ID A0A1A9VNH6_GLOAU Unreviewed; 1026 AA.
AC A0A1A9VNH6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT042612-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT042612-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT042612-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A1A9VNH6; -.
DR STRING; 7395.A0A1A9VNH6; -.
DR EnsemblMetazoa; GAUT042612-RA; GAUT042612-PA; GAUT042612.
DR VEuPathDB; VectorBase:GAUT042612; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000078200; 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 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; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 83..204
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 223..609
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 16..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 119400 MW; 519FC2D52EF20826 CRC64;
MEIEPDQSME AMDIQEMDAL PGGELQHQQH LNKLHLSPNP GQLPNENGNV PPQQLLADSG
SPYANEQEMA EDDDLKEDQC RSEAIFSYIV ENIVHLKQQQ LSPPVFVRML PWKIMVIPNE
RALGFFLQCN GENDSPTWSC NAIAELRLKS HKPGAKPFTR MRIKHLFYSK ENDYGYSNFI
SWQELRDPDN YYIHNGAITL EVFVHADAPH GVLWDSKKHT GYVGLKNQGA TCYMNSLLQT
LYFTNQLRRA VYKIPTEADD STKSVGLSLQ RVFHELQFSD KPVGTKKLTK SFGWETLDSF
MQHDVQEFLR VLLDKLESKM KGTNLEGTIT ALFKGKMFSC IKCENVDYSS MRYETFYDIQ
LNVKGKKDIM ESFQDYVATI NLKDDNKYDA GYYGLQWYKF DDDVVCSCKK IEAIELNYGG
MDDEVSFHAK CSNAYMLVYI RKSEINRILS DILENEIPSE LVERLDLEKR IEMARRKERS
EVNLYVSVHI ILEEYFEAQQ KRRLFDLDKI HQRLFKFKQT QSVEEMMEQF VKSFCVPKGR
MRVWIMYAAQ TQKFFYFDFQ REGHRTIEQI PSSQKPWVIF LELAPQDKPG GALQPFDPKK
EVLIFFKFYD ARNKRLNYIG CSQQPLGRRL IEIVPDVNTH LGFDNDTELT VYDECNDRKV
TNLNETLENI LDSHPDNTER GTLQGFILIF EKDHADPKLE LPTVVDYFSD LVYRVEVTFC
DKGNPNEPEI VLELSNRYTY DQMAQAVAER LNTDPNKLQF FTCTSSYKDQ PGTAIQYQTK
SCLKELLMPS KQSATKKLFY QRLSLSIHEL DNKKQFKCIW VSNDLKDEKE LVLYPNKNDT
VKGLLDEAAK KIQFSENSSK KLRLLKVNNH KIVTVLKEDM SLESLQNAMD PITPQSAQKT
FRIEEVPMED IQLAENEMLI PVAHYSKEIF NLFGVPFLIK AKLNEPYGAL KQRIQKRLNV
PDKEWENYKF VIMGGNTSDV HDNTPVDFDT YRTWNKSWPH FGLDHINKSR KRTSLNFSEK
AIKIYN
//
