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
//