ID W6QAH8_PENRF Unreviewed; 1126 AA.
AC W6QAH8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=DNA repair protein (XPGC)/yeast Rad {ECO:0000313|EMBL:CDM33420.1};
GN ORFNames=PROQFM164_S03g000144 {ECO:0000313|EMBL:CDM33420.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM33420.1};
RN [1] {ECO:0000313|EMBL:CDM33420.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM33420.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792017; CDM33420.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QAH8; -.
DR STRING; 1365484.W6QAH8; -.
DR OMA; PNSMDFS; -.
DR OrthoDB; 5479162at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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; IPR003903; UIM_dom.
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; PF02809; UIM; 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 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 821..890
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 471..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1126 AA; 127604 MW; F82BA594B4BA443A CRC64;
MGVTGLWTVV QPCARPIKLE TLNKKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHIVGFFR
RICKLLYFGI RPVFVFDGGA PVMKRQTIAG RKKKREGHRE DAARTAGKLL AVQMQRSAEE
ENARRRNKTH IQEEEEVPDA PVYAEEAFMT ETEKQQNRRF KKKDAYHLPN LGVSLQDMGA
PNDPRIMSQE ELEEYARHFH QGQDINLYDF SKIDFDSLFF LSLPATDRYN ILNAARLRSR
LRMGYSKEQL DTMFPDRMAF SRFQIERVAE RNDLTQRLMN INGMNGDEAF YNSGKRVAGE
RGREYVLVKD SEHEGGWVLG VVGNREGHEE KPIDLDRPEI LSDEDEVSDE DEFEDVPIEG
LNRLPKLPFL QEGVLDRSLQ LQTNEVLDMR RAIQESRHAA QQQSVNDRRV QEVEDDSLFV
EAEGNIAAQQ QNNDTDEFFN GDGDDDDLER AIALSLQPDK VDDEDMPDMP INRPVESAPP
YETVPDLDSE SDDGMDFAAA IARTKVSKKA SHAPTRFGGP LPFESIKLTK VTKDNDKAGE
VGENAGGFLK GPTEKPKQPD PLPPWFVGER SDVGFIVDPI EDPEKDDERS AVPDHMFLSN
RRSPDIIDVD EISATTEVVD LEKREEEEAE EEKENSKQIF QMEDIEKIYN ELPTNLHEKP
LSEPAPAQVN RNLDETALGR PETQIQDQVP AVEELSSRSE KSPSPEFEDV VPQLPTQGPE
ITVVSHQKAQ PQPQFFEEVE DFVQDQADYS DPEDEELFKQ LAAEGEEHVR FANTLNSAAP
SQEAFDYEQE LKQLRSQQRN ERRDADEVTT IMINECQQLL TLFGLPYITA PMEAEAQCAK
LVSLGLVDGI VTDDSDIFLF GGTRVYKNMF NQSKFVECYL TSDLEKEYAL HRRKLISFAH
LLGSDYTEGI PGIGPVTALE ILTEFSSLEE FREWWTELQM GTNNAEDAHL AFRKKFRKKA
SKIFLPPSFP DAKVDEAYLE PAVDDDPSQF QWGVPDLNAL RTFLMTTIGW SQERTDEVLV
PVIRDMNRRE QEGTQSNITH FMQGPQGAGA FAPRVRTGGP SRMEKAFSRL RQEAQTGETS
RDGEPANKDG EKEAPISQSK GKRGGSTTKG KAGTNKKRKT RHATSD
//
