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
//