ID N1QKV4_SPHMS Unreviewed; 1387 AA.
AC N1QKV4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=PIN domain-like protein {ECO:0000313|EMBL:EMF16922.1};
GN ORFNames=SEPMUDRAFT_146048 {ECO:0000313|EMBL:EMF16922.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF16922.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF16922.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF16922.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB456260; EMF16922.1; -; Genomic_DNA.
DR RefSeq; XP_016765043.1; XM_016903422.1.
DR STRING; 692275.N1QKV4; -.
DR GeneID; 27900559; -.
DR eggNOG; KOG2520; Eukaryota.
DR HOGENOM; CLU_003018_0_1_1; -.
DR OMA; PNSMDFS; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000016931; 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; SM00726; UIM; 2.
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:UP000016931}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 1045..1114
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 114..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1001..1035
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 115..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1387
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 154527 MW; 53A2D2131C15F2C9 CRC64;
MGVTGLWQIL QPCARPIKIE TLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
RICKLLFFGI KPVFVFDGGA PALKRQTIRA RKSRREGRRE DAVRTAGKLL AVQMQRAAEE
EDERRKRQEQ QQRGSARDNN GEEEVPDEGL VYVDELNMSA QERQQNRKFR KKDAYHLPDL
DVSMSEMGGP NDPRVMSLED LQAYAAQFNT GEELSVYDFS KIDYDSAFFM SLPPSDRYNI
LNAARLRSRL RMGHSKEQLD VMFPDRMAFS KFQIERVAER NDLTQRLMHL NESGGAEYGG
NRIAGEKGRE YVLIKNDGVE GGWALGVIDD EGKQEKPIDL DAPGPTKTED EEWEDEVDFE
DVPVEGLNRL PRQKTGTEGA LDALQEQRRE LYKSRGARER AMGDTFRRPT QRKPKKKAAK
RDENSLFVQS SDEEVVEDEW EENATDKKPV GSDEQYSDDE DLRRAIALSM QKDGSGSDQA
GSGPEDDDML EDFQQSATEE ARPVPRGSAR DIAHILNKRA QHAAPDSREI TSFGVPTQKP
DSSDDEDMMD LQAALAESRR SKRKTTPPRR RAPAENSAKE VAKKAGFNGP LPFEKLDLGT
SLLGKKKMQQ RTEEAAGGFE NPALSEKAKK AEPLPPWFSG DVEKDFRAQK AIEAGDRQKA
REYDQQFKFH DRGATLKRGR PNEIIDLEAE DEMPLQKEGE VIDLDAEGSC ISTPAGSQSV
LGGETGESRA GPVLLDKEIL ENDTAVATRY MTGMETANEQ TARPASTDHL SEEPNAELET
RLAVKNSVDT AQDRDTKYST GEAVTSTPPK VPLTDDVFDT EIEPSPALEI VSGRERPKDS
LNASGATEPA RNATRGENSD EEMLEWSESD GEDTAPHTVS NSTKQQGTSA KSPQEMQAAE
QDARSPSVEF EDVEMNQAAT TTTGLTANDF GDIGIPEMTN FDDLPAENEE TDEAQPASMR
QPISEGDEEF DDFSDPEDAE MLRNLTIEAE EHARFASTLN NKSQAQNVAE YERELKQLRN
QQKKDRRDAD EVTQTMIQEC QALLRLFGLP YVTAPMEAEA QCAELVHLGL VDGIVTDDSD
CFLFGGTRIY KNMFNQAKFV ECYLTSDLEK EFGLTRQKLI AVANLLGSDY TEGVPGVGPV
TALEIISEFP DLEEFKEWWT AVQMNERPKS EDAGNSFRKK FRRNASKLFL PHGFPDKRVE
MAYLEPEVDA DSQAFQWGVP DLDKLRSFLM ATIGWTQERT DEVLVPVIKD MNRRLDEGTQ
ANITAFFEGG VGIGAAGTNS RGEAFAPRKR VDPSKRMGTA LTKMAEKAKG KRSGAVQASE
VEDGDAETEQ AGTSDMSTAT AKRRKTAAST RPSTGSDEDG SDFNGPVKKR GTRKAPVKRV
GRRKATT
//
