ID A0A1Q8RJ67_9PEZI Unreviewed; 1240 AA.
AC A0A1Q8RJ67;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=DNA repair protein rad13 {ECO:0000313|EMBL:OLN84374.1};
GN ORFNames=CCHL11_05940 {ECO:0000313|EMBL:OLN84374.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN84374.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN84374.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN84374.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) 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:OLN84374.1}.
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DR EMBL; MPGH01000192; OLN84374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RJ67; -.
DR STRING; 708187.A0A1Q8RJ67; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000186583; 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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186583}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 919..988
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 120..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 860..902
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 120..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 139094 MW; 9CA385611FF9A5E9 CRC64;
MGVNGLWTVV QPCARPTNLA TLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
RICKLLWFGI KPVFVFDGGA PALKRQTIQG RKQRREGRRE DAVRTAGKLL AVQMQRIAEE
EEQKRKRDSE RGINREREEP QEEIPDTNNI VYAEEVGMSQ QERQRSRKFF KQDAYHLPEL
DGDIASMAKA DDPRIMSIEQ LEEYARHFHN GEDINLYDFS KIDFDGEFFK SLPPPDRYNI
LNAARLRSRL RMGLSKEQLD EMFPDRMAFS RFQIERVQER NNLTQRLMKE AGMTGLDLTL
TGGGRIAGER DREYILVKNE GAEGGWALGV VSKEKDLGDA HKPIDVDALD FQFQQKQKAE
VSDEDEFEDV PVEGLNRLPK MTSATASHES RNAAARRRQL YITRRGDAPI ETDEDTLFVG
GDLPEGLQDS RTYRQPEEML HPEEEDDINV AIAMSLQNQH GKGAGNSDEE EDFEDVDMPA
PEWKQKAVEA PRPFVAGSGR MVAHIVNNRS TAAVPRRRAS SASSSDDDLQ AALKASRLKK
KSQPKPAVPN VKNPFDGPLP FPKLDWGASL FSKKAQPPKK LDEAASSKQT TESSKETVHN
GPDTDLEGGF LTENIGEELA NGNNHEGVFR NEPQDEGPKP LPPWMVDDTD IRDSLKKQRQ
VESEINTEDR EAALEEERRF ERLRQNQLIE IQSSDDEDSD VEILENAPPP KGISPQREPA
SAHEEPQTDV ASDTHTDAPK ESIDATLERA DAESRISSPQ TEPDFEDVQL ANGDEDMQIT
VTELPDSPEP ELEDVEVTTG QPNPVGDEPE LTFEELMNGP ELDDPNTAGD PIQDAEAQVF
ADSDDEFSDP EDEELFANLA QEAEEHARFA SELNNKSERE NREAYEKELK ALRTQQKKDR
RDADEVTQVM VTECQALLRL FGIPYITAPM EAEAQCAELV RLGLVDGIVT DDSDIFLFGG
TRIYKNMFNS NKFVECYLSS DLEKELSLSR DQLIAIAQLL GSDYTEGLPG VGPVTAVEIL
SEFPGKNGLE RFKEWWQDVQ LNNRPKEADA ASPFRRKFRK AQSTKLFLPV AFPSTAVAEA
YNRPEVDSSP EQFQWGVPDL EGLRQFLMAT IGWSKERTDE VLVPVIRDMN KRDMEGTQAN
ITRYFEGSVG VGARDAFAPK QRGTTSKRMA EAVSRLRANA NGESAPAVEE DAAAPSSATG
KRKARSSSMA EVGDGDDAED EQVEDARKTR IRRGKKAKAS
//
