ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q5A651 | MDLVIMNFVFLLYLTSVVKCSIKLDFNKVSTPSKYTKRDALPMPLINDKILYTTELEIGSNKDKVSVSIDTGSYDLWVMSNDAVCYKVSEFQTEGAPQLPDIFNDIDQDYSCTFNGTYNSKSSKTFKNTSEDFSIGYVDGSAAQGVWGYDSVQFGQYGVTGLKIGIANRSSVSDGILGIGIANGYDNFPVLLQKQGLINKIAYSVYLNSSNSTTGTILFGAIDHAKYKGALSTVPVDSKSQLSVNVTNLKTKNGNVASGGHSILLDTGSTFSIFPDEWIDALGHSLNATYDEDESVYEIECDGYDEHFFGFSIGDSDFSV... | Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Required for cell surface integrity and cell separ... |
Q9BXL6 | MGELCRRDSALTALDEETLWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPDVYTLVTGLQPDVDFSNFSGLMETSKLTECLAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQRE... | Function: Acts as a scaffolding protein that can activate the inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase signaling pathways. Forms a signaling complex with BCL10 and MALT1, and activates MALT1 proteolytic activity and inflammatory gene expression. MALT1 is indispensable for CARD14-induced activ... |
Q9WVG6 | MAAAAATAVGPGAGSAGVAGPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDAAGIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLIQFATPHDFCSFYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFH... | Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability . Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and ... |
Q54ST2 | MTKNKSKNKSNNSNISNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNGESQLKNKNKNISENQHIYDKHNHDHSHDHNHDYDDNNEDDEEKEELEHYQLIVSTLLNYSQYSLHWVKDMQDFFHYKLSEDEKKLLPNYNAKMEALARAVLVNSQFLKKIGNEHCNIFSQSSDNSANSERIVDPTNLDHIKIDYFMMDQLKSTIRQLVREWSEEGKLERDQAFEPIKQQLLEIYGHIPFQERSKIRVYSPGAGLGRLCLEIASLGFSSQGIEYSFMMLIVSNFMLNKVEKINEFKIHPYIHQTVNVLRDID... | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine.
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 54029
Sequence Length: 463
EC: 2.1.1.22
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Q9I7X6 | MSSMDCATFPMHPKMDEQLARTFVINEEEEEKHIQKVQNAFLYYGPYACQRLKRSMDYLNSLSGEDQIMLAKYRGHLECVRTCIDRNQAVIREILRGRVLYPTDEATGDPSEFDEPPPNVRHGDMDQAQSTLKLIARDWSTEGALEREQSYKPIIDSIVAYFKHSDFELKDIKILVPGAGLGRLTYELACLGYSCEGNEFSYFMLIASNFVLNLCDNENKYVLYPWVHQYVNNLRREDQVAPVRFPDVCPLKNPPKGHFEIAAGDFLEVYKTPNAYNCVATCFFIDCANNVIDFIRTIYKILVPGGIWVNLGPLLYHFSD... | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine.
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50504
Sequence Length: 439
EC: 2.1.1.22
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Q8N4J0 | MQRRRRPPPPTSRLPEGCGGGGGGSEEVEVQFSAGRWGSAAAVSAAAAAATRSTEEEEERLEREHFWKIINAFRYYGTSMHERVNRTERQFRSLPANQQKLLPQFLLHLDKIRKCIDHNQEILLTIVNDCIHMFENKEYGEDGNGKIMPASTFDMDKLKSTLKQFVRDWSETGKAERDACYQPIIKEILKNFPKERWDPSKVNILVPGAGLGRLAWEIAMLGYACQGNEWSFFMLFSSNFVLNRCSEINKYKLYPWIHQFSNNRRSADQIRPIFFPDVDPHSLPPGSNFSMTAGDFQEIYSECNTWDCIATCFFIDTAHN... | Function: N-methyltransferase that catalyzes the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripepti... |
Q5BJZ6 | MQRRRRAPPASQPAQDSGHSEEVEVQFSAGRLGSAAPAGPPVRGTAEDEERLEREHFWKVINAFRYYGTSMHERVNRTERQFRSLPDNQQKLLPQFPLHLDKIRKCVDHNQEILLTIVNDCIHMFENKEYGEDANGKIMPASTFDMDKLKSTLKQFVRDWSGTGKAERDACYKPIIKEIIKNFPKERWDPSKVNILVPGAGLGRLAWEIAMLGYACQGNEWSFFMLFSSNFVLNRCSEVDKYKLYPWIHQFSNNRRSADQIRPIFFPDVDPHSLPPGSNFSMTAGDFQEIYSECNTWDCIATCFFIDTAHNVIDYIDTIW... | Function: N-methyltransferase that catalyzes the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripepti... |
Q9Y7J3 | MEYDEEEVKVLKEVLSAFFLYRQYAHTITQQKRKSMSRLSFEHKDLLLQDSDNNFLKHLSRIDQCIEQNSVLAEAIANAAIPVFCSDFDQNELFHVNVDMMQKVSSTLKQIARDWSTECVEERRTTYAPFIEELNSLFPSDSIDRSKIRVLVPGSGLGRLAFDIAVEGFACQGNEFSYFMLLTSHFILNCVKQENQFLVYPYIHSFSNHVMRDDQVRSLNIPDAVPSQYLRNSQNFSMAAGDFLEVYGTEESRDSFQVVATCFFIDTTKNILDYLDTIKNCLVDGGYWINLGPLLYHFESEGTSNSNSDSQQQPFVELTL... | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(... |
P53934 | MDENEFDNQRENKAVARVIISFLKYEEYALKEIYNLRVKKWASISDRQKDMVPNYTKYLANLKAAIIENGKFFRSVAEYALQSISFEPGEIVQPNDLDMSKTCSLLTQVYREWSAEAISERNCLNSRLVPFLKTLSPPKADILIPGCGTGRLLVDLSRMGYNCEGNEFSYHMLLVSQYMLNAGLLQNQIIIYPFIHCFSHWKKIEDQLSPIKVPDIEAWSSNKGMGSMSICAGSFVDCYGRNQGTKISSHYTFSRRMQLSRAKAENSKDVVVTNFFIDTGSNILDYLDTIGHVLKPGGIWCNFGPLLYHFENDHGVETTY... | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(... |
D0C9N4 | MDMDNQNTKIYTDKFLAVTSLLFVFISVAGLAIYSQESIKIAATWMQWTTSVFTTPVLLFAFLAIIFTFGLAFSKYGKIKLGEGKPQYSTMSWIFMFILSGIGSSTLYWGFLDWAYYYQTPGLSLPPESAEALKYSVAYSFFHSGLSAWAIYALASISLCYSYHVRKNKGLSLASVIEAVTGFKSTGVVGRLVDLMFLLCMFGALTISLVLTAVTFTNILSQLTGIPNTFMTKVIIILAVSVLFALSSYVGMDKGMQRLSHMVCLGVVLFAIYVLCFGPTQFILNNSLMSFGLMATNFVDMSLFTDPMGDGKFTREWTVF... | Function: Catalyzes the energy-dependent uptake of carnitine and is essential for growth on carnitine. Can also mediate the uptake of choline. Is probably a proton:substrate symporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60971
Sequence Length: 550
Subcellular Location: Cell inner membrane... |
S0ELR6 | MADHLYARKNDALNVNPDIVNGQRSDINITVRGSDWYWAVCAVMTVSTFAFLGLGMRKPRTDRIFHYITAGITMIASIAYFTMASNLGWTPIAVEFQRSNHRVAGIYREIFYARYIDWFLTTPLLLTDLLLTAGMPWPTVLWVILVDWVMIVTGLVGALVKSSYKWGYFAFGCAALAYIVYVLAWEARLHAKHVGPDVGRTFVMCGSLTAVVWILYPIAWGVCEGGNLIAPDSEAVFYGILDLIAKPVFGALLLWGHRNIDPARLGLRIRDIDERIFPDGPNNKVASGHGARNDTATASGSNVNPNA | Function: Opsin-like protein; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation . The exact role of carO in carotenoid biosynthesis is not known yet, but it could be involved in the r... |
F2XG53 | MKHINDYFWAKKTEENSRLLWLPLTQHLEDTKNIAGLLWEHWLSEGQKVLIENSINVKSNIENQGKRLAQFLGAVHDIGKATPAFQTQKGYANSVDLDIQLLEKLERAGFSGISSLQLASPKKSHHSIAGQYLLSHYGVDEDIATIIGGHHGRPVDDLDGLNSQKSYPSNYYQDEKKDSLVYQKWKSNQEAFLNWALTETGFNSVSQLPKIKQPAQVILSGLLIMSDWIASNEHFFPLLSLDETDVKNKSQRIETGFKKWKKSNLWQPETFVDLVTLYQERFGFSPRNFQLILSQTIEKTTNPGIVILEAPMGIGKTEAA... | Cofactor: Mn(2+) or Mg(2+) or Ca(2+). ATPase and nuclease activities are dependent on divalent cations, for ATPase Mn(2+) is marginally preferred over Mg(2+) or Ca(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genet... |
Q53VY2 | MSVEEAALALWAKSGNPFHPLLAHMLDTAAVALAVLRMEPPRTRALYAEDWGLPEEGALAWAAALVGLHDLGKASPVFQAGWEEGKERVQRAGLPFGELLDWVAHGVFTELFLRRLLKEKGLPERAANDLAAALGAHHGFPANAEEKSRARRHLRTEDPLWKEARRWLLEEVFRRLGAPLPPSQGNGEARPEAVLRVMALASFADWVASDPSLFPYGRDPRRGDYLKEALRLAQEALNRLGWPAFAKAQRREFGELFPYIPKPNALQESVPALLEGACTPVLLLVEAPMGMGKTEAALYAHHLLQAGLGHRGLYVALPTQ... | Cofactor: The ssDNA endonuclease activity (residues 6-260) is stimulated by Mn(2+), Co(2+), Ni(2+), Cu(2+) and Zn(2+), but not by Mg(2+) or Ca(2+). A Ni(2+) ion is seen in crystals upon soaking.
