IED ID | IndEnz0002012504 |
Enzyme Type ID | protease012504 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase 7 EC 3.4.19.12 Deubiquitinating enzyme 7 Ubiquitin thioesterase 7 Ubiquitin-specific-processing protease 7 |
Gene Name | math-33 CBG23105 |
Organism | Caenorhabditis briggsae |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis briggsae |
Enzyme Sequence | MCSPDPEDMHILTNDIPSFDKSLDPYGPEGHLALDIERFSSFMNKPDSRIMSKPVIVRGIPWRILAICRHQQNNRQVATSRSRNNYNFGFFLQCNNDDLLQKRGMWRCYGQATLEVLNANGPPIQKKIHHSFHNTEVDWGFSNYDQYDTLTSPKDGYVIDDVIRLRCRFTADVPTGANYMWDSKKHTGCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNMEVGTEPNESNIVLAMQRVFYELQMSSEAVETNSLTRAFGWDKLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAFDAYTTPETLDDDNKYDAGDHGLQRAEKGVKFVELPPVLHVQLMRFQYCGVEQKINERFSFPEKMNLSNCCELGPMLNEEDCVYSLHAVLVHSGEFHGGHYVTYINVNLHESAVDPTATAKWCKFDDDVVSRTTTDDAIVSNFGGEKAMNSSAYMLVYVRDNAIDQVLAPIPDTQIPQSVSRTFEMERMHRNREKKKQEEEQMCMSITLVTPDILATNHSFDLIEPVTITDVLPHETVYKHMVTAELYQFVQEKLFEKSTLPKVDMFDSDDETRMKRKEILRRLKTKKFGFRLWRMTDSYTVDKPQKMASRLRPSDFIEYSIDTRLDHTLSHDTETIYVEHSQFLQPLNEYLPTRDILFFLKYYDAITDKFTIIGHVTLDSHKRLNLYRMTFCDLLGLPKDTELKYYIEHAPNHVEQIDDPNRSTISRLVDDQDGAIVIVEKADPTAKKDAKTKMIELYNDVEFEFSQQFYSKMPNEEPFELFTKRFCLEQKLTDVTEFIGSELNVDPRNVMLWTRVSGSRFEPNFDDYAVTGIQCKYLTLRTLHDPRQHKKYSVSYAIFPFPVNEVHTTRMFVRLYRQMPNGNVEELNLFPPKDGTVTDLIAEAKRYYPSVEGGSGKFRLLQIGTSPLNNQRVFQIYNENTAIVDLDQRPVYKQQAQHTLNCRIEEIPHDELDVAQGEFFCPVVHYDREPTKLFGVSFVIKIRNGELMTDVRDRLRRKLPDVSDAEFAKYKFALLSRDKLCRNIEFNAGEKVNLMDMANQTTGVPQVYIGLDHKSPSQHSNEAAIRILN |
Enzyme Length | 1129 |
Uniprot Accession Number | Q60MK8 |
Absorption | |
Active Site | ACT_SITE 199; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 439; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q93009}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Hydrolase that deubiquitinates target proteins. {ECO:0000250|UniProtKB:Q93009}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (2) |
Keywords | Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93009}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 130,838 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |