... | Function: Is able to hydrolyze various linear maltooligosaccharides (maltotriose to maltoheptaose) and cyclomaltodextrins (CDs), to mainly glucose and maltose, by liberating glucose from the reducing end of the molecules. Shows a very weak activity on starch. Can neither hydrolyze maltose nor degrade pullulan, but rapi... |
B3VA59 | MNFISIIIPTFNEEKYITKCLENWFNQDYPKENYEILIFDGKSTDKTLDVIKELQKKHNFENIKIYTNEKRKQVYAFNEGIKNANGDFFIIFGAHAYPEQDFLKNNIETYQRIKKEEPKLAGVGGIINKISENMSAEIAKVIYSTPLSGGSSFWYAKEGFFSNTVVYGMYDTKMIKESEILFDTDFITGQDFEFNLHLIKEGFKLYTNPNIVSSYYTRSSVKKFIKQTISYGAAKGLMIRKGYFNILWLFPFGFLFMLLSIIITGLLIFIYIMAILIDTIRLLIKTREPLYIALPILLFLFHCLISYGFFKGLIKGNSTF... | Function: Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins . AglC catalyzes the transfer of 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (Glc-2,3-diNAcA) from uridine 5'-diphospho 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-Glc-2,3-diNAcA) t... |
D4GUA0 | MGRPTERRPAAATAAGVEVSVVLPAYNEARTIENTVRVTVETLESFLPADAFEVIVAEDGCDDETPEIADRLAAEDDRIRHYHSDDRLGRGGALERAFEAARGDTLVYFDTDLATDMRHLEELVERVRSGEYDAATGSRWMPDRVADRPRKRGVPSRAYNGLVRLFLRSDLRDHQCGFKAFSREAFEALRDDVEDNHWFWDTEMLVRAQRAGFRVAEFPVDWEPKGDTKVDLVRDILGMGSQILRTWWQLTVRPRITRRVTIVAGLLLTVLALALMTLYIDPSEVISVLGDADPALVAAAAVIYVVSWPLRGIRYREILR... | Function: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition of the mannose found at position 5 of the pentasaccharide to its own distinct dolichol phosphate carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 669... |
D4GYG7 | MTSTLPFVSVIIPVYNEAENIQKCLNAVTSQTYPKSKYEVLVVDNGSQDGTKEIARQFSTAYDNLEILIEDEQQGSYAARNTGIEQSSGAILAFLDGDCSPHQQWLERGVSTISGTGVDLVGGNVEFTYPNGGTAAERYDSFTNMQMKESISKRNVAKTVNLFVRQDVVEDVGPFPNHLISGGDVHWTKRATDAGYSLTFAHDVIGCHPARPFGELLKKQFRVGKGQIQVWMLDRISLRRVFALALWILVGFLPKPPHYLSQDLRRTGQTVTKAMFVRILVVAWCCRLAENAGRLSYILRSEEQ | Function: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition to the dolichol phosphate carrier of the hexuronic acid found at position 4 of the pentasaccharide.
Sequence Mass (Da): 33869
Sequence Length: 304
Pathway: Cell surface structu... |
D4GYH1 | MQAVVLAAGKGTRLRPLTEDKPKGMVEVDGKPILTHCFDQLVDLGAEKLVVVVGYKKEIIIQHYDDEYRGVPITYAHQREQKGLAHALLTVEDHIDEDFMLMLGDNIFNANLGDVVKRQREDRADAAFLVEEVDWDEASRYGVCVTNDYGEITEVIEKPEEPPSNLVMTGFYTFTPAIFHACHLVQPSNRGEYEISEAIDLLIRSGRTIDAIRIDGWRLDIGYPEDRDEAEQRLQEETTQATE | Function: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Involved in the biosynthesis of the hexuronic acid found at position 3 of the pentasaccharide.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequenc... |