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides prote... |
Q9YCL9 | MRPVSMLKEYAYCPRVAYYMEVLRPSYRPTEPMNLSREIYSVDHVRGILRSSGFRIVKEEWAVPLRSKRLGLQGVADGVVVEGSLGIIVVEAKLSVRSNRWLHTRGRHVIFQAAAYALALEETRGYSVDYLAIVSLEDSKTYVVKMSPSLRRDVIRLADDMNKTLDDGLEPPPKPGRKCVACRFRRVCQPWVAERGSER | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR cl... |
A0Q5Y6 | MNMDIFDNDLSIPVNLIRQWCFCPRIVYYQELLAIKPNKPLWVAQGEEFHKKVEQLEKRRSFSRYGLENAIRHFNLSIKSQKYKLHGIVDWVIETDTNVYVVEYKTNPNPNSLGHKLQIAAYALLVQEYFAKPCKTTFLTSDKKSYEIKITDELINKLIKTISDILSTLDSGNKPDSSASDHQCIQCEYYNFCNDR | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences ... |
D4GQN9 | MSSTDVVEEYVQDERDPSRSPNVPITGLMVQYYHVCKRELWFMANGIDIDRETTNIQRGTHVDETSYGTSRRSFMIDNRIQLDILDSGDVMEVKVSSALEKPARMQLLFYLWYLREIHDIDKDGVLAYPTERKRESVVLDETTTAEVESTVRGVLDVVGRDSPPQLEKKPYCGTCLYQDLCWM | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR cl... |
Q57822 | MENYLEEELIIGGIEINYLYVCKTKLWYFVRGITMEQESDFVDLGKFLHEKSYFGEEKEVQIGSIKIDFIKKRDVIEIHEVKRGKQMEKAHIMQVLYYIYYLNSLGIKSKAILHYPKLKEIKEIELKENNKEEIKRAIKEIEYIKSLKEPPEPIYQKICKNCAYYELCFI | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR cl... |
A3MTK6 | MELLSPKPLCSVVNCEDLEKLDHVSALNELRREQEIFKLLPGIYAHRYDFRRVSPSIINDFEYCPRLLWVQHKLGLKLLSEKSVVSIIRGRILHERYERLLSQYENVVAEYKVEIGDLVGVVDLVIKRGGEYIPVEIKTGFSKEAHKTQLQIYISMLKARFGYLVYRNHVEVVHRNDAALDVLKKIREILSAREAPPAKCNSCIFKPICKNLL | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. Not required for nuclease activity, since mutation of the Cys residues leads to a colorless but active protein.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic element... |
Q2RRV2 | MAPSDTPPSAEDLPSQGELALFAPPATAEDALVPASMVNAWIYCPRLAVLEWGRGEKARSVDLIAGLRAHQATESGPTPALPDPMVLREDQSLKTRKLSLSSERLGLTAELDLLDVEEGVVIPVEIKVGKRPSVDEGAYLPERAQVCAQALLLREAGYTCLEGALWFAESRERVTVDLTEALVTATLVATSDLRLTVASGRLPPPLDHSAKCPRCSLLPICLPDEIAWFRKGSIARTPPPPASPALPLYGQTPGARIGKKDRGGSVCLDRMAAWLSSRPVPCYAAIGMLNTASGASHPSVARHADGGASARSFRLPTAFR... | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR cl... |
Q97TX9 | MITEFLLKKKLEEHLSHVKEENTIYVTDLVRCPRRVRYESEYKELAISQVYAPSAILGDILHLGLESVLKGNFNAETEVETLREINVGGKVYKIKGRADAIIRNDNGKSIVIEIKTSRSDKGLPLIHHKMQLQIYLWLFSAEKGILVYITPDRIAEYEINEPLDEATIVRLAEDTIMLQNSPRFNWECKYCIFSVICPAKLT | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR cl... |
G4RJY5 | MSLCINPSLIRQYLYCPMAAYYIAAGAPEPPTLRMQRGREIQQEAAQAAAKALGAERAEYSVHITAPPLCGTVDAVLWINGRPSPLEVKAAARPRRIPIHHKAQAAAYIAMVQRAYGRAVATAYIYYAESGQIAQIRMAKDLQELLNYAVSRLQQILQGKPPVLNPNPAKCQNCWYRKWCSHLPTTVEKI | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR cl... |
Q65TW5 | MANRIRLHIWGDYACFTRPEMKVERVSYDVITPSAARGILSAIHWKPAINWVIDKIYVLKPIRFESVRRNELGAKISESKVSGAMKRKSVADLYTVIEDDRQQRAATVLKDVAYVIEAHAVMTSKAGVDENTTKHIEMFKRRALKGQCFQQPCMGVREFPAHFALIDDNDPLPLSQLSESEFNRDLGWMLHDIDFEHGNTPHFFRAELKNGVIDVPPFYAEEVKR | Cofactor: Does not require a metal cofactor.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementa... |
Q746C2 | MARLKVKVWGEYACFSRPEFKVERVSYPVPTPSAARGLLEAIFWKPEFRYEVRRIGVLRLGTPFALLRNEVGNRMGAKPFFVEDARQQRTSLVLKDVAYLVEADMVLRPHATDPLPKYLEQFERRLKKGQYHHTPYLGTREFPAYFSPPDGEVPDGGLNLDLGPMLFDLAFVEDPGRPELTFKRPGRGEVQGYALPLFFHARIREGWLEVPAEKYQELYRLEEGHAKGA | Cofactor: Does not require a metal cofactor.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementa... |
P70677 | MENNKTSVDSKSINNFEVKTIHGSKSVDSGIYLDSSYKMDYPEMGICIIINNKNFHKSTGMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSKEDHSKRSSFVCVILSHGDEGVIYGTNGPVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTDEEMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESFSLDSTFHAKKQIPCIVSMLTKELYFYH | Function: Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis . Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins . At the onset of apoptosis, it proteolytically clea... |
Q95ND5 | MENNKTSVDSKSIKTLETKILHGSKSMDSGISLDVSYKMDYPEMGLCIIINNKNFDKNTGMACRSGTDVDAANLRETFTNLKYEVRNKNDLTREEILELMHSVSKEDHSKRSSFICVLLSHGEEGKIFGTNGPVDLKKLTSFFRGDCCRTLTGKPKLFIIQACRGTELDCGIETDSGTEDDMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAALKQYVHKLELMHILTRVNRKVAVEFESFSTDSTFHAKKQIPCIVSMLTKELYFYH | Function: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-heli... |
P55866 | MEESQNGVKYGGDATDAKEYFTIQPRSLQNCDLKDIERKTKFAHLQNYRTNYPEMGMCLIINNKNFHSSNMAVRNGTDVDALKLHETFTGLGYEVMVCNDQKSSDIIGRLKKISEEDHSKRSSFVCAILSHGEEDGSICGVDVPIHIKNLTDLFRGDRCKTLVGKPKIFFIQACRGTELDSGIETDSCSEPREEIQRIPVEADFLYAYSTVPGYCSWRDKMDGSWFIQSLCKMIKLYGSHLELIQILTCVNHMVALDFETFHAKKQIPCVVSMLTKSFYFFK | Function: Important mediator of apoptosis. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond (By similarity).
