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Database: UniProt
Entry: A0A0V0WB55_9BILA
LinkDB: A0A0V0WB55_9BILA
Original site: A0A0V0WB55_9BILA 
ID   A0A0V0WB55_9BILA        Unreviewed;      1099 AA.
AC   A0A0V0WB55;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7 {ECO:0000256|ARBA:ARBA00021393};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   AltName: Full=Ubiquitin thioesterase 7 {ECO:0000256|ARBA:ARBA00031508};
DE   AltName: Full=Ubiquitin-specific-processing protease 7 {ECO:0000256|ARBA:ARBA00031500};
DE   Flags: Fragment;
GN   Name=Usp7 {ECO:0000313|EMBL:KRX72968.1};
GN   ORFNames=T06_10179 {ECO:0000313|EMBL:KRX72968.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX72968.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX72968.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX72968.1};
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|ARBA:ARBA00000707};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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:KRX72968.1}.
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DR   EMBL; JYDK01000190; KRX72968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0WB55; -.
DR   STRING; 92179.A0A0V0WB55; -.
DR   Proteomes; UP000054673; 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; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR024729; USP7_ICP0-binding_dom.
DR   InterPro; IPR029346; USP_C.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF880; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR   Pfam; PF00917; MATH; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF14533; USP7_C2; 1.
DR   Pfam; PF12436; USP7_ICP0_bdg; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50144; MATH; 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|ARBA:ARBA00022801, ECO:0000313|EMBL:KRX72968.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          65..190
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          209..515
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX72968.1"
SQ   SEQUENCE   1099 AA;  126761 MW;  DDF8D1FF7FC20DA1 CRC64;
     LMKSARPVED PYPVKVTELS EPMDVEENTV AVMENNNKSN GISTDKVEVK KQDEDDDDDD
     DYKAEGTLRL QIQDFSQVKG QVLSDPIYVR GLPWKIMAIP REIGRNQRSL GYFLQCNSDS
     DCPSWSCYAS ATLRLKSQKE GGNDCEKTIS HVFYPKENDW GYSCFLRWED VMDPQQGYLK
     DDTLLLEVHL VADAPHGVQW DSKKHTGYIG LKNQGATCYM NSLLQTLFFT NKLRKAVYQI
     STEQDDPHKS VALAMQRVFY ELQFSDKPVG TKKLTRSFGW DAFDSFLQHD VQELCRVLLD
     NLESKMKDTP VNGVIPQLFE GKMKSYVRCK KVPFESNREE AFYDIQLNVK GKANIYESFK
     DYVAVETLEG DNKYDAGDYG LQEATKGVVF IKFPPVLHLQ LMRVQYDPLN DQNLKINDRF
     EFPEKLDLDE FLESKESTPA KYTLHAVLVH SGDFHGGHYV VYINPKGNGR WCKFDDDVVS
     RCSKSEAIEQ NYGGNDSESA HRHCTNAYML AYIRDSVMDD ILCSVDEVDI PVQLRARLQR
     ERDVEALRKK EKSEAHLFCT VFVLSDDDFE GHQGPDLINT EQAERVCRKF RVRRTMTFSD
     VYAFMAREYQ LTPLVQFRLW PISNNESAGG LRPTTVPNLD GLTQIDRLSS GGDLEIALYM
     EVYDYLHGEL ELPSYRHSDD VLLFLKYYDP ISQTLIYCGH MIVSIDISLT DMIPEMCARV
     NLPPDTDIDI YEEDKYGDLE LLDKTAESVQ KACADFVDGL ILVYQSVELM KAKRGFKLAE
     VRSYYIELQN RVELEFIDKQ LECVENLVIQ ASFEWSYIDL ATVVGRRIGY DPFKIQFSRT
     SVYKDSNGLA VRFSLTSKLK DILNITTRSR VRRYRLYFQR MPLRIDELEL RFQVRIQYMD
     MKLRVEEMIV YPSKYGTVQD LLNEVSAGIQ FSEGSSKRLR LLQINSCRIV CTVQPDMVLE
     QMGFNHIVRV EEIPPDQVVV DPKSEFLLPV AHFYKDCYQT FGTPFYLKVK NGEPFGSVKQ
     RIQRILEVSD KEFEKFKFAL CTVSRTTYFE NENFIINLTD FTASHFSATA KPWLGLDHVN
     KMAKGRGMHT LEKAIVIHN
//
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