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Database: UniProt
Entry: A0A087YJ29_POEFO
LinkDB: A0A087YJ29_POEFO
Original site: A0A087YJ29_POEFO 
ID   A0A087YJ29_POEFO        Unreviewed;       506 AA.
AC   A0A087YJ29;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:ENSPFOP00000018032.2, 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:ENSPFOP00000018032.2}
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         ECO:0000256|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038490}.
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DR   EMBL; AYCK01000799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007560606.1; XM_007560544.2.
DR   AlphaFoldDB; A0A087YJ29; -.
DR   STRING; 48698.ENSPFOP00000018032; -.
DR   Ensembl; ENSPFOT00000018054.2; ENSPFOP00000018032.2; ENSPFOG00000017933.2.
DR   GeneID; 103143837; -.
DR   KEGG; pfor:103143837; -.
DR   CTD; 23326; -.
DR   eggNOG; KOG1867; Eukaryota.
DR   GeneTree; ENSGT00940000156623; -.
DR   OMA; QRDQWFK; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02660; Peptidase_C19D; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          4..121
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          159..501
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   506 AA;  58318 MW;  495F252D9B42B68D CRC64;
     MSPAGCPHVN SFKVDNWKQN LRLIYQCFVW SGSAETRKRK AKSCICHMCG AHLNRLHSCL
     YCVFFACFSK KHIHEHAKSK RHNLAIDLLY GGIYCFMCQD YIYDKEMEQI AKEEQRKAWK
     MQGIGEKYST WEPTKRELEL LRHNPKRRRI TSNCTIGLRG LINLGNTCFM NCIVQALTHT
     PLLRDFFLSD RHKCEMQSNS CLVCEMSQLF QEFYSGHRSP HIPFRLLHLV WTHARHLAGY
     EQQDAHEFLI AALDVLHRHC KDDNGKKANN PNHCNCIIDQ IFTGGLQSDV TCQVCHGVST
     TIDPFWDISL DLPGSSTPFW PLSPGGDVTA LNGESHATGA TTLMDCLRRF TRPEHLGSSA
     KIKCSGCHSY QESTKQLTMK KLPIVACFHL KRFEHSAKLR RKITTYVSFP LELDMTPFMA
     SSKESRMNGQ YQQTVEAFNN DNKYSLFAVV NHQGTLESGH YTTFIRQHKD QWFKCDDAII
     TKASIKDVLD SEGYLLFYHK QFLEYE
//
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