Catalytic Activity: Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- w... |
Q5E9C1 | MAEDKHNKNPLKMLESLGKELISGLLDDFVEKNVLKLEEEEKKKIYDAKLQDKARVLVDSIRQKNQEAGQVFVQTFLNIDKNSTSIKAPEETVAGPDESVGSAATLKLCPHEEFLKLCKERAGEIYPIKERKDRTRLALIICNTEFDHMPPRNGAALDILGMKQLLEGLGYTVEVEEKLTARDMESVLWKFAAREEHKSSDSTFLVFMSHGILDGICGTMHSEEEPDVLPYDTIFRTFNNRNCLSLKDKPKVIIVQACRGANRGELWVSDSPPALADSFSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDIKKGS... | Function: Inflammatory caspase that acts as the effector of the non-canonical inflammasome by mediating lipopolysaccharide (LPS)-induced pyroptosis (By similarity). Also indirectly activates the NLRP3 and NLRP6 inflammasomes (By similarity). Acts as a thiol protease that cleaves a tetrapeptide after an Asp residue at p... |
P49662 | MAEGNHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQISPNKKAHPNMEAGPPESGESTDALKLCPHEEFLRLCKERAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGICGTVHDEKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGS... | Function: Inflammatory caspase that acts as the effector of the non-canonical inflammasome by mediating lipopolysaccharide (LPS)-induced pyroptosis . Also indirectly activates the NLRP3 and NLRP6 inflammasomes . Acts as a thiol protease that cleaves a tetrapeptide after an Asp residue at position P1: catalyzes cleavage... |
Q59602 | MTTSKCPVTHLTMNNGAPVADNQNSLTAGTRGPLLTQDLWLNEKLADFVREVIPERRMHAKGSGAFGTFTVTRDITKYTRAKIFSEVGKKTEMFGRLATVAGERGADAYTRVRGFALKFYTEEGNWDVVGNNTPVFYPDLRKFPDLNKAVKRSAHQYSSATNNWDFWALLPEALHQVTIVMSDRGIPASYRHMHGFGSHTYSLWNEAGERFWVKFHFRSQQGIKNLTNEEAAKIIADDRESHQRDLYEAIERGEFPKWTMYIQVMPEADAAKVPYHPFDLTKVWPKKDYPLIEVAEFELNRNPENFFADVEQSAFAPSNL... | Function: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 56671
Sequence Length: 500
EC: 1.11.1.6
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P11934 | AAAQRRQNDSSVFLAIMVAAAVESESSLTDGDAGALLLQDISEWDEVFRFDRLEAVERAAHAAAAAAFGAFVARGDWTASAAAAFQAAGKQIAFMAAFSTVAGAKGSATVRDADAFAAKFASAAALQELVGNNSPISFFIFDLLFAAILFASKAKAANQAAFAAAAELAAESLFVRLPSLHQVSFFALAGFAAVAAHRHMNGYGSHTFKLVAKDGSVYCSKFWYKADQGQAAEVWKDAEEVAAEDVDYFRDLNFQAEAAGRYPLWELASQVMTFSDFEIDPFNENIPTKVVPRESVPLIVDAELLLNRNPLNMFAEVEQV... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 70260
Sequence Length: 670
Subcellular Location: Peroxisome
EC: 1.11.1.6
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P42321 | MEKKKLTTAAGAPVVDNNNVITAGPRGPMLLQDVWFLEKLAHFDREVIPERRMHAKGSGAFGTFTVTHDITKYTRAKIFSEVGKKTEMFARFSTVAGERGAADAERDIRGFALKFYTEEGNWDMVGNNTPVFYLRDPLKFPDLNHIVKRDPRTNMRNMAYKWDFFSHLPESLHQLTIDMSDRGLPLSYRFVHGFGSHTYSFINKDNERFWVKFHFRCQQGIKNLMDDEAEALVGKDRESSQRDLFEAIERGDYPRWKLQIQIMPEKEASTVPYNPFDLTKVWPHADYPLMDVGYFELNRNPDNYFSDVEQAAFSPANIVP... | Function: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 55614
Sequence Length: 484
Subcellular Location: Cytoplasm
EC: 1.11.1.6
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P04762 | MADSRDPASDQMKQWKEQRAPQKPDVLTTGGGNPIGDKLNIMTAGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDAMLFPSFIHSQKRNPQTHLKDPDMVWDFWSLCPESLHQVTFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLPVEEAGRLAQEDPDYGLRDLFNAIASGNYPSWTFYIQVMTFKEAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNR... | Function: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and t... |
P95607 | GSGSAATDKFKAERATADTSPERLAAIAKDALGALNDVILKHGVTYPEYRVFKQWLIDVGEGGEWPLFLDVFIEHSVEEVLARSRKGTMGSIEGPYYIENSPELPSKCTLPMREEDEKITPLVFSGQVTDLDGNGLAGAKVELWHADNDGYYSQFAPHLPEWNLRGTIIADEEGRYEITTIQPAPYQIPTDGPTGQFIEAQNGHPWRPAHLHLIVSAPGKESVTTQLYFKGGEWIDSDVASATKPELILDPKTGDDGKNYVTYNFVLDPA | Cofactor: Binds 1 Fe(3+) ion per subunit.
Catalytic Activity: catechol + O2 = cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 29704
Sequence Length: 270
EC: 1.13.11.1
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P55306 | MNSKDSNTVPVYTTNTGCPIFNPMAAARVGKGGPVLLQDSHLIDVFQHFDRERIPERVVHAKGSGAFGEFECTDDITKYTKHTMFSKVGKKTPMVARFSTVGGERGTPDTARDPRGFALKFYTDEGIFDMVGNNTPVFFLRDPAKFPLFIHTQKRNPQNDMKDATMFWDYLSQNAESIHQVMILFSDLGGTPYSYRFMDGFSSHTYKFVNDKGEFYYCKWHFITNQGTKGLTNEEAAALDGSNPDHARQDLFEAIERGDYPSWTLYVQVMTPQEAEKYRYNIFDLTKVWPHKDVPMQRVGRFTLNQNPTNFFADIEQAGF... | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 58279
Sequence Length: 512
EC: 1.11.1.6
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P07711 | MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRN... | Function: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of th... |
P06797 | MNLLLLLAVLCLGTALATPKFDQTFSAEWHQWKSTHRRLYGTNEEEWRRAIWEKNMRMIQLHNGEYSNGQHGFSMEMNAFGDMTNEEFRQVVNGYRHQKHKKGRLFQEPLMLKIPKSVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHAQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEFAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKNLDHGVLLVGYGYEGTDSNKNKYWLVKNSWGSEWGMEGYIKIAKDRDN... | Function: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen . In neuroendocrine... |
Q94714 | MMLLGASLYLNNTQEVSDEIDTANLYANWKMKYNRRYTNQRDEMYRYKVFTDNLNYIRAFYESPEEATFTLELNQFADMSQQEFAQTYLSLKVPRTAKLNAANSNFQYKGAEVDWTDNKKVKYPAVKNQGSCGSCWAFSAVGALEINTDIELNRKYELSEQDLVDCSGPYDNDGCNGGWMDSAFEYVADNGLAEAKDYPYTAKDGTCKTSVKRPYTHVQGFKDIDSCDELAQTIQERTVAVAVDANPWQFYRSGVLSKCTKNLNHGVVLVGVQADGAWKIRNSWGSSWGEAGHIRLAGGDTCGICAAPSFPILG | Function: May be involved in extracellular digestion.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 35159
Sequence ... |
Q28944 | MKPSLFLTALCLGIASAAPKLDQNLDADWYKWKATHGRLYGMNEEGWRRAVWEKNMKMIELHNQEYSQGKHGFSMAMNAFGDMTNEEFRQVMNGFQNQKHKKGKVFHESLVLEVPKSVDWREKGYVTAVKNQGQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGLMDNAFQYVKDNGGLDTEESYPYLGRETNSCTYKPECSAANDTGFVDIPQREKALMKAVATVGPISVAIDAGHSSFQFYKSGIYYDPDCSSKDLDHGVLVVGYGFEGTDSNSSKFWIVKNSWGPEWGWNGYVKMAKDQN... | Function: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release ... |
Q10991 | VPKSVDWTKKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDSSRPQGNQGCNGGLMDNAFQYIKENGGLDSEESYPYEATDTSCNYKPEYSAAKDTGFVDIPQREKALMKAVATVGPISVAIDAGHSSFQFYKSGIYYDPDCSSKDLDHGVLVVGYGFEGTNNKFWIVKNSWGPEWGNKGYVKMAKDQNNHCGIATAASYPTV | Function: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release ... |
P80342 | AVPDKIDRRESGYV | Function: Thiol protease that assists the parasite in burrowing through the gut wall and liver of its mammalian host.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no pe... |
O60911 | MNLSLVLAAFCLGIASAVPKFDQNLDTKWYQWKATHRRLYGANEEGWRRAVWEKNMKMIELHNGEYSQGKHGFTMAMNAFGDMTNEEFRQMMGCFRNQKFRKGKVFREPLFLDLPKSVDWRKKGYVTPVKNQKQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGFMARAFQYVKENGGLDSEESYPYVAVDEICKYRPENSVANDTGFTVVAPGKEKALMKAVATVGPISVAMDAGHSSFQFYKSGIYFEPDCSSKNLDHGVLVVGYGFEGANSNNSKYWLVKNSWGPEWGSNGYVKIAKDKN... | Function: Cysteine protease. May have an important role in corneal physiology.
