ID A0A0M5JDZ3_DROBS Unreviewed; 1140 AA.
AC A0A0M5JDZ3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=Dbus_chrXg1662 {ECO:0000313|EMBL:ALC49806.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC49806.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC49806.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC49806.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-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}.
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DR EMBL; CP012528; ALC49806.1; -; Genomic_DNA.
DR RefSeq; XP_017852750.1; XM_017997261.1.
DR AlphaFoldDB; A0A0M5JDZ3; -.
DR SMR; A0A0M5JDZ3; -.
DR STRING; 30019.A0A0M5JDZ3; -.
DR GeneID; 108606799; -.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000494163; Chromosome x 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:UP000494163};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 112..233
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 252..559
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 132482 MW; 2379253954FA4444 CRC64;
MDIETDQSIE AMDTQDTQEV EITTSDLQQQ QQLQQDQTNS PQLPKFKNLM HSQLQQQQQQ
QQQQQQQQQL PPSENGNMPP QQLLAESSST SFGNEQEMTM DDETKEDQFR SETTFSYTVE
NVGQIKQQHL SPPVYVRMLP WKIMVIPNDR ALGFFLQCNG ENDSPTWSCN AIAELRLKCH
KSDLQPFTRA KIKHLFYSKE NDYGYSNFIT WQELQDPDKS YVHNGSITLE VHVIADAPHG
VLWDSKKHTG YVGLKNQGAT CYMNSLLQTL YFTNSLRLAV YRIPTEADDS TKSVGLSLQR
VFHELQFGDR PVGTKKLTKS FGWETLDSFM QHDVQEFLRV LLDKLESKMK GTCLEGTIPG
LFEGKMSSYI KCKNVDYNST RYETFYDIQL NIKDKKNIFD SFQDYVASET LEGDNKYDAG
VHGLQEASKG VIFTSFPPVL HLHLMRFQYD PITDSSIKYN DRFEFYENIN LDRYLAEREK
TPADYVLHAV LVHSGDNHGG HYVVFINPKA DGRWFKFDDD VVSSCRKQEA IEQNYGGMDD
EISFHAKCSN AYMLVYIRES ELDRVLGDIP ETEISSDLVE RLDLEKRIEM ARRKERSEAN
LYMNIHVILE EYFESQQKRR LFDLEKTHQR PFKLKNNQTV NEMVEMLVKA FGVPRDRMRM
WNMCTAQTQK FLHFDFEAEA TRTLEQIPPP QKPWVIFLEL ASPESTAALL PFNPKTDVLL
FLKYYDARNK RLNYIGCTQQ PLSRRLGELV PEINRKLGFE EDTELTVFDE YADKKIGNLN
EPIENVLYIT QDHLQGPILI FERDNVDMKL DLPTVEDYFL DLVYRIEIIF TDKCNANEPD
FTLELSNRYN YDQLSNAVAE RLNTDPQKLQ FFMGINNYKE TAGNAVPYTF KGTIKDLLSY
TKQSTPKRIY YQRLSLSLHE LDNKKLFKCI WVSHDLKEEK ELVLYPNKND NVKGLLDEAA
KTISFAENSR RKLRLMKVGN HKIMAVCKDD IPLETLIRTN ESITTTQGTQ KIFRIEEIGP
DEMHIGENEM LVPCAHYSKE LYNSFGTPFL AKARHGEPYG AFKQRIQKRL CVPEKEWENY
KFTIISVGQN VDINDNTPVD LEVYRSWTGG QLPFFGLDHI NKSRKRSSLN FSEKAIKIYN
//
