ID E3QMS2_COLGM Unreviewed; 869 AA.
AC E3QMS2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=XPG-I domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GLRG_07304 {ECO:0000313|EMBL:EFQ32160.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG697360; EFQ32160.1; -; Genomic_DNA.
DR RefSeq; XP_008096180.1; XM_008097989.1.
DR AlphaFoldDB; E3QMS2; -.
DR STRING; 645133.E3QMS2; -.
DR EnsemblFungi; EFQ32160; EFQ32160; GLRG_07304.
DR GeneID; 24412669; -.
DR VEuPathDB; FungiDB:GLRG_07304; -.
DR eggNOG; KOG2520; Eukaryota.
DR HOGENOM; CLU_007575_0_0_1; -.
DR OrthoDB; 1779469at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0008821; F:crossover junction DNA endonuclease activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProt.
DR CDD; cd09906; H3TH_YEN1; 1.
DR CDD; cd09870; PIN_YEN1; 1.
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; IPR041177; GEN1_C.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR InterPro; IPR037316; Yen1_H3TH.
DR PANTHER; PTHR11081:SF71; ENDONUCLEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G13260)-RELATED; 1.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR Pfam; PF18380; GEN1_C; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT DOMAIN 40..135
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 142..219
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 508..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 95911 MW; D167FB2B728EDCB7 CRC64;
MLILIRRRNS PSTSFTKTCW LKFRRFTDLH NPRSYHAYRI YRELGPGQRI SLAKLATEQL
ENTGRPLRIA IDIAIWQFQT QAARGGTNPA IRTLFYRLLR LLSLGIQPIF VFDGPHKPAF
KRNKRSGRGD GVATAMAKRV IRLFGFPLHD APGEAEAECA LLQQRGIVDA VLSEDVDTIM
FGCTRTLRNW TAEGTRGAKT PTHVSLYDVD ELLSAGTGLD REGMVLVALM SGGDYIPEGV
PGCGVKLACE AAKAGFGKSL CRLKFDDDVE LEEWRANLRD ELRTNKSGFF RVRHKALSIP
DEFPSRHVLR HYTHPVVSCA TTVEKLEKEI IWSRPVDVQG LRYFVEETFD WVNRIGATKL
TRVLSPGLLV SKLLDRHMSS NTDSQTIEVT GQVKSDLIKR ITGRRNHHST DGIPELRVAH
IPADIVGLDL SQEADGVMTY DRQGLALNSD DEFVAVLDGD AEATNGRTRA KSTFDPTLVE
LIWLPESLVK LGAPLTIEDW EEKQRSKVLS RAPRKTTKTT KVNNMKFARG TPHEADALDK
WMQTTQTAAT TSGAKSRVRG LDGSDIGLSP LSQPTIRSPS SPDHPSSQLP THLQSSVNRS
KQSRSNGKAT AAAEPTGHRN PWASAGSQRM PRITKSQQST EPIVLSSSPM RPSPAAACSP
MNPLSSKHVV DLSSTDEAYV FAPSKPPKPT VPSLQQVALC KHQSIKTRPT KGSPALSSTP
PHGKLSMKQT RMDSFITRLS KLPVTESSQT QPRAWVGNGS QTCISASHIA VSSRLGHNRE
TSLTVSRDTQ TSATWNNHGD IFPLANKTDA SGQTRRMLVT RTSVGGFFKV VEMNDQEEDN
LKIMSPGRFT KSAWRQSEVS IIDLTVDDD
//