Catalytic Activity: The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).
Sequence Mass (Da): 37329
Sequence Length: 334
Subcellular Location: Lys... |
P80532 | DVPASIDWREYGYVTEVKD | Function: Thiol protease.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 2242
Sequence Length: 19
Subcellular Locati... |
Q94715 | MKQFLTAAIVTLLMTAGYYHLQEDDTNDFERWALKNNKFYTESEKLYRMEIYNSNKRMIEEHNQREDVTYQMGENQFMTLSHEEFVDLYLQKSDSSVNIMGASLPEVQLEGLGAVDWRNYTTVKEQGQCASGWAFSVSNSLEAWYAIRGFQKINASTQQIVDCDYNNTGCSGGYNAYAMEYVLRVGLVSSTNYPYVAKNQTCKQSRNGTYFINGYSFVGGSQSNLQYYLNNYPISVGVEASNWQFYRSGLFSNCSSNGTNHYALAVGFDSANNWIVQNSWGTQWGESGNIRLYPQNTCGILNYPYQVY | Function: May be involved in extracellular digestion.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 35189
Sequence ... |
Q24940 | MRLFILAVLTVGVLGSNDDLWHQWKRMYNKEYNGADDQHRRNIWEKNVKHIQEHNLRHDLGLVTYTLGLNQFTDMTFEEFKAKYLTEMSRASDILSHGVPYEANNRAVPDKIDWRESGYVTEVKDQGNCGSCWAFSTTGTMEGQYMKNERTSISFSEQQLVDCSGPWGNNGCSGGLMENAYQYLKQFGLETESSYPYTAVEGQCRYNKQLGVAKVTGYYTVHSGSEVELKNLVGARRPAAVAVDVESDFMMYRSGIYQSQTCSPLRVNHAVLAVGYGTQGGTDYWIVKNSWGTYWGERGYIRMARNRGNMCGIASLASLP... | Function: Thiol protease. Probably involved in interaction with host tissues. Displays a similar activity to that of papain. Has high activity on Z-Phe-Arg-NHMec, but no activity on Z-Arg-NHMec.
PTM: Contains cysteine residues involved in intramolecular disulfide bonding.
Sequence Mass (Da): 36896
Sequence Length: 326
... |
Q95029 | MNHLGVFETRFRPRTRHKSQRAQLIPEQITMRTAVLLPLLALLAVAQAVSFADVVMEEWHTFKLEHRKNYQDETEERFRLKIFNENKHKIAKHNQRFAEGKVSFKLAVNKYADLLHHEFRQLMNGFNYTLHKQLRAADESFKGVTFISPAHVTLPKSVDWRTKGAVTAVKDQGHCGSCWAFSSTGALEGQHFRKSGVLVSLSEQNLVDCSTKYGNNGCNGGLMDNAFRYIKDNGGIDTEKSYPYEAIDDSCHFNKGTVGATDRGFTDIPQGDEKKMAEAVATVGPVSVAIDASHESFQFYSEGVYNEPQCDAQNLDHGVL... | Function: Important for the overall degradation of proteins in lysosomes. Essential for adult male and female fertility. May play a role in digestion.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activ... |
P12360 | MASNTLMSCGIPAVCPSFLSSTKSKFAAAMPVYVGATNFMSRFSMSADWMPGQPRPSYLDGSAPGDFGFDSLGLGEVPANLERYKESELIHCRWAMLAVPGIIVPEALGLGNWVKAQEWAAIPGGQATYLGQPVPWGTLPTILAIEFLAIAFVEHQRSMEKDSEKKKYPGGAFDPLGYSKDPAKFEELKVKEIKNGRLALLAIVGFCVQQSAYLGTGPLENLATHLADPWHNNIGDVIIPKGIFPN | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
Q36718 | RIQAYRFRTRVPPSPAASGSPRSTRRDVAVQAKGSWLPGLQSPAYLDGSLEGDNGFDPLALAEDPEDLRWFVQADVVNGRWAMLGVAGMLIPEVLTKAGLMNAPEWLRLPGKETYFASSSTALRVHMSSTYVEIRRWQDIKNPGSVNQDPIFKSYSLPPHECGYPGRVFNPLNFAPLENKEKELANGRLAMLAFLGFLVQHNVHGKGPFENLQQHLADPWHNTIIQTISGQ | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
Q9SDM1 | MASSSGLRSCSAVGVPSLLAPSSRSGRSGLPFCAYATTSGRVTMSAEWFPGQPRPAHLDGSSPGDFGFDPLGLATVPENFERFKESEIYHCRWAMLCVPGVLVPEALGLGNWVKAQEWAALPDGQATYLGNPVPWGNLPTILAIEFLAIAFAEQQRTMEKDPEKKKYPGGAFDPLGFSKDPAKFEELKLKEIKNGRLAMLAFVGFCVQQSAYPGTGPLENLATHLADPWHNNIGDIVIPRNIYGP | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P10708 | MASACASSTIAAVAFSSPSSRRNGSIVGTTKASFLGGRRLRVSKYSTTPTARSATTVCVAADPDRPLWFPGSTPPPWLDGSLPGDFGFDPLGLASDPESLRWNQQAELVHCRWAMLGAAGIFIPELLTKIGILNTPSWYTAGEQEYFTDTTTLFIVELVLIGWAEGRRWADIIKPGCVNTDPIFPNNKLTGTDVGYPGGLWFDPLGWGSGSPAKIKELRTKEIKNGRLAMLAVMGAWFQHIYTGTGPIDNLFAHLADPGHATIFAAFSPK | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P27522 | MATQALISSSSISTSAEAARQIIGSRISQSVTRKASFVVRAASTPPVKQGANRQLWFASKQSLSYLDGRLPGDFGFDPLGLSDPEGTGGFIEPKWLAYGEVINGRFAMLGAAGAIAPEILGKAGLIPQETALAWFQTGVIPPAGTYNYWADNYTLFVLEMALMGFAEHRRFQDWAKPGSMGKQYFLGLEKGLGGSGDPAYPGGPLFNPLGFGKDEKSMKELKLKEIKNGRLAMLAILGYFIQALVTGVGPYQNLLDHLADPVNNNVLTSLKFH | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P76364 | MSDTLPGTTLPDDNHDRPWWGLPCTVTPCFGARLVQEGNRLHYLADRAGIRGLFSDADAYHLDQAFPLLMKQLELMLTSGELNPRHQHTVTLYAKGLTCKADTLSSCDYVYLAVYPTPEMKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Antitoxin component of a type IV toxin-antitoxin (TA) system . Antitoxin that counteracts the effect of its cognate toxin CbtA (YeeV) . It does not bind to the toxin but instead binds to MreB and FtsZ (the toxin targets), enhancing their polymerization by forming high... |
Q9LD90 | MAEVDISHSKKKKQDKTENDAADTGDYMIKPQSFTPAIDTSQWPILLKNYDRLNVRTGHYTPISAGHSPLKRPLQEYIRYGVINLDKPANPSSHEVVAWIKRILRVEKTGHSGTLDPKVTGNLIVCIDRATRLVKSQQGAGKEYVCVARLHSAVPDVAKVARALESLTGAVFQRPPLISAVKRQLRIRTIYESKLLEYDADRHLVVFWVSCEAGTYIRTMCVHLGLLLGVGGHMQELRRVRSGILGENNNMVTMHDVMDAQFVYDNSRDESYLRRVIMPLEMILTSYKRLVVKDSAVNAICYGAKLMIPGLLRFENDIDV... | Function: Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. P... |
G0SGK0 | MSGSAAIMKAPAKSEFIIKPENTKAEVDTSNWPGLLKNYDKMLIRTSHFTPIPDHGSAPWSRDIKSYVSSGVINLDKPSNPSSHEVVAWIKRILRVDKTGHSGTLDPKVTGCLIVCIDRATRLVKAQQGAGKEYVCCIRFHDTVPGGEPAFAKALETLTGALFQRPPLISAVKRQLRIRTIHKSRLLEFDNERHLGVFWVSCEAGTYIRTLCVHLGLLLGVGAHMQELRRVRSGVMSEDDGSLVTLHDVLDAQWQYDNNGDEALLRKVIQPLETLLCTYKRLVVKDTAVNAVCYGAKLMIPGLLRYDQGIEQGEEVVLMT... | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the co... |
O43100 | MAKEVDYTIKPEATASNINTEDWPLLLKNYDKLMVRTGHFTPIPAGSSPLKRDLKSYINSGVINLDKPSNPSSHEVVAWMKRILRAEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCVIRLHDKIPGGEAQFKRALETLTGALFQRPPLISAVKRQLRIRTIHESKLYEFDNERHLGVFWVSCEAGTYIRTLCVHLGLLLGVGAHMQELRRVRSGAMSENEGMVTLHDVLDAQWLYDNQRDESYLRKVIKPLESLLTTYKRIVVKDSAVNAVCYGAKLMIPGLLRFEAGIELGEEVVLMTTKGEAIAIGIA... | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the co... |
