ID L5KUR0_PTEAL Unreviewed; 1074 AA.
AC L5KUR0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=DNA repair protein complementing XP-G cell {ECO:0000313|EMBL:ELK14910.1};
GN ORFNames=PAL_GLEAN10013741 {ECO:0000313|EMBL:ELK14910.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK14910.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB030555; ELK14910.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KUR0; -.
DR STRING; 9402.L5KUR0; -.
DR eggNOG; KOG2520; Eukaryota.
DR InParanoid; L5KUR0; -.
DR Proteomes; UP000010552; 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; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
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 SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 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:UP000010552}.
FT DOMAIN 669..738
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 185..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1049
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1074
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 120496 MW; C4FEAE5588C549BC CRC64;
MGVQGLWKLL ECSGRQISPE TLEGKILAVD ILNASSEEED EKEWQERMNQ KQALQEELFQ
NPRAVDIESE DFCSLPPEVK HEILTDMKEF TKRRRTLFEA MPEESNDFSQ YQLKGLLKKN
YLNQHIENVQ KEMNQQHSGQ IQRQYEDEGG FLKEVESRRV VSEDTSHYIL IKGIQAEKIA
EVDSESFPSS SKMHSMSFDT KSSPCEKLKP EKESGATPPS PRTFLAMEAA MLPSSEEELE
SETQRQYNKR NASATVDGGS ISPLTLLAIQ KALDDDEDVK VHVGNDVQMG GSGAKKLLVN
SSDEEADEGL KKRDEKGMLL TTMPDSASVN FVEECVTSTN NKKELADSAP SSSTVICQGS
ESNVPKEQMS FIHMVNEGFQ TSDEPAVSDR KDPFPLEKTV VIHRNASGLQ SERGLTSTPL
TSPNAVSGNE IYTKVLELQQ DLCPSENKYN SSLSSDDETE CEKYSASEVT GTVSLQEASN
TLSVPSEATS NLENAVSFNG KECENFLKTI QERETMKSAG QDCISIPKFM EPTEISEESE
SDGSFIEVHS IISDDEPQAN LAEDFKPPSG QDEEELIGTK KEEATGDSEG LLRDNSESEA
LNIEPQEETE ENADSSFNEW QDINLEELET LESNLLVQQN SLKAQKQQQE RIAATVTGQM
FLESQELLRL FGIPYIEAPM EAEAQCAILD LTDQTSGTIT DDSDIWLFGA RHVYKNFFSK
NKFVEYYQYV DFHNQLGLDR NKLINLAYLL GSDYTEGIPT VGCVTAMEIL NEFPGHGLEP
LLKFSEWWHE AQKNKKIRPN PYDTKVKKKL RKLHLSPGFP NPAIADAYLK PVVDDSKGSF
LWGKPDLDKI SIFCQRYFGW NRTKTDESLF PVLKQLNTQQ TQLRIDSFFR LAQQEKQDAK
GIKSQRLNRA VTCMLRKERE ETTSEVEAVS VAMEKEFEFP DKAKGKTQKR SIANKWKESS
SLKRTRLSDS KRESKCGGFL GEASQSSDAS SSEDTDCLPL MNMQQRKAAG EAKFSSSDLQ
NTVKPDPVKD EGLTLSSSSD DDREKTKPVL VTARSVFGKK KGKRTIRGRK KKLI
//
