ID A0A091RSQ4_9GRUI Unreviewed; 1139 AA.
AC A0A091RSQ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=DNA repair protein complementing XP-G cells {ECO:0000313|EMBL:KFQ31507.1};
DE Flags: Fragment;
GN ORFNames=N332_06154 {ECO:0000313|EMBL:KFQ31507.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ31507.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ31507.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ31507.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK805062; KFQ31507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RSQ4; -.
DR Proteomes; UP000053369; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 733..802
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 476..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1139
FT /evidence="ECO:0000313|EMBL:KFQ31507.1"
SQ SEQUENCE 1139 AA; 128940 MW; 5DF81F11C71730F8 CRC64;
MGVQGLWKLL ECAGRPINPE TLEGKILAVD ISIWLNQAIK GARDRGGSSV RNAHLLTLFH
RLCKLLFFRI RPVFVFDGEA PLLKRQTLAK RRQRKEIAVS DSKKTTEKLL KTFLKRQIIK
TALTGKRNEA LPSITQVRRE GIDDMYVLPP LEDEEKNSSE EEDEKEWEAR MNHKKMLQEE
LCENPNSVDI ESEEFNQLPP EIKHEILTDL KEFTKRKRTL FEAMPEESND FSQYQLRGLL
KKSSLNRCIE NVQKELNQQH SGEIQTQYEN EGGFVKEVES RRVVSEDTSH YILIKGIQAK
EAVTGDKETT AGPSSKILEF IKSNKINESP ANAKLVASDK LQTEKVDNVV TAPPSPRTLL
AIQAAIVESS SEEELGDEDK GQLNVVQSVR EEGSVSPRTL RAIQQALSDD GKREEVVTFR
TDEVLPERRE VKGFLLSSSV EEDQIPEVNE GKKIPTSTIN SSNQVVMQDA EFEQKSQELE
KDITPKDTSI SRAENYSCID STGKDKEDVD KEENSSKMDL NSLGDKDINL GIQKPSRSPV
QTSIGALIHA EMTSLSKNEK NLKNSENTEE VISQTEENVS DVQKDTKPFP EAKGQEEERK
GILQSEDSDS DGSFIEVNAE SSSEAEFSTE YDEKLDDETA LPEMQTERHD AVTQDLLKES
DEVQLANDQN VEREGDDKDA VDEWQNISLE ELEGLENDLS AEQNMLQAQK QQQERVAASV
TGQMFLESQE LLRLFGIPYI EAPMEAEAQC AILDLTDQTS GTITDDSDVW LFGARHVYKN
FFSQNKYVEY YQYVDFQNQL GLDRSKLINL AYLLGSDYTE GIPNVGFVTA MEILNEFPGH
GLDPLLKFAA WWTEAQKNKK LRPNPHDTKV KKKLRELQLS SGFPNPAVAE AYLKPVVDET
RGSFVWGKPD VEQIREYPFT ASLTFHTFCQ DHFGWTRTKI DEILLPVIKQ LNLQQTQLRI
DSFFRLEQHE KQAIKSQRLR RAVTCLKRKE KEEADEIREA TAAMKIELKQ HKEKKGQSTV
GCANRQAVVA TEVQSGKRRK HSDSREECLY GGGFLGNLNL SEASSDSSVE ELEGRGLGKS
KRRKNVSAVE TADHKEKKGC SSSSDEDEEL GNVVMVTAKP VFEGRKKKSW SMRGRKKKR
//