O14007 | MTDTHPGVDFMIKPEATSASKIDTAEWPLLLKNFDKLLVRTGHYTPIPCGNNPLKRPIAEYVSSGVINLDKPANPSSHEVVAWVKKILRVEKTGHSGTLDPKVTGCLIICNDRATRLVKSQQSAGKEYVCVLRLHDSVEGERNVASAIETLTGALFQRPPLISAVKRQLRIRSIYESKLIEFDNERNLAVFWASCEAGTYMRTLCVHLGLLLGVGGHMQELRRVRSGCLSENDDIVTMHDVLDAQWIYDNTRDESYLRRVIRPLESLLVGYKRIVVKDSAVNAICYGAKLMIPGLLRYEAGIEVNEEIVLITTKGEAIAV... | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the co... |
P33322 | MSKEDFVIKPEAAGASTDTSEWPLLLKNFDKLLVRSGHYTPIPAGSSPLKRDLKSYISSGVINLDKPSNPSSHEVVAWIKRILRCEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCIVRLHDALKDEKDLGRSLENLTGALFQRPPLISAVKRQLRVRTIYESNLIEFDNKRNLGVFWASCEAGTYMRTLCVHLGMLLGVGGHMQELRRVRSGALSENDNMVTLHDVMDAQWVYDNTRDESYLRSIIQPLETLLVGYKRIVVKDSAVNAVCYGAKLMIPGLLRYEEGIELYDEIVLITTKGEAIAVAIAQM... | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA . This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 . Pseudouridine ('psi') residues may serve to stabilize the ... |
Q05590 | MLSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCREIERCQAAIELAQAGHNVALISSGDAGIYGMAGLVLELVSKQKLDVEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWPVIEKRIVAAGEADFVICFYNPRSRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDFEPVDMTSLVIVGNKTTYVQDGLMITPRGYTL | Function: Methyltransferase that likely catalyzes the ring contraction and methylation of C-17 in cobalt-factor III to form cobalt-factor IV. May also convert cobalt-precorrin-3 to cobalt-precorrin-4.
Catalytic Activity: Co(II)-factor III + H(+) + S-adenosyl-L-methionine = Co(II)-factor IV + S-adenosyl-L-homocysteine
S... |
Q977V1 | MNIWIRGGTSDANNISKEIKRNFKDSFLILTTTTDFGGKIAENFADLVISEKMTYDNLKKTLLDKKIDVFIDATHPFATHASETGIKISKELNIPYIRYERPSEKFKNAFYVENYEEAAKLALKISKKNIFYMSGIKNLKNVSEIIPIEKLIVRILPTSVPEALKILPSKNIVAMQGVFSENLNKELIIDYNCDVIITKDSGKSGGLYEKVSGATLAGAKPIIIKRPEINYPLKFEKIVEIVNYLKNV | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 27999
Sequence Length: 248
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from s... |
O27083 | MQTPEIKEGTEQYLWRRKTMNPGDKGVKRKGSDRQREKMSVIVMAGTEDARRIISRLSGMPWVEVTATATTEHGSDLAEKSGASRTVTGALDSDGLRELMADLDACILIDATHPFAAQATENALRACRETGTIYVRFERPEVIPDGVIRVGSFREAGEVASSLIGDGEVVMHLAGVSTLGDVLRSLEPERVAVRVLPSTSSIEKCLQLGVPPSHIIAMQGRFSAEMNLALLREYRAGAVITKESGETGGLPEKVEAASELGIPVILVERPEVNLEGEAVFGNINDLMDHVLKILRDMGQPGD | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 32673
Sequence Length: 302
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from s... |
O87691 | MILLLAGTSDARALAVQVKKAGYDVTATVVTDNAAIELQRAEVKVKIGRLTKEDMTDFINEHGVKAIVDASHPFAEEASKNAIGAAAETAIPYIRYERASQAFTYDNMTMVSTYEEAAEVAAEKKGVIMLTTGSKTLQVFTEKLLPLSDVRLVARMLPRLDNMEKCQQLGLPQKNIIAIQGPFTKEFDRALYKQYGVTVMVTKESGKVGSVDKKVEAAKELGLDIIMIGRPKIEYGTVYSTFEEVVHALVNQTRS | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 27994
Sequence Length: 255
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from s... |
Q05591 | MNEGDVLVVGGTSDARALCRQLDAANVAYTLSVATPAGKALAGDIKGQVRCGRLEYGQMVAWLKENRTRWVIDASHPYAEMVSHNLLRACETAGVLLSRYQRPEQLSNLTHPLLYTARSIADACEIARRFGPRVLLTTGSKDLAVWRAGLAEKTLLARVLPVAEVIQRCSELGFGVGEIFALCGPFSADFNAAFYHQCRADVVITKASGAEGGYQEKVQPCLDAGIPCIVIARPTPLVTGDELLESQAAFAQRLSRWLAAAKE | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 28403
Sequence Length: 263
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from s... |
P72711 | MVDSLATVWLIGGTVDSRAVAEGLIAQGINCLVTVTTSEAKHLYPIHQCLTVHVGALTPQEIPKFLKRHSIAVIVDASHPFAAQITTTVTAIAKEQQIPYIRFERPPLALGKNTLEVPDIQSLTRGKYQPYLRGKRVLLTVGARWLSHFSLLQDEAVLFARILPYPQALAQAIAAGFTSDRIIALRPPVAEPLEKALWQQWQIQGVVTKASGAQGGELVKQKVAEALGVNLIRIARPQTIPGQITDDLSQINQFCQRHLPS | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 28565
Sequence Length: 261
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from s... |
Q72CB8 | MVPPRWGSLDSLKPQQHLPMTKKGILLAAFGSGNRQGESTLRLFDERVRERFPGVPVRWAFTSVIMRRRLAAARKKTDSVLKALQKMWFEKYTHVAVQSLHIIPGAEYGDLVADVEAMRRDDGFTAATVGAPLLAGSGDMERSAAALLAHLPAGRKPDEAVVFMGHGTRHPAESSYEALAALVRRVDPHVHIGTMGGSRTLDHILPELQQGGVKGVWLMPLLSVVGRHATEDMAGTDPESWKSRLEASGLRCIPVLRGTAEYEGFVDIWLDHLTAAVSALDD | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 30825... |
Q72EC8 | MSRHPMVTRLLCLVFSCLIILACSPAFAGHGAPKAQKTGILLVAFGTSVEEARPALDKMGDRVRAAHPDIPVRWAYTAKMIRAKLRAEGIAAPSPAEALAGMAEEGFTHVAVQSLHTIPGEEFHGLLETAHAFQGLPKGLTRVSVGLPLIGTTADAEAVAEALVASLPADRKPGEPVVFMGHGTPHPADICYPGLQYYLWRLDPDLLVGTVEGSPSFDNVMAELDVRKAKRVWLMPLMAVAGDHARNDMAGDEDDSWTSQLARRGIEAKPVLHGTAESDAVAAIWLRHLDDALARLN | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme. Its periplasmic location means that it cannot participate in cobalamin biosynthesis and its genomic environment suggests it is likely to be associated with a hem... |
Q05592 | MKKALLVVSFGTSYHDTCEKNIVACERDLAASCPDRDLFRAFTSGMIIRKLRQRDGIDIDTPLQALQKLAAQGYQDVAIQSLHIINGDEYEKIVREVQLLRPLFTRLTLGVPLLSSHNDYVQLMQALRQQMPSLRQTEKVVFMGHGASHHAFAAYACLDHMMTAQRFPARVGAVESYPEVDILIDSLRDEGVTGVHLMPLMLVAGDHAINDMASDDGDSWKMRFNAAGIPATPWLSGLGENPAIRAMFVAHLHQALNMAVEEAA | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 29239
Sequence Length: 264
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q58181 | MNKLVKKVYGVGVGVGDKKLLTLKALEVLKKVDKIFVPVSKKGKKSIAYEIIKDYVDGKNIEELLFPMIKDKERLKKYWENALEKVLKEDGEVAIITIGDPTLYSTFSYVWKLLKERGVEVEIVNGISSIFASAAALNIPLVEGDEKLCILPQGKDLEKYIDEFDTIIIMKTKNLNEKLSVIKNRDDYIIGLVKRATFEDEKVVIGKLDEINFDEFNDYLSLAIIKRFKR | Function: Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.
