ID A0A091H775_BUCRH Unreviewed; 1343 AA.
AC A0A091H775;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000256|ARBA:ARBA00026136};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme 47 {ECO:0000256|ARBA:ARBA00030277};
DE AltName: Full=Ubiquitin thioesterase 47 {ECO:0000256|ARBA:ARBA00029910};
DE AltName: Full=Ubiquitin-specific-processing protease 47 {ECO:0000256|ARBA:ARBA00032453};
DE Flags: Fragment;
GN ORFNames=N320_10053 {ECO:0000313|EMBL:KFO90490.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO90490.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO90490.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO90490.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KL523926; KFO90490.1; -; Genomic_DNA.
DR MEROPS; C19.055; -.
DR Proteomes; UP000054064; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF702; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 47; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF19718; USP47_C; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KFO90490.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054064}.
FT DOMAIN 156..532
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 99..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 546..573
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 400..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO90490.1"
FT NON_TER 1343
FT /evidence="ECO:0000313|EMBL:KFO90490.1"
SQ SEQUENCE 1343 AA; 153376 MW; DD669CD5948AC98C CRC64;
QVESAAEEPR VLCIIQDTTN SKTVNERVTL NLPASTPLKR LFEDVASKVG YVNGTFDLMW
GNGDNVIDMT PIDQNSDKTI LDAGFEPGKK NFLHLIDKDG EQPHTMPEES GTTEDSAQDR
FIGPLPREGS VGCTNDYVSQ SYSYSSVLSK SETGYVGLVN QAMTCYLNSL LQTLFMTPEF
RNALYKWEFE ESEEDPVTSI PYQLQRLFVL LQTSKKRAIE TTDVTRSFGW DSSEAWQQHD
VQELCRVMFD ALEQKWKQTE QADLINQLYQ GKLKDYVRCL ECGYEGWRID TYLDIPLVIR
PYGSNQAFAS VEEALHAFIQ PEILDGPNQY FCERCKKKCD ARKGLRFLHF PYLLTLQLKR
FDFDYTTMHR IKLNDRMTFP EELDMSVFID VEDEKSPQTE SCTDSGAENE GSCHSDQMSN
DFSNDDGVDE GICLESNSTA ERISKAGSEK SSLLYELFSV MVHSGSAAGG HYYACIKSFS
DDQWYSFNDQ HVSKITQEDI KKTYGGSSGS RGYYSSAFAS STNAYMLIYR LKDPTRNAKF
LEAHEYPEHI KQLVQKEREL EEQEKRQREI ERNTCKIKLF CMHPTKQIMM ENKLEVHKDR
TLKEAVEIAY KLMDLEEAVP LDCCRLVKYD EFHDYLERSY EGEEDTPMGL LLGGVKSTYM
FDLLLETRRP DQIFQCYKPG EVMVKVHVVD LKAESVSPPI SVRAYLNQTV SEFKQLISKA
TNLSAETMRV VLERCYNDLR LLNISSKTLK TEGFFRSNKV FIESSESLDR HVAYTDSHLW
KLLDRHANTI RLYVSLPEQS PGSQLRRAVY HKASGDAGNL DEACERVKGP VGNMKSVEAI
LEESTEKLKS LSLQQQQEGD NGDSSKSTEA SDFENIESPL NEIDSSASAE NRELENQIQI
SDPENLQSEE RSDSDVNNDR STSSVDSDIL SSSHSSDTLC NVDNAPLPLA NGLDSHSITS
SRRSKANQGK KETWDTAEED SGTDSEYDES GKSRGEAQYM YFKSEPYAAD EGSGEGQKWL
MVHVDKRITL SAFKQHLEPF VGVPSSHFKV FRVYASNQEF ESVRLNETLS SFSDDNKITI
RLGRALKKGE YRVKVYQLLV NEPEPCKFLL DAVFAKGMTV RQSKEELLPQ LREQCGLDLT
IDRFRLRKKT WKNPGTVFLD YHIYEEDINI SSNWEVFLEI LDGVEKMKSM SQLAVLSRRW
RPSEMKLDSF QEVVLESSSV EELKEKLSEI SGIPLENIEF AKGRGTFPCD ISILEIHQDL
DWNPKVSTLN VWPLYICDDG AVIFYRDKTE ELMELTDEQR NELMKKESSR LQKTGHRVTY
SPRKEKALKI YLDGAPNKDL TQD
//