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Database: UniProt
Entry: A0A091H775_BUCRH
LinkDB: A0A091H775_BUCRH
Original site: A0A091H775_BUCRH 
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
//
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