Catalytic Activity: Co-precorrin-2 + S-adenosyl-L-methionine = Co-precorrin-3 + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26267
Sequence Length: 230
Pathway: Cofactor b... |
Q05593 | MNGKLYALSTGPGAPDLITVRAARILGSLDILYAPAGRKGGDSLALSIVRDYLGEQTEVRCCHFPMSADGAEKEAVWNEVAAALTAEVEAGKQVGFITLGDAMLFSTWIFLLQRIGCPEWLEIVPGVTSFAAIAARAKMPLAIERQSLAVISCTAPEAEIAQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMSEATLPGEQCWRHLHEVNDDRPLPYFSTILVNKQWEYAE | Function: Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.
Catalytic Activity: Co-precorrin-2 + S-adenosyl-L-methionine = Co-precorrin-3 + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25806
Sequence Length: 237
Pathway: Cofactor b... |
A2SQF0 | MHFMDGFLPIGWCVFWAVLAAPFLIYGMWKITKMINNDRHVLPLMAVCGAFIFVVSLVDIPSPTGSCSHPTGTGLSASFFGPAVTSVLGLIILVFQALLLGHGGFTTLGATAFSMAVMGPLAAWLVFKGLRKTGRVPLGPAVFCAAVVANCVTYLITSLQIALAYPVEGSVLTAFLAAAAVFAVVQIPISIIEGIISGLVATYIARIKPEILQKLGVISGEEVKKVLSEQA | Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24296
Sequence Length: 231
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
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Q46AL8 | MHIMEGYLPAIWCIVWFVVSIPVVAYGVYKLNKLVKEERGILPVLAVAGAFIFVLSSLKMPSVTGSCSHPTGTGIGAIIFGPAITAVLSTIVLIYQALFLAHGGLTTLGANVFSMGIVGPIVAYLIYKTGMKAKLNFYLIVFLAATLGDWATYIVTSTELALAFPAGDILTFGGFFSSFSKFVAIFAITQVPLAIVEGAVSALLFKYIIQAKSDLLVEMKVIGEPLVRKLRGLPA | Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25069
Sequence Length: 235
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
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A1ANE2 | MHIMEGFLPVEHAIGWSVASAPVVAYGLYSINKKIKKNPEQRMLLGVAAAFTFVLSALKMPSVTGSCSHPTGTGLGAILFGPSAVAPIGAVVLLFQALLLAHGGLTTLGANIFSMAIVGPFAAAAVFRLARAARFPFGVGVFLAASLGDLLTYVTTACQLAFAFPDPVGGFTASLAKFAGVFALTQIPLAISEGLLTVVVMNALLRFNREELGSLNIEGNGQEVQA | Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23364
Sequence Length: 226
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell inner membrane
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Q8U3L0 | MEEVFQNETIKQILAKYRRIWAIGHAQSVLGWDLEVNMPKEGILERSVAQGELSVLSHELLLHPEFVNLVEKAKGLENLNEYERGIVRVLDRSIRIARAFPPEFIREVSETTSLATKAWEEAKAKDDFSKFEPWLDKIISLAKRAAEYLGYEEEPYDALLDLYEEGLRTRDVEKMFEVLEKKLKPLLDKILEEGKVPREHPLEKEKYEREWMERVNLWILQKFGFPLGTRARLDVSAHPFTTEFGIRDVRITTRYEGYDFRRTILSTVHEFGHALYELQQDERFMFTPIAGGVSLGIHESQSRFWENIIGRSKEFVELIY... | Cofactor: Binds 1 cobalt ion per subunit. Can also utilize Mn(2+) (in vitro). Is not active with zinc ions.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.
Catalytic Activity: Re... |
P86516 | AFDLNDFNTLEDTYDQMNVFQLSEAGLTHEGRDMKSWIDSLTHCRSHLDEDVFMFKRNEPDSGSACVGTDLNRSSNNPCSDTYGGSGPASALETRHSYSQQYEDELNQRQRYEPSGTTVNNLLNKDAGSIYSYTPELR | Cofactor: Binds 1 zinc ion per subunit.
Function: Carboxypeptidase that catalyzes the release of hydrophobic and acidic C-terminal amino acids.
Sequence Mass (Da): 15590
Sequence Length: 138
Subcellular Location: Secreted
EC: 3.4.17.-
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P42663 | MTPEAAYQNLLEFQRETAYLGSLGALAAWDQRTMIPRKGHGHRARQMAALARLLHERATDPRIGEWLEKVEGSSLVEDPLSDAAVNVRAWRRAYERARAIPERLAVELAQARSEGETAWEALRPRDDWQGFLPYLKRLFALAKEEAEILMAVGPDPLDPPYGELYDALLDGYEPGARARDLEPLFRELSSGLKGLLDRILGSGRRPDVGVLHRHYPKEAQRAFALELLQACGYDLEAGRLDPTAHPFEIAIGPGDVRITTRYYEDFFNAGIFGTLHEMGHALYEQGLPEAHWGTPRGEAASLGVHESQSRTWENLVGRSL... | Cofactor: Binds 1 zinc ion per subunit. Can also utilize cobalt ions, but contains bound zinc when purified after heterologous expression in E.coli.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro.... |
P55747 | GSDLLTPGDNKTAHDSYAFLVNWLERFPQYKYRDFYIAGESYAGHYVPQLSQLVHRNNKGVRKPILNFKGFMVGNAVIDDYHDFVGTFEYWWTHGLISDDTYQKLQLACEFDSAEHESEACNKINNVAEAEEGLIDAYSIYTPTCKKTSLHRRRLIKGRRPWLPRGYDPCTEQYSTKYYNLPEVQKAFRANVTGIPYSWTACSDVLSDHWKDSPRSMLPIYRELIAAGIRIWVFSGDADSVVPLTATRYSIDALYLPTVTNWYPWYDEEEVAGWCQVYKGLTLVTIRGAGHEVPLHRPQQALKLFEHFLQDKPMPRPAHS... | PTM: The linker peptide is endoproteolytically excised during enzyme maturation.
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Mass (Da): 37408
Sequence Length: 324
EC: 3.4.16.6
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P55748 | VPRVPGQAFDASFAHYAGYVTVSEDRGAALFYWFFEAAHDPASKPLLLWLNGGPGCSSIAFGVGEEVGPFHVNADGKGVHMNPYSWNQVANILFLDSPVGVGYSYSNTSADILSNGDERTAKDSLVFLTKWLERFPQYKEREFYLTGESYAGHYVPQLAQAIKRHHEATGDKSINLKGYMVGNALTDDFHDHYGIFQYMWTTGLISDQTYKLLNIFCDFESFVHTSPQCDKILDIASTEAGNIDSYSIFTPTCHSSFASSRNKVVKRLRSVGKMGEQYDPCTEKHSIVYFNLHEVQKALHVNPVIGKSKWETCSEVINTN... | PTM: The linker peptide is endoproteolytically excised during enzyme maturation.
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Mass (Da): 48952
Sequence Length: 436
EC: 3.4.16.6
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P52711 | MKCTVVALVLLVAVQCLVLGAGPAAAAKARRTRQGDYLNRLRGSPSSRASWESLAAVEEQTTTKAAGRPAPVAAAVEAGRKEADRVEALPGHPRGVDFAQYAGYVTVDAAAGRALFYYLAEAVGGNGDKTKPLLLWLNGGPGCSSLGYGAMEELGPFRVMSDGKTLYSNPYSWNHAANVLFLESPAGVGYSYSNTTADYGRSGDNGTAEDAYQFLDNWLERFPEYKGREFYITGESYAGHYVPQLAHAILRHASPDINLKGIMIGNAVINDWTDSKGMYDFFWTHALISDETADGISKNCNFTAYGAGVASNALCDAASD... | PTM: The linker peptide is endoproteolytically excised during enzyme maturation.
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Mass (Da): 55914
Sequence Length: 516
EC: 3.4.16.6
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P08818 | MRTTTRRLPPAPAAAAVLLAALTCLLLRPAAVAAAGGHAADRIVRLPGQPEVDFDMYSGYITVDEAAGRSLFYLLQEAPEEAQPAPLVLWLNGGPGCSSVAYGASEELGAFRVMPRGAGLVLNEYRWNKVANVLFLDSPAGVGFSYTNTSSDIYTSGDNRTAHDSYAFLAAWFERFPHYKYREFYVAGESYAGHYVPELSQLVHRSGNPVINLKGFMVGNGLIDDYHDYVGTFEFWWNHGIVSDDTYRRLKDACLHDSFIHPSPACDAATDVATAEQGNIDMYSLYTPVCNISSSSSSSSLSRRRTRGRYPWLTGSYDPC... | Function: May be involved in the degradation of small peptides (2-5 residues) or in the degradation of storage proteins in the embryo.
