ID A0A0L1J618_ASPNO Unreviewed; 1138 AA.
AC A0A0L1J618;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Single-stranded DNA endonuclease {ECO:0000313|EMBL:KNG87120.1};
GN ORFNames=ANOM_004813 {ECO:0000313|EMBL:KNG87120.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG87120.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG87120.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG87120.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG87120.1}.
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DR EMBL; JNOM01000091; KNG87120.1; -; Genomic_DNA.
DR RefSeq; XP_015408043.1; XM_015550070.1.
DR AlphaFoldDB; A0A0L1J618; -.
DR STRING; 1509407.A0A0L1J618; -.
DR GeneID; 26806617; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000037505; 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; 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; 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; 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 Endonuclease {ECO:0000313|EMBL:KNG87120.1};
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:UP000037505}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 818..887
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 115..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 128340 MW; F1387765F3589746 CRC64;
MGVHGLWTVL QPCARPIKLE ALNKKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
RICKLLYFGI KPVFVFDGGA PILKRQTIAG RKKRREGRRE DAVRTAGKLL AVQLQRSAEE
EAARRRDGAP REQEEVPDNP VYVEDAGMTE KEKHQARSFR KKDAYHLPEL HVSLEEMGAP
NDPRIMSREE LEEYAKQFYR GEDINLYDFS KIDFDSPFFM SLPATDRYNI LNAARLRSRL
RMGYSKEQLE NMFPDRMAFS KFQIERVKER NDLTQRLMNI NGMNGEDAFY NSGQRIAGER
GKEYVLVKDN AVEGGWALGV VGNKDEGREH KPIDVDQYGK QEILPEKDED SEDDGGFEDV
PIEGLNRLPK LEFLREGIFD ASIRQQVQEN TERRATPGLP QSHEDDSLFV QEDGHERLHH
RERRAIDDIF EMDGENQDED LQKAIEMSLR PTSPLDQHDS DMPDISINRS SAPLAPLKET
IPSFSPDSDD DGLDFATALA QSKMAKKDPI SNNPFDGPLP FESIKLDKPF KTKKPQYEEL
DQHAGGFEKE PAKKTKAEQP LPPWFSGGSS TAEFIADTDA GANPLETHRD STSTITPDHV
FLKNHQTPKV IDVDMLPSTN EVVDLEANSE CKQPRATQTL DKTETPTKDT TTAFREIPPA
ATEATDISGR VSIAEAAHGP FTSHDIEPSR DEQADLLRTQ PSPSPEFEDV ELHPKEAITD
TVVPEMESQS HRVDELEGII GEDDGFSDPE DEELMRQLAA EGEEHVRFAA TLNSTSHTEN
TFDYEQELKQ LRYQQRKDRR DADEVSQIMI SECQQLLTLF GLPYITAPME AEAQCAELVA
LGLVDGIITD DSDIFLFGGT RVYKNMFNQG KFVECYLTSD LEKEYALHRR KLISFAHLLG
SDYTEGIPGI GPVTALEILT EFSSLEEFRD WWTQVQMGMN LSDGEHAAFY KKFRKQASKI
FLSPSFPNGQ VDVAYLEPEV DSDPSAFQWG VPDLHGLRNF LMATIGWSQE RTDEVLVPVI
RDMNRREQEG TQSNITAFFQ GPQGAGAFAP RVRSGGQSRM EKAFNRLRQE AGSETVRSKQ
STGAETNSVE HSESTGSSQP PQGEKSTGTK RSAQTKDSVS GDDVTGKKRR TRRTITKK
//
