SLX4_MAGO7
ID SLX4_MAGO7 Reviewed; 955 AA.
AC A4R1T1; G4MMG4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=MGG_16183;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Regulatory subunit of the SLX1-SLX4 structure-specific
CC endonuclease that resolves DNA secondary structures generated during
CC DNA repair and recombination. Has endonuclease activity towards
CC branched DNA substrates, introducing single-strand cuts in duplex DNA
CC close to junctions with ss-DNA. {ECO:0000255|HAMAP-Rule:MF_03110}.
CC -!- SUBUNIT: Forms a heterodimer with SLX1. {ECO:0000255|HAMAP-
CC Rule:MF_03110}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03110}.
CC -!- PTM: Phosphorylated in response to DNA damage. {ECO:0000255|HAMAP-
CC Rule:MF_03110}.
CC -!- SIMILARITY: Belongs to the SLX4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03110}.
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DR EMBL; CM001231; EHA56942.1; -; Genomic_DNA.
DR RefSeq; XP_003709554.1; XM_003709506.1.
DR AlphaFoldDB; A4R1T1; -.
DR SMR; A4R1T1; -.
DR EnsemblFungi; MGG_16183T0; MGG_16183T0; MGG_16183.
DR GeneID; 12984549; -.
DR KEGG; mgr:MGG_16183; -.
DR VEuPathDB; FungiDB:MGG_16183; -.
DR eggNOG; ENOG502SEB3; Eukaryota.
DR HOGENOM; CLU_005957_0_0_1; -.
DR InParanoid; A4R1T1; -.
DR OMA; TWHEKIL; -.
DR OrthoDB; 231792at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR HAMAP; MF_03110; Endonuc_su_Slx4; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
DR InterPro; IPR027784; Slx4_ascomycetes.
DR InterPro; IPR018574; Structure-sp_endonuc_su_Slx4.
DR Pfam; PF09494; Slx4; 1.
DR SMART; SM00384; AT_hook; 2.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..955
FT /note="Structure-specific endonuclease subunit SLX4"
FT /id="PRO_0000388031"
FT REGION 75..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 103087 MW; 6C70080930047681 CRC64;
MTTPRFLPSS PPGQARSDLY TTLVSSSPDL PSINELVSRY AKKPKPLRSG SNAASIPTTA
TTTFTTAAKL LQSAQAEQAD LVETLPPPRA KTKAKPKQKD PPEVVDLSPD LPVNIPEPQP
ERRKARKTAN GVTKKKRGGG EESVADDATN EITTPTKNQP WKFFKSPSPR TTSDLEITGF
QEVAATTAPV TTSTTDLTKG TASAQNKVTK SRVRKTSSAA SRKKKAETVS RHFAVPDDVS
TAPEPITVPD DAPEEQLFNL EPAVARRLDW TPPRETNTAD LCPVSSNAKE VTSTLDGALS
AAPAAVQNVF LTLQDKFAYP VEQVARRPDS PSKELGPPPE VIKKRKVIQL VGPSNDSKIP
NQASPVKSKA PKKKPRTITD LATAAYTTEG KQSNAPAKKG TLTSYLEGQG EQVFQHCHPD
SRLRKPERKR KPKGRGQVLL SPLSAIDQSA RQDFVFGTSS QLAQEHSPTF LRDLHAALRQ
SNDFSDDPFA SPIMAAPQGR KLWTAGARGE EGDLMNIEVI DLVDSPAFPD DPDAIVRAEM
QKSPSRSEPK GIKNRRTPMV NLDSSEIDIS EPHARDLESA NSAEHTLKTQ ASKSTHFAST
TPPRPTKITM VPACENTAEP PIVASDVDSD NEPPPSNQQA YQMPPPPRPV VPEETAIPRP
NFEVMTDTQL SKQVSSYGFK SVKKRSAMIA LLNQCWESKA GATGAAGQSS AFATTSRTSA
PRGPRGKTST AAAAAKSPTK RPVGRPRKNS VGASGDVTVV EATTPVKRPR GRPKKNAKAE
ASPDMMQNIA ASMPPTVAAA VKTPRRRKKA ATQPAVEILD SDGEAGLSPS PSLSPEPVFS
SPEKDSVDVS IGEHTTMSLA VTPTAQQAEL FTRITRAVKS APRSTDPDKP SWHEKMLMYD
PIVLEDLAAW LNSGQLDRVG YDGEVAPADV KMWCESKSIC CLWRMSYRGR ERKRL