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Mass (Da): 52625
Sequence Length: 476
Subcellular Location: Secreted
EC: 3.4.16.6
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P21529 | MVTTPRLVSLLLLLALCAAAAGALRLPPDASFPGAQAERLIRALNLLPKDSSSSSGRHGARVGEGNEDVAPGQLLERRVTLPGLPEGVADLGHHAGYYRLPNTHDARMFYFFFESRGKKEDPVVIWLTGGPGCSSELAVFYENGPFTIANNMSLVWNKFGWDKISNIIFVDQPTGTGFSYSSDDRDTRHDETGVSNDLYDFLQVFFKKHPEFIKNDFFITGESYAGHYIPAFASRVHQGNKKNEGTHINLKGFAIGNGLTDPAIQYKAYTDYALEMNLIQKADYERINKFIPPCEFAIKLCGTNGKASCMAAYMVCNTIF... | Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 56362
Sequence Length: 508
Subcellular Location: Secreted
EC: 3.4.16.5
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Q96VC4 | MRVLPATLLVGAATAATPAQQVLGGLQDFGNAVQDAMHENLPKINKPLEAFQEQLKSLYEAREFWEEVANAFPQNLDHNPVFSLPKKHTRRPDSHWDHIVRGADVQSVWVTGENGEKEREIEGKLEAYDLRIKKTDPSSLGIDPDVKQYTGYLDDNENDKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLTGLFMELGPSSIDENIKPVYNPYAWNSNASVIFLDQPVNVGYSYSGSTVSDTVAAGKDVYALLTLFFKQFPEYAEQDFHIAGESYAGHYIPVFTSEILSHQKRNINLKSVLIGNGLTDGLTQYEYYRPM... | Function: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity).
Catalytic Activity: Release of a C-terminal am... |
D4ANB6 | MELYLNMLSFWYILLATSFFGPSQAVYQAPLSVDESQKVTIEEGFQIFTSKHSPQHSIRIKKQDGSICDAHSAQYTGWLDIGPKHLFFWYFESQNDPENDPLTLWMTGGPGYSSMLGMLEEVGPCLVNEYGNGTKYNPWGWSKKSSMLFVDQPVGVGFSYGDEGHDIPNDSYLAAVDMHRFLQLFISEVFPNKLNSPFHISGESYGGHYIPYLGAQIVRQNKLYPNEPQVQLKSCLIGNGCMSHMHTTFGYWETLCTTNPGVEKPIFNETRCDIMAKNMPRCMKVAEVCRRNPDPAICLSAQSVCDEGITGLYNKESDVK... | Function: Involved in degradation of small peptides.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 57171
Sequence Length: 508
Subcellular Location: Secreted
EC: 3.4.16.5
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P52710 | MILHTYIILSLLTIFPKAIGLSLQMPMALEASYASLVEKATLAVGQEIDAIQKGIQQGWLEVETRFPTIVSQLSYSTGPKFAIKKKDATFWDFYVESQELPNYRLRVKRNNPEVLKVDFTKQYSGYLDVEADDKHFFYWFFESRNDPQNDPIILWLNGGPGCSSLTGLFFELGSSRINENLKPIFNPYSWNGNASIIYLDQPVNVGFSYSSSSVSNTVVAGEDVYAFLQLFFQHFPEYQTNDFHIAGESYAGHYIPVFADEILSQKNRNFNLTSVLIGNGLTDPLTQYRYYEPMACGEGGAPSVLPADECENMLVTQDKC... | Function: Involved in degradation of small peptides.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 59448
Sequence Length: 523
Subcellular Location: Vacuole
EC: 3.4.16.5
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O13849 | MLMKQTFLYFLLTCVVSAQFNGYVPPEQNGGDIVVPKDFYEKFGEDFIREQEESSAPLMNPVPERDEAEAPHHPKGHHEFNDDFEDDTALEHPGFKDKLDSFLQPARDFLHTVSDRLDNIFDDDEDEHVREKRPHDSADEDAPRRKHGKCKGKGKHHKGKHAKGKGKKSHPKPEDDSVFFDDERPKHHEFDDEDREFPAHHEPGEHMPPPPMHHKPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEP... | Function: Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence ... |
P00729 | MKAFTSLLCGLGLSTTLAKAISLQRPLGLDKDVLLQAAEKFGLDLDLDHLLKELDSNVLDAWAQIEHLYPNQVMSLETSTKPKFPEAIKTKKDWDFVVKNDAIENYQLRVNKIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSA... | Function: Vacuolar serine-type carboxypeptidase involved in degradation of small peptides . Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate . Also plays a role in breakdown of the autophagic... |
Q66K79 | MPPPLPLLLLTVLVVAAARPGCEFERNPAGECHRPPAADSATCVDLQLRTCSDAAYNHTTFPNLLQHRSWEVVEASSEYILLSVLHQLLEGQCNPDLRLLGCAVLAPRCEGGWVRRPCRHICEGLREVCQPAFDAIDMAWPYFLDCHRYFTREDEGCYDPLEKLRGGLEADEALPSGLPPTFIRFSHHSYAQMVRVLRRTASRCAHVARTYSIGRSFDGRELLVIEFSSRPGQHELMEPEVKLIGNIHGNEVAGREMLIYLAQYLCSEYLLGNPRIQRLLNTTRIHLLPSMNPDGYEVAAAEGAGYNGWTSGRQNAQNLD... | Function: Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing.
Sequence Mass (Da): 73655
Sequence Length: 652
Subcellular Location: Secreted
EC: 3.4.17.-
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P42788 | QYHTLPEIYSWLDRLVQEHPEHVEPVVGGKSYEGREIRGVKVSYKKGNPVVMVESNIHAREWITAATTTYLLNELLTSKNSTIREMAENYDWYIFPVTNPDGYVYTHTTDRMWRKTRSPNPDSLCAGTDPNRNWNFHWMEQGTSSRPCTETYGGKKAFSEVETRSFSDFLKTLKGQIKVYLAFHSYSQLLLFPYGHTCQHTYNHDDLQAIGDAAARSLAQRYGTDYTVGNIYDAIYPASGGSMDWAYDTLDIPIAYTYELRPRDGWNGFQLPANQIIPTGEETVDSVVTILKESRRLGYFNTSD | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the digestion of the blood meal.
