ID A0A668A513_9TELE Unreviewed; 960 AA.
AC A0A668A513;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=OTUD7A {ECO:0000313|Ensembl:ENSMMDP00005040201.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005040201.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005040201.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family.
CC {ECO:0000256|ARBA:ARBA00005865}.
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DR AlphaFoldDB; A0A668A513; -.
DR Ensembl; ENSMMDT00005041029.1; ENSMMDP00005040201.1; ENSMMDG00005018612.1.
DR GeneTree; ENSGT00940000158999; -.
DR Proteomes; UP000472263; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd14347; UBA_Cezanne_like; 1.
DR Gene3D; 1.20.5.4770; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF9; OTU DOMAIN-CONTAINING PROTEIN 7A; 1.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472263};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 169..351
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 915..950
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 58..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 105936 MW; 785C6A8E580CA841 CRC64;
MTLDMDAVLS DFVRSTGAEP GLARDLLEGQ NWDLTAALSD YEQLRQVHTN LPHVFNEGRY
YRQPPLSPPP PPPPATAKRL SRGISHASSA IVSLARSHVA SECSSSSSSD QLPVEMPIYT
FQLPDLSVYS EDFRSFIERD LIEQSTMLAL EQAGRLNWWS TMCSSCKKLL PLATTGDGNC
LLHAASLGMW GFHDRDLVLR KSLYGMMKSG AEREALKRRW RWQQTQQNKE SGLVYTEEEW
EREWNELLKL ASSEPRTHSS KTSSTGGGVD NSEDPVYESL EEFHVFVLAH VLRRPIVVVA
DTMLRDSGGE AFAPIPFGGL YLPLEVPPSR CHCSPLVLAY DQAHFSALVS MEQKDQSREQ
AVIPLTDSEH RLLSLHFATD PGKDWDWSRD DNDNGKLAGL ILSLEAKLNL LHSYMNVTWI
RIPSETRAPL AMPESPTASA GEDVQSLADS MDSDRESVCS NSNVNNGKTA ASAAAAASSC
KDKTQEKEKA ERQQQRKDKD KTRTDSVANK LGSFSKTLGI KLKKNMGGLG GLVHGKINRS
NSGGNGRSKT TSPSPTERLP AMPSPLLERD RGSLLARLVG DKALSEHWKY STDVKLSLNI
LRAAMQGERK FIFAGLLLTS HRHQFHEEMI SFYLSNAQER FSQEQEQKRK EAEKKPTQAA
AAATTANGPA TTMTVSSAKK SDPESASGRE RERERERERE RERLTDRAAT PTPPPVAPPP
VSSLLPEGSS PAKQHHQSHT APPHLALKMQ GRHSPSPHSS PCSRRTLLGS AQPSAPIPVS
AHYSHTPPVQ RSSVIHLREV SVGSPPASLH EEPYRPVVGT LKTCATYPQQ NRSLSSQSYS
PARMSGVRTA GSSAAAEPYS MPGEHKSHTY TNGFNASDIR DCLEFADADS PPTWGGGISG
GAAADKTKGR GGMHCLQQRR CRRENCSFYG RPETENYCSY CYKEELKRRE REGKLHRPFS
//
