ID A0A3M9Y5H9_9PEZI Unreviewed; 1223 AA.
AC A0A3M9Y5H9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=DNA repair protein rad2 {ECO:0000313|EMBL:RNJ55036.1};
GN Name=RAD2 {ECO:0000313|EMBL:RNJ55036.1};
GN ORFNames=D7B24_009054 {ECO:0000313|EMBL:RNJ55036.1};
OS Verticillium nonalfalfae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ55036.1, ECO:0000313|Proteomes:UP000267145};
RN [1] {ECO:0000313|EMBL:RNJ55036.1, ECO:0000313|Proteomes:UP000267145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ55036.1,
RC ECO:0000313|Proteomes:UP000267145};
RA Stajich J.E., Kasson M.T.;
RT "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL Submitted (OCT-2018) 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:RNJ55036.1}.
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DR EMBL; RBVV01000087; RNJ55036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9Y5H9; -.
DR STRING; 1051616.A0A3M9Y5H9; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000267145; 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: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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 896..965
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 469..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 614..641
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 852..879
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 472..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 136097 MW; E6C18739F8D2650B CRC64;
MGVNGLWTVL QPCARPTNLA TLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
RICKLLWFGI RPVFVFDGGA PALKRQTIQG RKRRREGRRD DAVRTAGKLL AVQMQRIAEE
QDEKRKRELE RGVDERARQA EMAEEEAVPN ADQLVYVGEV GMSQQERQQT RTFRKQDQYH
LPKLDGDISS MARADDPRIM SVEELEEYAR QFNNGEDLNL YDCSKIDFNG EFFKSLPPPD
RYNILNAARL RSRLRMGLSK EQLEEMFPNR MDFSRFQIER VKERNNLTQL LMKEVGMTGL
DLTINGGGRI AGERDREYIL VKNDGVEGGW ALGVVSKEKD IGEAHKPIDI DALEFKYQQK
DEEPEMEEEE EFEDVPVQGL NRLPKLSHGT EGQPMDEEDS LFVGGDTALK LSTKSQEQKS
EDLHPEEEDD INQAIALSLR SQHVANSDTP EVEDVFEDVE LAVPQWEQKA VPQNKPIASS
SGRMVAHIVN NRASAAVPKR RQSNASSSDS DNDLQAALAA SRKNRKAQPK AVPGNIKNPF
GGPLPFPKLD IGSIFPGRSR PSNPTASERP SSRRSGGDEP LMGDLDDMAG GFEPEPDPNA
PKPLPPWMTD NTDIRDTMLK AKEVEQEINA EDREAAAEEE MMFQRKRQNE TIEIASSDDG
SDVEVLEVAP APKKMASPAE ISSTQSSLAQ ESSEKAEVTE TQTVPGGNSS GAPSADEANE
PVPTITLGGV AISSKSSVSP EPEFEDIEIP EQEDEHDITV RELSNTPEPV VPVADISTAD
KEPDTTGVAH QADFEEALAQ TAQPADENAE DNYNPFGDSD VDEYSDPEDE ELFASLAQEA
DEHARFASEL NHKSEQENRE AYERELKALR TQQKKDRRDA DEVTQVMVGE CQALLRLFGI
PYITAPMEAE AQCAELVRLG LVDGIVTDDS DTFLFGGTRV YKNMFNSNKL VECYLSSDLD
KELSLSREQL VSIALLLGSD YTDGLPGVGP VTAVEILSEF PESEGGLAAF CDWWADVQGQ
RRPKEDDAPN AFRRKFRKSQ AAKLFLPVGF PNPAVREAYM KPEVDDSPET FQWGVPNLEG
LRQYLMATIG WSEERTDEVL VPVIRDMNRR DVEGTQSNIT RYFEGGVGTG AKESFAPRQK
QKASKRMAEA VNKLRNTGAS VSESSPTTDT PTTSSGSKRK RTVRAATRNS LVDEEPETGE
DDDEAEAAVP RTRGRGKRTR ADR
//