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Database: UniProt
Entry: A0A0V1CQD8_TRIBR
LinkDB: A0A0V1CQD8_TRIBR
Original site: A0A0V1CQD8_TRIBR 
ID   A0A0V1CQD8_TRIBR        Unreviewed;       727 AA.
AC   A0A0V1CQD8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, 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=usp20 {ECO:0000313|EMBL:KRY51489.1};
GN   ORFNames=T03_3816 {ECO:0000313|EMBL:KRY51489.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY51489.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY51489.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY51489.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY51489.1}.
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DR   EMBL; JYDI01000124; KRY51489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1CQD8; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
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:SF86; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 2.
DR   PROSITE; PS51283; DUSP; 2.
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:KRY51489.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          54..492
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          494..595
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          619..726
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
SQ   SEQUENCE   727 AA;  83402 MW;  58F6775F51E59508 CRC64;
     MFNLFHAFRL CTLFIFYLKI FLLRDILRQL AMLSKIGLPV SVLTHTDEPN FGLKGIQNLG
     NTCYLNAAVQ ALSNCPPLTE YMRHCSLPCS SSPDGNRRNK LASEFQKLID TLWDDEYENM
     LSPIFFVDAV LACNPHFRLF QQQDTQEFLR FLLNELHEQL KRPVYKWEHR LLKTRNHHEM
     LKNNTHGYDS DSSMSSCSSF VSCVSAASDN LDCEKNGISS DTDDASSYNS TAELMEGSDN
     FVAEEEVLNK EFLLRKPVRY NSIINDIFSG QLVTSITCLR CKSVSHNKEI FQDISLSIPS
     LEQLVLMQNA SINGNEYVSP SSVANQSWLS WLTLRFKEYI SRMDLTLSDC LKLFFSPEDL
     RGDDMYRCDR CKSLQPGVKI CRLLKTPQIL CIHIKRFRHE ASSSFKLNNR IDFPLEGLDL
     SDFVQGRSSD LHTYNLVAVI SHSGNADGGH YVSYCMNHSN YRWYLFDDET VTAVDPCTVE
     NVEAYVLFYE KTSNTIGFVR EQASALFENS HLLSPVETSF YYISMEWVIR LSTFAEPGPV
     NNYSFLCRHG RNNNFVNGKK LSSMHNYCLK LSPSLWNYLR VKFGGGPVCH HLKHCIICSA
     YQEAFESRRK HELSKFYRYQ NDDEYFISKS IADENHDFAS SSRLICTKWL RRWKAFVFGE
     TDELPGPIDN SCMVPVPLRN GSAKTISIEV SDLLPNLCFC CINNDTWRDL ISIYGGGPEI
     CCQNKEL
//
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