ID A7EV70_SCLS1 Unreviewed; 1188 AA.
AC A7EV70;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=PIN domain-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_09228 {ECO:0000313|EMBL:EDN93362.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN93362.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476633; EDN93362.1; -; Genomic_DNA.
DR RefSeq; XP_001589507.1; XM_001589457.1.
DR AlphaFoldDB; A7EV70; -.
DR STRING; 665079.A7EV70; -.
DR EnsemblFungi; EDN93362; EDN93362; SS1G_09228.
DR GeneID; 5485779; -.
DR KEGG; ssl:SS1G_09228; -.
DR eggNOG; KOG2520; Eukaryota.
DR HOGENOM; CLU_003018_0_0_1; -.
DR InParanoid; A7EV70; -.
DR OMA; PNSMDFS; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IEA:EnsemblFungi.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
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; SM00726; UIM; 2.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 897..966
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 113..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 853..880
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 113..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 133725 MW; C01495F83D4A97E6 CRC64;
MGVTGLWTIV QPCARPTPLP ALNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHIVGFFR
RICKLLFHGI KPVFVFDGGA PILKRQTVLG RKRRREGRRE DAVRTAGRLL GVQMKRRAEE
EDSERKKRER EGRNKPTVEE EEVVPEEQLA YVDEIGMSAQ ERQTSRKFYK KDAYHLPELT
NGIEGMGRPE DPRIMSAEEL EEYARQFHSG EDVNLYDFSK IDFNGEFFMS LPAVDRYNIL
NAARLRSRLR MGLSKEQLEE MFPDRMAFSR FQIERVRERN ELTQRLMNLN GMNSEEHMFG
VNGTNRIAGE RGREYVLVKN DGVEGGWALG VVSLEKGMGD RNKPIDVDDY DKRKNKVNLV
SESEEDDFED VPVEGLNRLP KARDNGLNLT YSEFQAREVA NRRREYENSR RESDRRPVRK
PSEDPDSLFV DDTGGQPRPS TTNATYDDED EDINRAIAMS LQQDQGQDDE LDEEDHLKRA
IELSLQKGHG QEEEGDDPFE DVPMLEYEQR AVADARPLTK SSGKMIAHMV NNRANAAVPK
RKEDSETLDS DSDSDMDFQA ALRKARTQKA PEKVQKIAPV AVNKKNPFDG PLPFESLQFK
SSLFGKKKQP EKLAVDPQEE DEEALAGGFE KEDEEEKAKP LPPWLLGNDD IRSQVQQQHK
APTLEVAKES VDDLTDAARA EPSKSDISQD RQLPVQSCAE NTIDLLQDSD EPVEWSESDH
GDVIPKPKKT LDASNTTSVS IEQNSSKSKS PSPVFEDVDL PDVQATEPIQ PLASTRKSPS
PVFEDVDMTN STTFLSSGPT KPPQPPVDDA YDRQEAETIP DEFDFSDPEE EELMTQLAIE
AEEHARFAST LNNKSEKENH DSYEKELKAL RSQQKKDRRD ADEVSHIMIT ECQALLRLFG
IPYITAPMEA EAQCAELVHL GLVDGIVTDD SDIFLFGGTR VYKNLFNSNK LVECYLLSDL
EKELSLSRDQ LISIAHLLGS DYTEVGWSQE RVDEILVPVI RDMNRRELEG TQSNITRFFE
GGVGVGGLGT ASAGGGEREK GGSKRMREAV GKLKAKKKGN ALKDRGTFAD DAREWAKRNE
LSVGAQERKK AESAGRKGSG KGKGKGKKRS VEEMDGGENE NEDEDQDKDA DEDADIETEE
NEPDDEDEEE TATSTPKPSR SRSTSGKATS RGKGINKTQG QGPKRKKM
//
