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Database: UniProt
Entry: S4R5Y9_PETMA
LinkDB: S4R5Y9_PETMA
Original site: S4R5Y9_PETMA 
ID   S4R5Y9_PETMA            Unreviewed;       412 AA.
AC   S4R5Y9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000000619.1};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000000619.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
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DR   AlphaFoldDB; S4R5Y9; -.
DR   STRING; 7757.ENSPMAP00000000619; -.
DR   Ensembl; ENSPMAT00000000620.1; ENSPMAP00000000619.1; ENSPMAG00000000560.1.
DR   GeneTree; ENSGT00390000002854; -.
DR   HOGENOM; CLU_668273_0_0_1; -.
DR   Proteomes; UP000245300; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR039087; VCPIP1.
DR   PANTHER; PTHR14843; DEUBIQUITINATING PROTEIN VCIP135; 1.
DR   PANTHER; PTHR14843:SF2; DEUBIQUITINATING PROTEIN VCPIP1; 1.
DR   Pfam; PF02338; OTU; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   DOMAIN          11..165
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
SQ   SEQUENCE   412 AA;  45546 MW;  E64BACB037295B1B CRC64;
     VQQANSGDSR LVPLHVDGDG HCLVHAISRA LVGRELFWHA LRTALRAHLA EERDTYRALL
     ADFLVDDEWD EIVRESEPDY RPLRGTLHGL RNVHLLGLSS VLRRPIILLD SDGGMASSGD
     YAGTFLPGLV PSEQRRRPSD GKLHRPLCVA WANLEHIHFV PLVGVRGLVP PVLPKEMLPT
     VWGFTDKALE DYIDFSEGDC CVIGGDRMLT DSYVERLISS MQEMFTEVHG IPPSFVVDCQ
     ESLNMGSWKT DGEMIATLKV YLSKGQLYRC IDCTGVFVVG NETTDGDRAA GVQDEEQQPC
     AVGAGAPSGA RAPSPCRSCC SERVRMIRED GSTQYENTDR TSTPSGTCKC GFKHYWDGQE
     YDGLPQLLGV SFSLHGKRIE DTVVVFKDQS DPGLNTNAQK MAQYLQLKHF PG
//
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