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Database: UniProt
Entry: A0A0V0ZX84_9BILA
LinkDB: A0A0V0ZX84_9BILA
Original site: A0A0V0ZX84_9BILA 
ID   A0A0V0ZX84_9BILA        Unreviewed;      1122 AA.
AC   A0A0V0ZX84;
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 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};
GN   Name=Usp7 {ECO:0000313|EMBL:KRY17344.1};
GN   ORFNames=T12_15948 {ECO:0000313|EMBL:KRY17344.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY17344.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY17344.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY17344.1};
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:KRY17344.1}.
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DR   EMBL; JYDQ01000063; KRY17344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0ZX84; -.
DR   STRING; 990121.A0A0V0ZX84; -.
DR   Proteomes; UP000054783; 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:KRY17344.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          88..213
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          232..538
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          56..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1122 AA;  129380 MW;  8A437514F42DF88B CRC64;
     MVEAEFFAFK TQLNDSVLLQ NGPLMKSARP VEDPYPVKVT ELSEPMDVEE NTVAVMENNN
     KSNGISTDKV EVKKQDEEDD DDDDYKAEGT LRLQIQDFSQ VKGQVLSDPI YVRGLPWKIM
     AIPREIGRNQ RSLGYFLQCN SDSDCPSWSC YASATLRLKS QKEGGNDCEK TISHVFYPKE
     NDWGYSCFLR WEDVMEPEHG YLKDDTLILE VHLVADAPHG VQWDSKKHTG YIGLKNQGAT
     CYMNSLLQTL FFTNKLRKAV YQISTEQDDP HKSVALAMQR VFYELQFSDK PVGTKKLTRS
     FGWDAFDSFL QHDVQELCRV LLDNLESKMK DTPVNGVIPQ LFEGKMKSYV RCKKVPFESN
     REEAFYDIQL NVKGKANIYE SFKDYVAVET LEGDNKYDAG DYGLQEATKG VVFIKFPPVL
     HLQLMRVQYD PLNDQNLKIN DRFEFPEKLD LDEFLESKES TPAKYTLHAV LVHSGDFHGG
     HYVVYINPKG NGRWCKFDDD VVSRCSKSEA IEQNYGGNDS ESAHRHCTNA YMLAYIRDSV
     MDDILCSVDE VDIPVQLRAR LQRERDVEAL RKKEKSEAHL FCTVFVLSDD DFEGHQGPDL
     INTEQAERVC RKFRVRRTMT FSDVYAFMAR EYQLTPLVQF RLWPISNNES AGGLRPTTVP
     NLDGLTQIDR LSSGGDLEIA LYMEVYDYLH GELELPSYRH SDDVLLFLKY YDPISQTLIY
     CGHMIVSIDI SLTDMIPEMC ARVNLPPDTD IDIYEEDKYG DLELLDKTAE SVQKACADFV
     DGLILVYQSV ELMKAQRGFK LAEVRSYYIE LQNRVELEFI DKQLECVENL VIQASFEWSY
     IDLATVVGRR IGYDPFKIQF SRTSVYKDSN GLAVRFSLTS KLKDILNITT RSRVRRYRLY
     FQRMPLRIDE LELRFQVRIQ YMDMKLRVEE MIVYPSKYGT VQDLLNEVSA GIQFSEGSSK
     RLRLLQINSC RIVCTVQPDM VLEQMGFNHI VRVEEIPPDQ VVVDPKSEFL LPVAHFYKDC
     YQTFGTPFYL KVKNGEPFGS VKQRIQRILE VSDKEFEKFK FALCTVSRTT YFENENFIIN
     LTDFTASHFS ATAKPWLGLD HVNKMAKGRG MHTLEKAIVI HN
//
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