ID A0A3B5AAK3_9TELE Unreviewed; 677 AA.
AC A0A3B5AAK3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=usp49 {ECO:0000313|RefSeq:XP_008280929.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000017765.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000017765.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008280929.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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.
CC {ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_008280929.1; XM_008282707.1.
DR AlphaFoldDB; A0A3B5AAK3; -.
DR STRING; 144197.ENSSPAP00000017765; -.
DR Ensembl; ENSSPAT00000018039.1; ENSSPAP00000017765.1; ENSSPAG00000013418.1.
DR GeneID; 103357940; -.
DR CTD; 25862; -.
DR GeneTree; ENSGT00940000157997; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
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 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:SF7; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 49; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000694891};
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 2..99
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 261..675
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT COILED 147..185
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 677 AA; 76992 MW; 29DF0FE9C0F3D222 CRC64;
MDRCKHVGRL RLGQDHSILN PQKWHCVDCS TTDSVWACLK CSHVACGRFM EEHSLKHFQE
SHHPLAMEVR ELDVFCFACG DYVLNDNAEG DLKLLRGALS TVRSPGRRSL RSSTGGECTP
WVGEGGPQPA MQLALRHRRK ALLGKMLQMW ISKHQELQNQ RKEKLEEARR QKKEVKRRLM
EELGNVPPRK SARLLTQAPR STITLIPRKF RDPPERLPPP PKKPSLLTLS RKAPQNGRAA
KLRRYYSTHA VTRRRLAPGV TGLRNLGNTC YMNSILQVLS HLQKFRECFL TLDLCETEEL
LAKTNHSQGM KGVTGGVVNS GNTALSGCPL GRMGKAGCWN LPVGKKESVP PAPQASELVQ
PKEPRCSTRQ QMSLCHELHT LFRVMWSGRW SLVSPFAMLH SVWNLIPAFR GYDQQDAQEF
LCELLDKVQQ ELDTEGSKRR IVIPITKRKL SKQVLKVLNT IFHGQLLSQV TCLSCKHKSN
TVEPFWDLSL EFPERYHSID KGSGSSAYQR SCTLTEMLSK FTEMEALEGS IYACNHCNKR
RRKSSHKPLV LSEARKQLLI YRLPQVLRLH LKRFRWSGRN HREKIGVHVA FDQVLNIKPY
CCTGSGHSVH RGGYTYDLSA VVMHHGKGFG SGHYTAYCYN TEGGFWVHCN DSEMKVCSVE
EVCNTQAYIL FYTQRSA
//
