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Database: UniProt
Entry: D2H095_AILME
LinkDB: D2H095_AILME
Original site: D2H095_AILME 
ID   D2H095_AILME            Unreviewed;      1192 AA.
AC   D2H095;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=DNA repair protein complementing XP-G cells {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=PANDA_002828 {ECO:0000313|EMBL:EFB25962.1};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB25962.1};
RN   [1] {ECO:0000313|EMBL:EFB25962.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
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; GL192404; EFB25962.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2H095; -.
DR   InParanoid; D2H095; -.
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   NCBIfam; TIGR00600; rad2; 1.
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}.
FT   DOMAIN          1..98
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          785..854
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          146..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..732
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1088
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1145..1160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1176..1192
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1192
FT                   /evidence="ECO:0000313|EMBL:EFB25962.1"
SQ   SEQUENCE   1192 AA;  132634 MW;  45179E77BBCC00EA CRC64;
     MGVHGLWKLL ECSGRQVNPE TLEGKILAVD ISIWLNQALR GVRDCHGNSI ENAHLLTLFH
     RLCKLLFFRI RPIFVFDGDA PLLKKQTLAK RRHRKDLATT DSRKTTEKLL KTFLKRQAIK
     TALKSKRQDE DLPSLTQVQR EDDIYVLPPL QKEEKNSSEE EDEREWQERM SQKQALQEEF
     FHNPHAIDIE SEDFSSLPLE IKHEILTDMK EFTKRRRTLF EAMPEESNDF SQYQLKGLLK
     KNLLNQHIEN VQKEMNQQQS GQIQRQYEDE GGFLKEVESR RVVSEDTSHY ILIRGIQAKK
     VAEVGSEALP SSSDMHSRSF DTKSSPCENL KPEKEAAAAP PSPRTSLAVQ AAMRGSSSEE
     EWESENQKQS DVKNAPVSPR TLLAIQKVLD DDEDMEAHAG NDAQTGGSGV ETLVENSCHE
     EAAEGLEEGD GEGMLLPAGP HLTRVDCAHE PSPDSSRRLA DSALLSRPVF CPGSESSVPK
     EEMSLTHVVS EAFQTSDESS VKGGKDPVPP ESTVVMRSDA PGPQGGRQLT PGPPVSLSSV
     PRNETHTKEP GLQPDLCPSG SKCDSSVLSS DDETECEKNP VSEIVATVSL QEMSNTQNVP
     SEAISNLENA GSFHSEEHDN FLKTIQEHET VVSADQDLIS VLKSVEPVEM DSEESESDGS
     FIEVQSIISN DELQAELHEA SESPSRQDEE EPIGTRKEEA TGDSEGLLTH DSGSEALDTE
     PHEEAEKDAD SSLNEWQDIN LEELETLENS LLAQQNSLKA QKQQQERIAA TVTGQMFLES
     QELLRLFGIP YIEAPMEAEA QCAILDLTDQ TSGTITDDSD IWLFGARHVY KNFFNKNKFV
     EYYQYVDFHN QLGLDRNKLI NLAYLLGSDY TEGIPTVGCV TAMEILNEFP GHGLEPLLKF
     SEWWHEAQKN KKIRPNPYDT KVKKKLRKLQ LTPGFPNPAV ADAYLKPVVD DSRGSFLWGK
     PDLDKIREFC QRYFGWNRTK TDESLFPVLK QLNAQQTQLR IDSFFRLAQQ ERQDAKGIRS
     QRLNRAVTCM LRKEREAAAS EIEAMSVAME NDFEFPDKAK GKTQKRSIAN KWEESSSLKR
     KRLSDSKQES KCGGFLGGAC PSPSSGTSSG EDAECVSSVN VQRGRAAPES PASRPGLQSA
     ASPAPARDQG ATTSSSSDDD GGGPAPVLVT ARSVFGRRKG KGRGTRGRKR KS
//
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