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Database: UniProt
Entry: A0A087VBK4_BALRE
LinkDB: A0A087VBK4_BALRE
Original site: A0A087VBK4_BALRE 
ID   A0A087VBK4_BALRE        Unreviewed;       386 AA.
AC   A0A087VBK4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE   Flags: Fragment;
GN   ORFNames=N312_02330 {ECO:0000313|EMBL:KFO09996.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO09996.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO09996.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO09996.1};
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,
CC         ECO:0000256|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; KL487167; KFO09996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087VBK4; -.
DR   Proteomes; UP000053309; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02660; Peptidase_C19D; 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; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR   Pfam; PF00443; UCH; 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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KFO09996.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          37..381
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO09996.1"
FT   NON_TER         386
FT                   /evidence="ECO:0000313|EMBL:KFO09996.1"
SQ   SEQUENCE   386 AA;  43980 MW;  7B0E843EFFE2BFC1 CRC64;
     GIGEKYSTWE PTKRELELLR HNPKRRKITT NCTIGLRGLI NLGNTCFMNC IVQALTHTPL
     LRDFFLSDRH KCEMQSPSSC LVCEMSTLFQ EFYSGHRSPH IPYRLLHLVW THARHLAGYE
     QQDAHEFLIA ALDVLHRHCK GDDNGKKANN PNHCNCIIDQ IFTGGLQSDV TCQVCHGVST
     TIDPFWDISL DLPGSSTPFW PLSPGSDGSV VNGESHVSGT TTLTDCLRRF TRPEHLGSSA
     KIKCSGCHSY QESTKQLTMK KLPIVACFHL KRFEHSAKLR RKITTYVSFP LELDMTPFMA
     SSKESRMNGQ YQQPTDSLNN DNKYSLFAVV NHQGTLESGH YTSFIRQHKD QWFKCDDAII
     TKASIKDVLD SEGYLLFYHK QFLEYE
//
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