ID A0A0L0BUU0_LUCCU Unreviewed; 1118 AA.
AC A0A0L0BUU0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=FF38_13826 {ECO:0000313|EMBL:KNC23758.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC23758.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC23758.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC23758.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC23758.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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:KNC23758.1}.
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DR EMBL; JRES01001303; KNC23758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0BUU0; -.
DR STRING; 7375.A0A0L0BUU0; -.
DR EnsemblMetazoa; KNC23758; KNC23758; FF38_13826.
DR EnsemblMetazoa; XM_023443027.2; XP_023298795.1; LOC111681273.
DR EnsemblMetazoa; XM_023443028.2; XP_023298796.1; LOC111681273.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000037069; 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, ECO:0000313|EMBL:KNC23758.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 87..208
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 227..534
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 18..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 129785 MW; 7ADC28EDFEFD8344 CRC64;
MEIEPDQSME AMDIQEIDSL PGAELHQQQH LQKLHLPPTA GGQQQLPNEN GNVPPQQLLA
DSGSPYTNEQ EMTALDDGPK EDEFRSEATF SYTVEKIAQL KTQQLSPPVY VRMLPWKIMV
IPNERALGFF LQCNGENDSP SWSCNAIADL RLKSHKPGAK PFSRMRIKHL FYAKENDYGY
SNFITWQELQ DPENCYIHNG AITLEVFVHA DAPHGVLWDS KKHTGYVGLK NQGATCYMNS
LLQTLYFTNQ LRRAVYKIPT EADDSTKSVG LSLQRVFHEL QFSDKPVGTK KLTKSFGWET
LDSFMQHDVQ EFLRVLLDKL ESKMKGTNLE GTIPGLFEGK MSSYIKCKNV DYNSTRYETF
YDIQLNIKDK KDIYESFQDY ITPETLEGDN KYDAGVHGLQ EANKGVHFTS FPPVLHLHLM
RFQYDPVTDS SIKYNDRFQF YEQIDLDRFL EKEGDTKAEY ILHAVLVHSG DNHGGHYVVF
INPKCDGKWY KFDDDVVCSC RKNEAIEMNY GGMDEEVSFH AKCSNAYMLV YIRKSEIERV
LSDIPEHDIP SELVDRLELE KRIEMARRKE RSEANLYVSI HVILEEYFEA QQKRRLFDLD
KVHQRLFKMK QTQTIEEMMD QFVKSFCVPK ERMRVWIMYV TQTQKFLYFD FQREGNRSIE
QIASSQKPWV IFLELAPPDK PSRALPTFDP KKEVLIFFKY YDARNKRLNY IGCSQQPLGK
RLVELVPDIN THLGFERDTE LTVFDECNDQ KITNLNESLE TVLCLHPDNA DRGSLQGYIL
IFEKEHIDPK LELPTVIDYF NDLVYRVEIT FCDKTNPNEP EIVLELSNRY TYDQMAQAVA
ERLNTDPNKL QFFTCTGSYK DQPGTAIQYN QKGCLKDLLV STKQSNTKKL FYQRLSLSIH
ELDNKKQFKC IWVSNDLKEE KELVLYPNKN DTVKGLLDEA AKKIQFSENS SKKLRLLKVN
NHKISTIFKE DIPLESLQKT TEPITPQSTQ KTFRIEEVPL EDIQLAENEI LIPVAHYSKE
IFSVFGVPFL IKARQGEPYG ALKQRIQKRL NVPDKEWENY KFAVIGGNTP DFNDNTPIDI
NVYRSWNGNA PFFGLDHINK SRKRTSLNFS EKAIKIYN
//