Sequence Mass (Da): 34849
Sequence Length: 304
Subcellular Location: Secreted
EC: 3.4.17.-
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Q5F362 | MAVNYSAKEEADGHPAGGGPGGGATAGGGGAVKTRKPDNTAFKQQRLPAWQPILTAGTVLPAFFIIGLIFIPIGIGIFVTSNNIREYEIDYTGVEPSSPCNKCLNVSWDSTPPCTCTINFTLEHSFESNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDNSSLLNPSKECEPYRTNEDKPIAPCGAIANSMFNDTLELYHIENDTRTAITLIKKGIAWWTDKNVKFRNPKGDGNLTALFQGTTKPVNWPKPVYMLDSEPDNNGFINEDFIVWMRTAALPTFRKLYRLIERKSNLQPTLQAGKYSLNITYNYPVHSFDGRKR... | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be... |
Q9NV96 | MAMNYNAKDEVDGGPPCAPGGTAKTRRPDNTAFKQQRLPAWQPILTAGTVLPIFFIIGLIFIPIGIGIFVTSNNIREIEIDYTGTEPSSPCNKCLSPDVTPCFCTINFTLEKSFEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDSSALLNPSKECEPYRRNEDKPIAPCGAIANSMFNDTLELFLIGNDSYPIPIALKKKGIAWWTDKNVKFRNPPGGDNLEERFKGTTKPVNWLKPVYMLDSDPDNNGFINEDFIVWMRTAALPTFRKLYRLIERKSDLHPTLPAGRYSLNVTYNYPVHYFDGRKRMILSTISWMGG... | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be... |
Q8VEK0 | MAMNYSAKDEVDGGPAGPPGGAAKTRRPDNTAFKQQRLPAWQPILTAGTVLPTFFIIGLIFIPIGIGIFVTSNNIREIEIDYTGTEPSSPCNKCLSPNVTSCACTINFTLKQSFEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDPSALLNPSKECEPYRRNEDRPIAPCGAIANSMFNDTLELYLVANESDPKPIPIPLKKKGIAWWTDKNVKFRNPPGKESLEEKFKDTIKPVNWHKAVYELDPEDESNNGFINEDFIVWMRTAALPTFRKLYRLIERRDDLHPTLPAGQYFLNITYNYPVHSFDGRKRMILSTISW... | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be... |
Q6AY41 | MAMNYSAKDEVDGGPTGPPGGAAKTRRPDNTAFKQQRLPAWQPILTAGTVLPTFFIIGLIFIPIGIGIFVTSNNIREIEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDPSALLNPSKECEPYRRNEDKPIAPCGAIANSMFNDTLELFLVANESDPKPVPILLKKKGIAWWTDKNVKFRNPPGKDSLQEKFKDTTKPVNWHKPVYELDPDDESNNGFINEDFIVWMRTAALPTFRKLYRLIERTDDLHPTLPAGQYYLNITYNYPVHFFDGRKRMILSTISWMGGKNPFLGIAYITIGSISFLLGVVLLVINHKYRNS... | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be... |
Q3MIR4 | MTWSATARGAHQPDNTAFTQQRLPAWQPLLSASIALPLFFCAGLAFIGLGLGLYYSSNGIKELEYDYTGDPGTGNCSVCAAAGQGRALPPPCSCAWYFSLPELFQGPVYLYYELTNFYQNNRRYGVSRDDAQLSGLPSALRHPVNECAPYQRSAAGLPIAPCGAIANSLFNDSFSLWHQRQPGGPYVEVPLDRSGIAWWTDYHVKFRNPPLVNGSLALAFQGTAPPPNWRRPVYELSPDPNNTGFINQDFVVWMRTAALPTFRKLYARIRQGNYSAGLPRGAYRVNITYNYPVRAFGGHKLLIFSSISWMGGKNPFLGIA... | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be... |
A7GN74 | MKRFKRAGAIIETLKEHGHEAYFVGGSVRDFIIDRPIGDIDIATSALPEEVMKLFPKHVPVGLEHGTVIVLQDGEPYEVTTFRTESDYEDFRRPSSVQFVRSLEEDLKRRDFTMNAIAMNEDGEIIDLFGGQEAIQKREIVTVGNAAERFQEDALRMMRGIRFVSTLGFSLEEKTECAIKRYGHLLEHIAIERITVEFEKLLTGPYCVKGLQKLVETKLFMHLPYLQMSEEKILKAAEYNWESFETEIEAWAFFLSCIGEEHPSVFLRQWKFSNKKIKEIVAVLLAIRTRKTKEWDAVFLYQTGVQIALMAERVYQVMIE... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
A9VME7 | MERFKKASSIIEMLKQHGHEAYFVGGSVRDLIIDRPIGDIDIATSALPEEVMAIFPRHVPVGLEHGTVIVVENGEPYEVTTFRTESEYEDFRRPSSVQFVRSLEEDLKRRDFTMNAIAMTEEGEMVDLFAGKEAIRLKEITTVGDAADRFQEDALRMMRGIRFVSTLGFSLEIKTKQAIETYGHLLEHIAIERITVEFEKLLTGTYCVNGLQELVETKLFSHLPYLQMSEERLLKATQYKWDSFETDVEAWAFFLYCIGEEHPSVFLRQWKFSNKKIKDIVAVLLAIRSRKEKEWDTILLYKTGIRIAEMAERVYEAIIE... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
P42977 | MEKVFIKALPVLRILIEAGHQAYFVGGAVRDSYMKRTIGDVDIATDAAPDQVERLFQRTVDVGKEHGTIIVLWEDETYEVTTFRTESDYVDFRRPSEVQFISSLEEDLKRRDLTINAMAMTADGKVLDYFGGKKDIDQKVIRTVGKPEDRFQEDALRMLRAVRFMSQLGFTLSPETEEAIAKEKSLLSHVSVERKTIEFEKLLQGRASRQALQTLIQTRLYEELPGFYHKRENLISTSEFPFFSLTSREELWAALLINLGIVLKDAPLFLKAWKLPGKVIKEAIHIADTFGQSLDAMTMYRAGKKALLSAAKISQLRQNE... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Has no poly(A) polymerase activ... |
Q493X4 | MEKYLVGGAVRDALLKLPVQEKDWVVVGSSPQEMLNIGYEQVGKDFPVFLHPESHEEYALARTERKSGQGYTGFICHTAPSITIEEDLYRRDLTINAMAYDSHGNLIDPYHGQRDIKLRLLRHVSHTFHEDPLRVLRVARFAARFAHMNFAIAPETLILMKQMIHELLSLSPERIWTETKKALITDNPQVYFTVLRHCGALKILFPELDALFDIPTPTQYCTKINTGYYTMTTLSKAAYLTDDISVRFSVLCRDLGKGIPLNKINKNTKHHDHRKLGITLIHNLCNRFKIPHEIRNFSKITSEYHDYLYNVKILKPEMLM... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
Q7U358 | MSRTDDPGVAGLRVYIVGGAVRDDLLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGADVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFGDFSIAPETMQLCRRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELHDDTAVRAEIDRAAAAGLPLAGRYALLCRHTPERDALGRRLRAPVECMDQARLLPLAVDALAASATPAAQLDLIERCDALRKPERFDALLQAAAIVAPVDL... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
Q9HI95 | MIDYQEVLSRYRPTQEEENKLKIISDDIIRKINSICRSRGLRAEAVIVGSYAKGTNLRDGDLDIFIAFDRDYPEEIINTEGLHIGHAVIPNGREKYAEHPYVSGEIGGVKIDVVPCYKMSFGDKKISAVDRTLLHTEYVNGHLDEKGRDEVRLLKIFTKSIGVYGAEARTFGFSGYLCELLVIRFGSFENVIRYFSKAKGRVLIDLDERFRDPMVLIDPVDPDRNVASPVSLESLSRMKIASKMFLSSPDEGFFQIEHNGKNVQYHDRGTCIMIYSLPKPDLTDDVIYPQVYRFRSVLQKIMESHEIRVISSEIDVSDRI... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
Q9V302 | MIDYQEVLSRYRPTQEEENRLRIISDDIIRKINSICRSRRLRAEAVIVGSYAKGTNLRDGDLDIFIAFDRDYPEEIINTEGLHIGHAVIPNGREKYAEHPYVSGEIGGVKIDVVPCYKMSFGDRKISAVDRTLLHTEYVNGHLDEKGRDEVRLLKIFTKSIGVYGAEARTFGFSGYLCELLVIRFRSFENVIRYFSKAKGRVLIDPDERFRDPMLLIDPVDP | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
A1WHX2 | MQIYMVGGAVRDRLLGRPVHDRDWVVVGATPEQMRAQGYLPVGRDFPVFLHPATREEYALARTERKSGRGYRGFVVHSAPEVTLQEDLSRRDLTINAIATSADASGAGCLIDPHHGARDIAARVLRHVSTAFREDPVRILRVARFAARLPDFTVAPETLQLMREMVAHGETDHLVAERVWQELARGLMAEKPSRMFEVLRACGALERLLPEVERLWGVPQSAEHHPEIDTGAHLLLVLDMAARLQAPLAVRFACLAHDLGKGSTPADMLPRHIGHETRGAELLKHLAERLRVPADCRATADKVAREHGHIHCSNALSAAA... | Cofactor: Magnesium is required for nucleotidyltransferase activity.
Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates a... |
Q9KPC6 | MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLAAGFQAVGKDFPVFLHPNSKEEHALARTERKTSVGYTGFACHYAPDVTLEEDLLRRDLTINAMAQDNSGQLIDPYGGQRDLAAKVLRHVSPAFVEDPLRVLRVARFAAKLHHLGFTVAEETMQLMAKIAQSGELQHLTAERVWQEWHKSLSAHHPEMFLQVLRDCGALAVVLPEIDRLFGVPQPEKWHPEIDTGIHTLMVAKQAAQLSDSLLVRFAAQVHDLGKGVTPPSEWPRHKLHCHTGLNIIESLCERIRVPNEFRDLALAVCAQHSNIHRADELKPTTKL... | Cofactor: Magnesium is required for nucleotidyltransferase activity.
Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates a... |
Q6Z0E2 | MENGEIEGAADDGVPVPAPPNGRRYRPVGSSDRAVIQMTSMEPGSSSSTAVAAVSGITPQPPRNLTVDPSMQEDHTVSQGDSKLELFGFDSLVNILGLKSMTGEQIQAPSSPRDGEDVAITIGRPKETGPKFGTMMGVFVPCLQNILGIIYYIRFTWIVGMAGVWQSLVLVSFCGACTFLTGISLSAIATNGAMKGGGPYYLIGRALGPEVGVSIGLCFFLGNAVAGSMYVLGAVETFLDAVPSAGFFKESVTVVNNTLVNGTATASTATISTPSLHDLQVYGVIVTILLCFIVFGGVKIINKVAPAFLIPVLFSLLCIY... | Function: Probable cation/chloride cotransporter that may mediate potassium-chloride cotransport. Involved in plant development and K(+) and Cl(-) homeostasis. May not be involved in sodium-chloride cotransport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 108454
Sequence Length: 989
Subcellular L... |
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