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Database: UniProt
Entry: A0A135TWP4_9PEZI
LinkDB: A0A135TWP4_9PEZI
Original site: A0A135TWP4_9PEZI 
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
//
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