ID A0A3P9PG84_POERE Unreviewed; 307 AA.
AC A0A3P9PG84;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000020804.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000020804.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000020804.1};
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A3P9PG84; -.
DR Ensembl; ENSPRET00000021025.1; ENSPREP00000020804.1; ENSPREG00000013518.1.
DR GeneTree; ENSGT00390000001830; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000013518; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.40; -; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR InterPro; IPR033865; Ataxin-3.
DR InterPro; IPR006155; Josephin.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR14159; ATAXIN-3-RELATED; 1.
DR PANTHER; PTHR14159:SF0; ATAXIN-3-RELATED; 1.
DR Pfam; PF02099; Josephin; 1.
DR Pfam; PF02809; UIM; 2.
DR PRINTS; PR01233; JOSEPHIN.
DR SMART; SM01246; Josephin; 1.
DR SMART; SM00726; UIM; 2.
DR PROSITE; PS50957; JOSEPHIN; 1.
DR PROSITE; PS50330; UIM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00331}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..179
FT /note="Josephin"
FT /evidence="ECO:0000259|PROSITE:PS50957"
FT REGION 275..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 13
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1,
FT ECO:0000256|PROSITE-ProRule:PRU00331"
SQ SEQUENCE 307 AA; 35081 MW; D609055EA43ECE66 CRC64;
YSHLHSLQEG SLCAQHCLNN LLQGEYFTPV DLSSIAHQLD EEERMRMAEG GMASEEYRTF
LQQPSGNMDD SGFFSIQVIS NALRVWGLEL ILFNSPEYQR LMINPINEKA FICNYKEHWF
TIRKLGQQWF NLNSLLTGPE LISDTYLALF LAQLQQEGYS IFVIRGNLPE CEAEQILGIM
RVHQQQRPRL IGEDEAQTSM GYVSTARRRP DPTEPLTPVF TASRTSASQV QTDAGFVVED
EDEELKRALA LSRQDMDVED EEADVRRAIQ LSMQGVKSSS ADEGQKVQSE TLTAEELRKR
RQAYFDR
//