Q9Z3R6 | MEQLIAAILTMVAGVLVCAAYFWSTNLVLDWIFPSKGKFGAVASRNLRIANSIRPWLFLAPALLALTLYLVYPVVQSVWLSLHGRGGQNFVGLSNYSWMINDGEFRQSIFNNFLWLLVVPALSTFFGLIIAALTDRIWWGNIAKTLIFMPMAISFVGAAVIWKFIYDYRAAGSEQIGLLNAIVVALGGEPQAWITLPFWNNFFLMVILIWIQTGFAMVILSAALRGIPEETIEAAVIDGANGWQIFFKIMVPQIWGTIAVVWTTITILVLKVFDIVLAMTNGQWQSQVLANLMFDWMFRGGGDFGRGAAIAVVIMILVVP... | Function: Part of the binding-protein-dependent transport system for alpha-glucosides such as sucrose, maltose and trehalose. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37399
Sequence Length: 336
Subcellular Locatio... |
D4GYH3 | MKVSVVVCTYSMERYESFSETVESVLAQTYEPLELVIVVDGNEEEFDRVQDDFGDIDDVVLHCNDENRGISYSRTKGAELGTGDVVAMIDDDATAEPDWIETLVDTYENNPDAVAVGGTVVPDWVARKPEFFPEEFYWLVGCDERGFGEHMEEVRNTYGSNISFKRDVFLEVGGYDTNTGRKGDKHVQAHEAPVCIRIYEQTGERVIYNKQARVNHKLFEYRTEFDWLVFRSFWQGYSKRVMDLLYPQASDDKNAYLKDLMLVYVVDRLKNLVEDPSLAQVQQLIAIFVFTAAVGFGYVYGLLTPNLVEKTNN | Function: Involved in the protein N-glycosylation pathway responsible for the assembly and attachment of an N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins . Catalyzes the transfer of a glucuronate residue (GlcA) to a glucose residue already bound to a dolichol phosphate (DolP), a compou... |
Q9Z3R7 | MNPSRRSPLTWAVHLSVLLLVLLWTLPTAGLLISSLRDKDQLAVSGWWTALSSSSRNAVVRAPSAEDQVERDGKFVISGNLLEGRGEVSAFGFSSREPTKFKPGETAELNDGERLTVQSDGSFEIVSDQRMEGSRGQRIFFTATTPPRFTLDNYAEVLSAAGIGRSFLNSLTVAVPSTVIPILIAAFAAYALAWMPFPGRAVLLAVVVGLLVVPLQMSLIPLLQLYNGVGAFFGVSAKTYMGIWLAHTGFGLPLAIYLLRNYMAGLPREIMESARVDGASDFDIFVKIILPLSFPALASFAIFQFLWTWNDLLVAIVFLG... | Function: Part of the binding-protein-dependent transport system for alpha-glucosides such as sucrose, maltose and trehalose. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41127
Sequence Length: 380
Subcellular Locatio... |
D4GYH2 | MADSPFPCVSVIVPVYNDPTGIRDTLTALTKQTYPTERVNILPIDNGSTDETRDVIRQFEREHENVTLVVEDEIQGSYAARNTGIEQATGEIFAFVDADMYMDESWLETAVDAMDEAAYVGCDIELVTNGEDTLPARFDAQTAFPIAQYIRQQQYAPTCGLLVSREVVDDVGPFDERLVSGGDSEFGSRVANAGYRQAFAPAATLYHPVRDSFSSLVKKELRVGRGLCQRQEYYADRFGRPGIPPRPSGVKSPDEESSGLDFERLLFGVLSVVMTGVRALGYYREYVRYVRGNTR | Function: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition to the dolichol phosphate carrier of the hexuronic acid found at position 3 of the pentasaccharide.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32846
Se... |
P19926 | MNKTLIAAAVAGIVLLASNAQAQTVPEGYQLQQVLMMSRHNLRAPLANNGSVLEQSTPNKWPEWDVPGGQLTTKGGVLEVYMGHYMREWLAEQGMVKSGECPPPYTVYAYANSLQRTVATAQFFITGAFPGCDIPVHHQEKMGTMDPTFNPVITDDSAAFSEQAVAAMEKELSKLQLTDSYQLLEKIVNYKDSPACKEKQQCSLVDGKNTFSAKYQQEPGVSGPLKVGNSLVDAFTLQYYEGFPMDQVAWGEIKSDQQWKVLSKLKNGYQDSLFTSPEVARNVAKPLVSYIDKALVTDRTSAPKITVLVGHDSNIASLLT... | Function: Absolutely required for the growth of E.coli in a high-phosphate medium containing G-1-P as the sole carbon source.
Catalytic Activity: alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate
Sequence Mass (Da): 45683
Sequence Length: 413
Subcellular Location: Periplasm
EC: 3.1.3.10
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