ID A0A0T6B0P9_9SCAR Unreviewed; 1110 AA.
AC A0A0T6B0P9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AMK59_5901 {ECO:0000313|EMBL:KRT81039.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT81039.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT81039.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT81039.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT81039.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-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:KRT81039.1}.
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DR EMBL; LJIG01016292; KRT81039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6B0P9; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000051574; 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:UP000051574};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 76..206
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 225..534
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..66
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 1110 AA; 127992 MW; 5982BCEA7FAC0A1E CRC64;
MNHVTGQDRR NEVSPQNNVS EVEEMETQAD VAMEYTTDSG GGEMESQNGD VVIGPQPDPS
VTTQDADMEE DDARSEATFK FSVTQFSKLK DSVLSPPCYV RNLPWKIMVM PRTSHAQERT
PAQKSLGFFL QCNGESESSS WSCYAVAELR LLSVRPDGEP FSRKIQHLFY SKENDWGFSH
FMSWNDVLDV EKGYIKDDTI TLEVHVVADA PHGVSWDSKK HTGYVGLKNQ GATCYMNSLL
QTLYFTNQLR KAVYKMPTES DDSTKSVALA LQRVFHELQF CDKPVGTKKL TKSFGWETLD
SFMQHDVQEF LRVLLDKLES KMKGTCVEGT VPKLFEGKMI SYIRCKNVDY TSNRTETFYD
IQLNIKGKKN IDESFKDYIA RETLDGENKY DAGEHGLQDA EKGVIFSSFP PVLHLHLMRF
QYDPITDCSV KFNDRFEFYE KISLDNYLQE PDPTNPANYT LHAVLVHSGD NHGGHYVVFI
NPKGDGKWCR FDDDVVSRCT KQEAIEYNYG GHDEDMNMTV KHCTNAYMLV YIRDSELHNV
LKEVTDADIP SELADRLAEE KRMEQVRRKE RSEAHLYMTI NILLEDAFDG HQGNDLYDPE
KALYRVFKIK KTATVAEMLE MLAVSFKYPP EQIRPWPFGT RSNNTFRPSM LDLEQDLHKS
VIDASENQNP WNIFLELLPP DSELNSLPPF DKESDVLMFF KMYDPKQKKI HYCGHGYLAV
TSKLSEIVPV LNERAGFPRD TELALYEEIR PNMVDRINDL NMPLERVLEE LMDGDIIVFE
KEDREELSDL PTCVDFFKDL FHRVEVTFVD KCIPNDQGFT MELSQRMTYD QLARAVAQRV
GTDPYLLQFF KCQSYKDSPG HPLRCTFEGT LKDLLVYTKP KMPKKIFYQQ LSIRVNELES
KKQFKCPYLG LTMKDEKELI LYPNKNGTVG DLLDEAKKQI EFTEGSTGKL RLTEISCNKV
SLGPKEDTSL ETIALCTSKV YRIEEIPRDE IHLADDEMLV PCAHFYKEVF STFGSPFLIK
IKQGEPFLKV KERIQKKLAL PEKEFEKFKF AIVAMNQPNF IRDDDYIINL TEFKPHSTQT
GKPWLGLEHV NKAPKRARFN YLEKAIKIYN
//
