SLX4_PHANO
ID SLX4_PHANO Reviewed; 946 AA.
AC Q0V640;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=SNOG_00524;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445325; EAT92019.2; -; Genomic_DNA.
DR RefSeq; XP_001791208.1; XM_001791156.1.
DR AlphaFoldDB; Q0V640; -.
DR SMR; Q0V640; -.
DR STRING; 321614.Q0V640; -.
DR EnsemblFungi; SNOT_00524; SNOT_00524; SNOG_00524.
DR GeneID; 5968610; -.
DR KEGG; pno:SNOG_00524; -.
DR eggNOG; ENOG502S832; Eukaryota.
DR HOGENOM; CLU_302495_0_0_1; -.
DR InParanoid; Q0V640; -.
DR OrthoDB; 231792at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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: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 HAMAP; MF_03110; Endonuc_su_Slx4; 1.
DR InterPro; IPR027784; Slx4_ascomycetes.
DR InterPro; IPR018574; Structure-sp_endonuc_su_Slx4.
DR Pfam; PF09494; Slx4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..946
FT /note="Structure-specific endonuclease subunit SLX4"
FT /id="PRO_0000388040"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 102257 MW; F1A2B97A73F05F47 CRC64;
MPASPLPALS PPASPRRNTS GASALGSRKA DIPPDAIRGF ATVGSLVRSE HFAQHFDDDI
AGKDQEQSRK KSPEDVGNIA ATKKKPGKRA ATTSTADGEA KPKPKPRARK PKAADEEAVI
IDPELRLPAA KVSPFFAAEG APAAIEPSDE PVVDVPKLTK AGKPRKPRAK KENVGGEEAV
PKPKRTRVTK PKAAKAKAGG KSQEEACVES AHFRKSEDTG DETVAGVLAT RKSATTENVG
SGEASIWDVP QSPKPKKKRA PKKPPPDPVI NNLELDEAVS RRRDWTPPRD TAIPSPFTDS
VGKENKQIEP DADNGGFTHM ISNFAYAQAL PAQVASTVAD SATGTMAATK RRRIELLDVP
GNQTTSRNSS PEKGKAPKKK PRTITDIATE QYQHRAAQLD QSDVASDFFQ SHTAVTKVPL
NDASLPNGDA PTKKPPRKRS TSKPASEKEK VGSKARSKKA STKAAAKPKH IAEKLLSPGS
ALMRMNKQDI LFGTSSQLAL EEPPTLVRQL QHALKESEVE ADLSSNGMIA PPPRWPKLDK
VVGKRSLWDA SSRDVEGGML EHMEDVYIPE FDRTQDFPLL MDGTNDQPDG APPSFADIDD
FEPAPPVIIS SDGPTPPPTT SRTSQRKAND EPDHVMEGPV FEDIDDFDFQ PPPSNQNVEF
QDSFADDDEI LHTSVQSSTH PPPRLRPPAT SDPMNGSSKK PRGCPAKSQS AIATSGSPAV
AKEPKRTKGK EVKSAPAPPT TPAKGSGRFI DIDEILDSDD EALQALSPTP PRIHNFENSQ
PLPLYSVSPT RAKKPKADSS VDSKIVPVHI IPTAHLEWLN LKNSIFPSIT SHIRSLPSTR
DPSKPSWHEK ILMYDPIVLE DFTAYLNAKT SLRTWRRATK IQSKAWNKAQ KSIGAQEIGV
VEGGGNVLAV EKELEAWQVQ SWCESMSVCC IWGEGRGKGG VRKGFY
