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Database: UniProt
Entry: G3IDW5_CRIGR
LinkDB: G3IDW5_CRIGR
Original site: G3IDW5_CRIGR 
ID   G3IDW5_CRIGR            Unreviewed;      1028 AA.
AC   G3IDW5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=DNA repair protein complementing XP-G cells-like {ECO:0000313|EMBL:EGW00239.1};
GN   ORFNames=I79_021903 {ECO:0000313|EMBL:EGW00239.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW00239.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JH002108; EGW00239.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3IDW5; -.
DR   STRING; 10029.G3IDW5; -.
DR   PaxDb; 10029-XP_007627078-1; -.
DR   eggNOG; KOG2520; Eukaryota.
DR   InParanoid; G3IDW5; -.
DR   Proteomes; UP000001075; 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: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   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   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   4: Predicted;
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:ARBA00022759};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT   DOMAIN          624..693
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          137..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..911
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..960
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1028 AA;  114925 MW;  98CAE9812136C995 CRC64;
     MDQKQALQEE FFHNPQAIDI ESEDFSSLPP EVKHEILTDM KEFTKRRRTL FEAMPEESND
     FSQYQLKGLL KKNYLNQHIE NVQKEMNQQH SGQIQRQYED EGGFLKEVES RRVVSEDTSH
     YILIKGIQTK KVMDVDSEAS SSSKMHSMSF GLKSSPHKTV KPEKEPEAAP PSPRTLLAIQ
     AAMLGSSSEE EPESGEGRQS RERNLWATAD AGSISPQTLA AIQRALDDDE DGKVCDRGDE
     PTGRTLMAVL GDDKDEKVCG RDDELAVRTL LGNVPDQEHS DEVVVRDGGM PFASVPPLPT
     MTLVKEGVVS SSSEKEETAS AHSLSTACHQ ASERYAPKEQ MPRIHVVVEA SQISSECEVE
     SQQAPLPSAC TELPCSDASR LPSERKLTLV PPTRTHSDQK IDTHSEESGL YPPENKCVSS
     CFSSDETESG QNPASKAWST VHVPSEAKGN LEKADEHGDS LRTIQQLEMP EAAARELTLV
     PKPMGPMGME SEESESDGSF IDVQSVISDG ELETDSSEAS KPPSEQDEEE PRGTLVEDTP
     RDTEHLRQDN FDSEDLANEE HNKADRDAKG SPDEWLDINL EELDSLESNL LAEQNSLEAQ
     KQQQERIAAS VTGQMFLESQ ELLRLFGIPY IQAPMEAEAQ CAILDLTDQT SGTITDDSDI
     WLFGARHVYK NFFNKNKFVE YYQYVDFHNQ LGLDRNKLIN LAYLLGSDYT EGIPTVGCVT
     AMEILNEFPG RGLDPLLKFS EWWHEAQTSK KVAANPHDTK VKKKLRKLQL TPGFPNPAVA
     DAYLRPVVDD SRGSFLWGKP DVDKIREFCQ RYFGWNKTKT DESLFPVLKQ LNVQQTQLRI
     DSFFKLAQQE KQDAKHIKSQ RLNRAVTCML RKEREEAASE LEKETEALDE AKGKTQKRSL
     MSPRETSVPK RRRASGSGGF LGDSHLSESP RDSSEDAESS SVVCTPRGRT AESSTVSCSD
     LPDVVRDAHR RDGYMSTSSS GEDDGDKAKA VLVTARPVFG KKKGKLMRRR KRKDQFNKVI
     NLEEQCLQ
//
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