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
//