ID A0A2A4K8B3_HELVI Unreviewed; 1123 AA.
AC A0A2A4K8B3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=B5V51_13250 {ECO:0000313|EMBL:PCG79910.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG79910.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG79910.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG79910.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG79910.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-2017) 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:PCG79910.1}.
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DR EMBL; NWSH01000075; PCG79910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4K8B3; -.
DR Proteomes; UP000218220; 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; cd03772; MATH_HAUSP; 1.
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:SF644; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 84..213
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 232..540
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 129895 MW; 113E00B33110EFDC CRC64;
MNHTPAPDRQ QQHDSNVNQV EEMETQDVET VDTVTDKTWE DDLMKGPNGE VVMGEVMKNQ
ETTSSDMPLA CLDTEMEDDE ARSETTFRFT VQNFRNLKDS VLSPACFVRN LPWKIMVMPR
QAPSPDRQQQ KSLGFFLQCN GESESSSWSC YAMAELRLIS HKPDTEPFFR KIQHLFYSKE
NDWGFSHFMA WNDVLDPEKG YIKDDAITLE VHVTAEAPHG VSWDSKKHTG YVGLKNQGAT
CYMNSLLQTL YFTNQLRKAV YKMPTESDDS TRSVALALQR VFYELQFSDK PVGTKKLTKS
FGWETLDSFM QHDVQEFLRV LLDKLESKMK GTCVEGTVPR LFEGKMTSYI KCKNVNVSST
RVETFYDIQL NIKGKKNIDE SFKDYISTET LDGENKYDAG EHGLQEAEKG VIFASFPPVL
HLHLMRFQYD PITDSSVKFN DRFEFYEHIN LDAYLQEKPE TPADYTLHAV LVHSGDNHGG
HYVVFINPKG DGKWCKFDDD VVSRCTKQEA IEYNYGGHDE DMALTVRHCT NAYMLVYIRD
SQLKTVLQEV TQADIPTELS ERLAEEKRIE TIRRKERNEA HLYMNVNVVL EEAFDGHQGN
DLYDPERAHY RVFRVRKQAT VADLMDLLAD SFKFPPKQLR PWPFSARSNQ TCRPTCLDIV
NDQHKTVADV SENMNPWNIF LEMLPPDSGF SALPTFDKEN DVVLFFKFYD PKQKRIHYCG
HHYLPIASKP ADLIPILNKR AGFPPDTPLV LYEEIKPDFV EKISNYSEPL EKVLDELMDG
DIIVFERADH RHEDLELPTC QDYFKYIFYK VEVQFVDKTV PNDPGFTMEL SMQMRYDQMA
RAVGQRLNVD PYLIQFFKCQ NYKDTPGLPL RYSYDGILKD LLVYCKPKCP KKLFYQILSI
KVNELDNKKQ FKCLWVGPNY KEDKELILYP NKGGKVSDIL QEAAKVVEMS PDGSGTLRIV
EVSCHKVLPG PDPELTLDQV TISPPRLYRI EEIPRDELNL QEDEIIVPCA HFHKQVYATF
GIPFYARVKH NEPFQAVKDR LQKKLDIPDK EWEKYNFAIV TNGRPNYISE GATINIYDFR
PSSNANLSLP DATARPWLGL EHINKTPKRS RVNYLEKAIK IYN
//
