ID A1DMF1_NEOFI Unreviewed; 1132 AA.
AC A1DMF1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=DNA excision repair protein Rad2 {ECO:0000313|EMBL:EAW15972.1};
GN ORFNames=NFIA_053180 {ECO:0000313|EMBL:EAW15972.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW15972.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW15972.1; -; Genomic_DNA.
DR RefSeq; XP_001257869.1; XM_001257868.1.
DR AlphaFoldDB; A1DMF1; -.
DR STRING; 331117.A1DMF1; -.
DR EnsemblFungi; EAW15972; EAW15972; NFIA_053180.
DR GeneID; 4584384; -.
DR KEGG; nfi:NFIA_053180; -.
DR VEuPathDB; FungiDB:NFIA_053180; -.
DR eggNOG; KOG2520; Eukaryota.
DR HOGENOM; CLU_003018_0_0_1; -.
DR OMA; PNSMDFS; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IEA:EnsemblFungi.
DR CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 6.10.140.100; -; 1.
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; 2.
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; SM00726; UIM; 2.
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; PS50330; UIM; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 810..879
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 117..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 127770 MW; BE6E7C81478578EA CRC64;
MGVTGLWTVV QPCARPIKLE TLNKKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHIVGFFR
RICKLLYFGI KPVFVFDGGA PALKRQTIAG RKKRREGRRE DAVRTAGKLL AVQMQRSAEE
EAARQKTGTS RQDEEEVPDN PVYVEETYLT EKEKRQSRAF RKKDAYHLPD LHVSLEEMGA
PNDPRIMSRA ELEEYARQFH QGEDINLYDF SKIDFDSPFF ISLPATDRYN ILNAARLRSR
LRMGYSKEQL DNMFPDRMAF SKFQIERVKE RNDLTQRLMN LNGMNGEEAF YNSGQRIAGE
RGREYVLVKD NAVEGGWVLG VVGNKGEGHA DRPIDVDRYG QRDVIYDHEE ASDGDDGAFE
DVPIEGLNRL PKLNFPQKDA FDESIEKQMT GVSRRRDSLF QETQDNSLFV QDGDLEDALP
HQRRHIDDVP GGTVDSEDED LQRAIAMSLE PSASRVEDMP DIPLNRNDVP AAPPKETSPG
LAESDDDEMD FAAALAQSRR TKRKPSSSVP RPVMDHPFEG PLPFESIRLK PSKAEKPPYE
ELDEEAGGFE KESAKKEESL PLPPWFSGEQ LNEEFVVDKI DNTSLEAYRD RAMTPDHLFL
KEHRSPDVID VDKMPGPEEV IDLEAEPKTE KLDTAVPSST ENAQIQLDDV AVPTISDKDK
AVEEVTYERK ATDGETPSTE KTETKNVAHD SPSPEPEFED VTIRTEAKPT EVTVTGNEPQ
TFAESDQAHV VVEDDEDFSD PEDEELMRQL AAEGEEHVRF AATLNNNVQQ SSTFDYEQEL
RQLRSQQKKD RRDADEVTQV MITECQQLLS LFGLPYITAP MEAEAQCAEL VSLGLVDGII
TDDSDIFLFG GTRVYKNMFN QGKFVECYLT SDMEKEYALH RRKLISLAHL LGSDYTEGIS
GIGPVTALEI LTEFSSLQEF RDWWTQIQTG MYVPETHAAF YRKFKKTATK IFIPPTFPDP
QVDKAYLEPV VDSDPSPFQW GVPDLHGLRN FLMTTIGWSQ ERTDEVLLPV IRDMNRREQE
GTQSNITNFF SGPQGAGAFA PRVRSAGQSR MEKAFSRLRQ EAGAKTHQST STGETDTGAD
GSTDDQTTSR NSQKKAKGRK RAQAKDTITS SADADGVSMT PKKQKTRRST NN
//
