ID A0A135TWP4_9PEZI Unreviewed; 1273 AA.
AC A0A135TWP4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=DNA excision repair protein {ECO:0000313|EMBL:KXH52568.1};
GN ORFNames=CSIM01_09149 {ECO:0000313|EMBL:KXH52568.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH52568.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH52568.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH52568.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-2014) 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:KXH52568.1}.
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DR EMBL; JFBX01000040; KXH52568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TWP4; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000070328; 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 942..1011
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 120..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 883..925
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 517..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 142596 MW; 0D9CB3007F7DCE5F CRC64;
MGVNGLWTVV QPCARPTNLA TLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
RICKLLWFGI KPVFVFDGGA PVLKRQTIQG RKQRREGRRE DAVRTAGKLL AVQMQRIAEE
EEDKRKRDAD RGIQREREEP QEAIPDMEQI VYVDEVGMSQ QERQKTRKFF KQDAYHLPEM
DGDIASMAKA DDPRIMSIEE LEEYARQFHN GEDINLYDFS KIDFDGEFFR SLPAADRYNI
LNAARLRSRL RMGLSKEQLD EMFPNRMDFS RFQIERVRER NNLTQRLMKE AGMTGLDLTL
NGGGRIAGEK DREYILVKND GAEGGWALGV VSKEKDLGEA HKPIDVDALD FQFQAKEKAE
ASEEEDDFED VPVEGLNRLP KMSSSAAAQA SRQAAIQRQQ LYGNRGSSEV NDLFEEEEES
LFVDGDLPEP HVRNVARQRG DEPMHPEEED DINRAIAMSL QNQHGEAAEK SEEDEQFEDV
ELEAPEWKQK AVEAPKPIAA RSGRMVAHIV NNRSNAAVPK KRANSASSSD GEMDLQAALK
ASRQKKRVLP KPAVPNVKNP FDGPLPFPKL AWGPSLFSMK AQSKKPEAVA PKQLAQSSQE
PARQYGDDEF GGGFLAEGAE ERPADDEDDE GGFERGLEED RPKPLPPWMV DDTDIRESIK
QQRQVESEIN TEDREAAQEE ERRFERQRQN QLIEIQSSDD EDDDVEILDA PPPPKHAASQ
EEITFLDEPN AADDVTNAEV EAEKGENETV ALPEKADVSR KSSESPEVEF EGIQPEEVDE
DMEVTITAIP DSPEPEMEDV AEPQGPDSPP DPIMEDVTIT AEEPKPVEEE EHELTFEELM
DGPTLDDPNT AGDPVQDVEA AVFAESDDEF SDPEDEELFA NLAQEAEEHA RFASELNNKS
EQENKEAYEK ELKALRTQQK KDRRDADEVT QVMVTECQAL LRLFGIPYIT APMEAEAQCA
ELVRLGLVDG IVTDDSDCFL FGGTRIYKNM FNSNKFVECY LGSDLEKELS LSRDQLIAIA
QLLGSDYTEG LPGVGPVTAV EILSEFPGKD GLAQFKEWWA DVQLNNRPKE ADAGSPFRRK
FRKSQGTKLF LPAGFPNPAV TDAYIRPEVD DSPEHFQWGV PDLEGLRQFL MATIGWSKER
TDEVLVPVIR DMNKRDIEGT QTNITRYFEG AVGVGARDTF APRQKGTTSK RMANAVSRLR
ANANGEQEGG ASATAAPDDT AAPTRATGKR KARSRTAAAE DEDEFVDDEG EEENGQGGRS
GRARRGKKAK ASA
//