UniProt: A0A096M3X5

Database: UniProt
Entry: A0A096M3X5_POEFO

LinkDB:  A0A096M3X5_POEFO 
Original site:  A0A096M3X5_POEFO

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (5)   
   Pfam (3)   
   PROSITE (3)   
   SMART (1)   
All databases (21)   

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ID   A0A096M3X5_POEFO        Unreviewed;       748 AA.
AC   A0A096M3X5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000026116.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000026116.1}
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   -!- SIMILARITY: Belongs to the peptidase C64 family.
CC       {ECO:0000256|ARBA:ARBA00005865}.
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DR   EMBL; AYCK01001825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A096M3X5; -.
DR   Ensembl; ENSPFOT00000027275.1; ENSPFOP00000026116.1; ENSPFOG00000017835.2.
DR   GeneTree; ENSGT00940000158045; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd22767; OTU_ZRANB1; 1.
DR   Gene3D; 1.25.40.560; -; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 3.
DR   InterPro; IPR041294; AnkUBD.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR049768; ZRANB1_OTU.
DR   PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR   PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1.
DR   Pfam; PF18418; AnkUBD; 1.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00547; ZnF_RBZ; 3.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 3.
DR   PROSITE; PS50199; ZF_RANBP2_2; 3.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          4..33
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          92..115
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          169..198
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          472..632
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   REGION          123..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   748 AA;  84711 MW;  54C5193D58E1CC2B CRC64;
     MTELVAKWAC EYCTYENWPS AIKCTMCRAQ RPSGGAIITE EPFKSSPALD ASLHQWDPAD
     LSNSPSQGGS SLLICPDSSA RPRVRVTDVP ETSSKWSCHM CTYLNWPRAI RCTQCLYGHH
     ATRQGHHTQQ PRSPTESPQT SGSGCRPAAP VTATDPCEEY NDRNRLNTHT QHWTCTACTY
     ENWAKALKCV VCDHPRPNSL LAEPIELASE PESQQPSSKL NEQDRDNRRG VVGQGTGCVV
     GGVVGCSSSQ RRSPPSEKRE SEVNMDFQRI ELASGAGIGS KEELEVDFKK LKQIKNRMRR
     TDWLFLNACV EGVVEGDLAA VEAYKTSGGD IARQLTSDEV RLLNRPSAFD DGFTLVHLAI
     RFQRQDMLAV LLTEVSQQAA KCIPAMVCPE LTEQIRREVA ASLHQRKGDF TCYFLTDLVT
     FTLPADIEDL PPAVQEKLFD EVLDRDVQKE LEEESPIINW SLELGTRLDS RLYALWNRTA
     GDCLLDSVLQ ATWGIYDKDS VLRKTLHDSL HDCSHWFYSR WKEWESWYSQ SFGLHFSLRE
     EQWQEDWAFI LSLASQPGSS LEQTHIFVLA HILRRPIIVY GVKYYKSFRG ETLGYTRFQG
     VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGFDNR GAGANLNTDD DETVTFLPLV
     DSERKLLHIH FLSAQEMGNE EQQEKLLREW LDCCVTEGGI LVALQKSSRR CNHPLVTQMV
     EKWLDGYRQI RPCASLSDGE EEEDDDDE
//

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