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Database: UniProt
Entry: F0XU78_GROCL
LinkDB: F0XU78_GROCL
Original site: F0XU78_GROCL 
ID   F0XU78_GROCL            Unreviewed;      1287 AA.
AC   F0XU78;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=DNA excision repair protein rad2 {ECO:0000313|EMBL:EFW98861.1};
GN   ORFNames=CMQ_4713 {ECO:0000313|EMBL:EFW98861.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFW98861.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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; GL630006; EFW98861.1; -; Genomic_DNA.
DR   RefSeq; XP_014168344.1; XM_014312869.1.
DR   STRING; 655863.F0XU78; -.
DR   GeneID; 25977955; -.
DR   eggNOG; KOG2520; Eukaryota.
DR   HOGENOM; CLU_003018_0_1_1; -.
DR   InParanoid; F0XU78; -.
DR   OrthoDB; 5479162at2759; -.
DR   Proteomes; UP000007796; 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; 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:UP000007796}.
FT   DOMAIN          1..98
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          915..984
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          120..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1152..1194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1211..1287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1260
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1261..1278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1287 AA;  141765 MW;  F11DE73D4E69232E CRC64;
     MGVNGLWQVL QPCARPTNLA TLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
     RVCKLLWFGI LPVFVFDGGA PALKRSTLQA RRQRREGRRE DAVRTAGKLL AVQMQRIAEE
     DAEKRRKRRR EAPSESAPSA VEASGEDGMV DGEMLPSMDK VVYAEEMHKP EQERLQARKF
     TKKDAYHLPE LDRPIEGMGR PEDPRIMNID ELEEYARQFH AGEDINLYDF SKIDFDGDFF
     KSLPPADRYY ILNAARIRSR LRMGLSKEQL DVMFPDRMAF SRFQIERVRE RNHLTQRLMI
     EAGMTGIDLT MGVNGRVAGE KDREYILVKN EGVEGGWALG VVSRDKEQGQ VHKPIDVDAL
     QFQYDGGKGE DSEDDVEFQD VPIEGLNRLP KLSVSQKDDQ TAGGHEADAE DESLFVSSYQ
     PVETLQPETM QEAVGDENLV ADEEEDLHKA IAMSLRNQHD ADASGGDIDE DEDETFEDVD
     IPAPEWTQKA AEVVSRPIVA TSGRMVAHIV NNRSNAAISA SKAQGSKDDD NSDSSDSELD
     IRAAMVAAAK KKKRTVEQGT SQAGSVQSAD PPKSRVKPLF DGPLPFEQLD WKTSIFEKKP
     NADAASSFAA LASASTVQDG KAAAAAAETG SLEADSDDDG LAGGFVIEAD EANSATGDVD
     DDMAGADRET GVKDDAPRPL PPWMADATDI RTAIRQQQAY DDGINAEDRE MALAEERTWQ
     RQQEPQIVEI GSSSDSGSDI EIIEAPRLAR ESETVEQLTR VAETNTAEDQ QEPTAVTDSI
     SEAVEMVEPA VTRLSSPEME FEDVELPDRP TVTKEVVAEA VTGIAPVDDD GLFTGEGEDE
     FDISDPEEEE LFAQMAEEAE EHARFASTLN HKTGRESQAV FEQEVKALRN QQKKDRRDAD
     EVTMVMVSEC QALLRLFGIP YITAPMEAEA QCSELVSLGL VDGIVTDDSD TFLFGGTRVY
     KNMFNGNKFV ECFLAADLEK EMSLSREKLI SLAQLLGSDY TDGLPGVGPV TAMEILSEFP
     GPQGLEEFRT WWDDVQMHGR SREADAGSPF RRKFRKSQGT KLFLPTGFPN AAVAAAYKKP
     EVDSSTEPFQ WGVPDLDGLR SFLMSTIGWS QDRTDEVLVP VIRDMNRREA EGTQSNITRF
     FSGAVGSGAR LTAAQQRAQA QAQAQMPDEF APRHAPRNKS SRGSSRRLAA AVSNLKAGTT
     SMEAAAAIMR SGPVVRAPSR KKTTAAGRKR KPEASPTVTG SGEPETSANE DDEDSAAELD
     NDKDEPAGRL SGRQQRATRR GEKRVKA
//
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