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Database: UniProt
Entry: C6HSC6_AJECH
LinkDB: C6HSC6_AJECH
Original site: C6HSC6_AJECH 
ID   C6HSC6_AJECH            Unreviewed;      1159 AA.
AC   C6HSC6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=DNA excision repair protein Rad2 {ECO:0000313|EMBL:EER36944.1};
GN   ORFNames=HCDG_09107 {ECO:0000313|EMBL:EER36944.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER36944.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) 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}.
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DR   EMBL; GG692437; EER36944.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HSC6; -.
DR   STRING; 544712.C6HSC6; -.
DR   VEuPathDB; FungiDB:HCDG_09107; -.
DR   eggNOG; KOG2520; Eukaryota.
DR   HOGENOM; CLU_003018_0_0_1; -.
DR   OMA; PNSMDFS; -.
DR   Proteomes; UP000002624; 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; 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   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:UP000002624}.
FT   DOMAIN          1..98
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          836..905
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          579..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          792..819
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        590..604
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1159 AA;  131747 MW;  A614F218C45BF8D9 CRC64;
     MGVTGLWTVV KPCARPIKIE TLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNAHIVGFFQ
     RICKLLYFGI KPVFVFDGGA PTLKRQTIMS RKQRREGKRE NAARTAGKIL AVQIQRKAEE
     EIETQRRMRA NSLEPEEPLP DHFVYVDELN MTPEERQKNR QFRKQDAYHL PELDVSLAEM
     GAPNDPRIMS HEELEEYARQ FHSGEDISLY DFSKIDFNSP FFVNLPPSDR YNILNAARLR
     SRLRMGYSKE QLDNMFPDRM AFSRFQIERV KERNDLTQRL MHLSGMTDDD SLYEIGSNSR
     IAGERGKEYV LVKNSGVEGG WALGVLGNKD EGQRNKPIDV EEYGEHLLSD DHNALENEDE
     DFEDVPIEGL NRMPKLPVFD RGVFDKKFGE HSRKVTDHRT KEVVDKSLDQ TNSGKYTLFV
     PEEPSRSTVD HDTLHKYSRF QDTSDNDDLL RAIQMSLETG NDQAVLQLDV SSSSDKNQEI
     SKVAIGEEDV SDIADDEDMN FFAALSKSKA MNIKPNAPIS NPFDGPLPFE PLKIRKPTSW
     DKVIDVTGPS EEPTSNGQRI PQALPPWFDV KLTEKTLLNQ DPGNEVDGVD PTSDARRCDN
     TPKEGEMINF DVGVARGIEI NELETAGRDN QAHRVPIQSN ASNCRTCHPP VSSREPLANT
     FSSTQEHTEP EGTAEQEADN RGSVENNGEA YEWETTYHKD VQNEKSNSKM KTQEAILPPS
     PDFEDAKIYC PSEALQTSPH MYNSSDDTSR HNNFTHYDHD SDDFSDPEDD ELIHQLQKEA
     EEHARFASTL NSKSQAENAF NYEQELKQLR SQQKKARRDA DEVSHIMVSE CQELLRLFGL
     PYITAPMEAE AQCAELLSLG LVDGVVTDDS DIFLFGGTRV YKNMFNQAKF VECYISNDLE
     KEYNLDRNKL IQFAHLLGSD YTEGIPGVGP VSALEILTEF PTLEDFRDWW SQVQMGAKLP
     EDSHSIFRKK FKKNVTKLFL PPGFPDKRVD TAYLEPKVDS DPSAFQWGVP DLNALRQFLM
     STIGWSQERT DEVLVPVIRD MNRREQEGTQ SNITNFFQGP QGAGAFAPHR RPDGKSRMQK
     AFSRLRHQAQ MKQRGSGPVP DEDKAPNPSG SKHSTNRKSG KRSPDNGYPT SNDREITGDN
     KSDTAHKTSK KQKTTKRQR
//
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