ID A0A1A9UGQ0_GLOAU Unreviewed; 1169 AA.
AC A0A1A9UGQ0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=XPG N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
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:GAUT004280-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:GAUT004280-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT004280-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC {ECO:0000256|ARBA:ARBA00005283}.
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DR AlphaFoldDB; A0A1A9UGQ0; -.
DR STRING; 7395.A0A1A9UGQ0; -.
DR EnsemblMetazoa; GAUT004280-RA; GAUT004280-PA; GAUT004280.
DR VEuPathDB; VectorBase:GAUT004280; -.
DR OrthoDB; 26655at2759; -.
DR Proteomes; UP000078200; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR PRINTS; PR00066; XRODRMPGMNTG.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 807..876
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 171..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 763..790
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 327..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 133015 MW; 3B5595B3FB4956CA CRC64;
MGVTGLWKLI DSCGKPVPVE SLEGKVLAVD ISIWLHQVIK GFQDNKGAAL NNAHLLGLFH
RLCKLLYYRV KPVFVFDGCV PQLKKETIAR RQQQRSKLNT EAERIQALLL QSLAKEQMVQ
QALGPNTAEL LLTSPLKRIA QSKTTQKNES ADDMFKLPDL PCISEDSQDS FNNSLDKSAT
DTSADDSSFE EDCARRNYNT NLQTLDVRSQ HFRSLPADVR HEILVDIKET RKQSSWGRLH
ELPSRSNDFS TFQMKRLLKR RDVQVSLEEA EKQMGGRTLT YSELSNIFTE EGILESSIVN
KGSKQVCSDE HTRFLLVRDL KKQLSQGKNV KEEKTIAETK ELQSDELLPS TSKTAKPKSE
EEADDDYETD LQMAIALSLV DTTTVYDKKD YEYDSSEALK LNKSQRQELK HAAKGPARSY
MIEYGGMNDD EVVGIMDKTQ DQKDFEDILF MEEHAFNGKG EKIENDHKNA NNESQELKLY
VSDNDTDSDL EEVQEVTHSN VKESGLNIVV NVNESLEADN DFFKDVFENT NLEKEEHKAI
EENLIQITEK KCISLNGESE EVIEETPPFI DVETKKCDED FEIQEHSNKN LILKGFEARN
TTLSKCVKTN ELDGVKLSDN DGIIEIKDEG QLPIPESLKS EIIEIYDSDD NKRSVAVTTP
TLKTPTKNCS ITDYFQVNYA IKRTPDEKQV EENATPHKVK SPFFVRKTPK TDRKNKSSSP
SPNSSKVSKN LFAEDADEKD RESLNEKEIL TEAAKVLQSE KTSEELQMLA DNFAQERKDL
ENERNRQERM GMSITQRMNS ECQQLLRLFG IPFIVAPMEA EAQCAFLDIV DLTQGTITDD
SDIWLFGGRT VYKNFFAQNK HVMEFRAEQI KQNFNCDRYK LIQLACLVGS DYTTGIHGIG
AVTALEILAQ FSSAKEICNE LKSNNPNNMQ LLLSTLQKFR DWWQSFKHHA APPGSSARFA
LQKKLKNIEL QDGFPNIKVI EAYITPTIDE SRETFTWGDP DIESIREFAR QTFGWTAEKI
NNILHPVLKK LKEKKTQTSI RNYLTIKNPL SVKQIKVSKR VQRAIEKMSG AAIESDDNSD
KRSKVKRPRN SKTSKAKKSA ASDSNNDVSE DKVVEQTEDT ARGPIKRAQK RKEVIPQREK
DLQQMEANKK LAIEIIKNTK NVPTKKRKS
//
