SLX4_BOTFB
ID SLX4_BOTFB Reviewed; 896 AA.
AC A6SK19;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=slx4; ORFNames=BC1G_13159;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., 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., Gueldener 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 -!- 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; CH476952; EDN19004.1; -; Genomic_DNA.
DR RefSeq; XP_001548439.1; XM_001548389.1.
DR AlphaFoldDB; A6SK19; -.
DR SMR; A6SK19; -.
DR OMA; TWHEKIL; -.
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.
FT CHAIN 1..896
FT /note="Structure-specific endonuclease subunit slx4"
FT /id="PRO_0000388019"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 97303 MW; 885ED94CE2F1153F CRC64;
MATTDVFIIS SSPPRQSVSY NVSSPPLPSL DEMIKQKKAP NLRRGGGAAS TPLDPTATFT
SASALLRRGS SGSLQEFDTA RSLATTTKPD ENEQKKTAKP KAPRKPAAKK EDGPIEKVAK
VPRKTTRNKG EDRAEGFIEG VVEEGKEGVK TIPEKKPRKS RAKKTDNLGG DGEDGGITGA
VVPDVSKVAV ETKACKPRAK KGDDITGEGV KERAPRKPRA KKTDVEAGSE SVAKEKAGRV
TKTTNASNPD KVETPKADKV SKHFASNPVV EDLLAEEGSG LSEAVKRRKN WTPPKSNQVL
IDYDDSPEAG SSGCNQGFTE LLGSFGFSSS EANSIEKRIS SGVSSGAAVT RKRKLIEMVH
TNIPTTAGTK ATKEKAVKKK ARTLTDLATS AYTATEDDDT INDTPAPLLQ HFPKAASGEL
TNDGFKKPPK LRSKSPVKGL PKSKKGSAEE PILLSPESAL KQVGNQDFVF GTSSQLARED
SPSLLRDLHD AMQASNELDD YDDPFISPPT KIAERAKAVI AAKRNLWSIA ARDDHGDLID
IETVDLAHTP VAKPDRIILS QKPSSLWITP AKDEWYDIDE IEENRPPSTQ VPVRQMGPIE
MAINLELSNS PLQPKNSSKD VSTSSPRKKH TKASIIETTP KKTTTAKMPD YESFTTPQLS
REIQKYKFKQ IKSRKKMIDL LVQCFESQNR PALGVLQAGS STQLEPTISS SQRGRGRPTK
DTAASKSKAK SKIKDSVAIL ETDSNAPLSE FRTPKKSKKG KQVIEDVPDS DHPMTPSPPR
RSASQIRKAS KALELSPIKN DHDDEAQQAQ LFTHIYTAIT SAPPSQDLSN PSWHEKILLY
DPVVLEDLAS WLNTGALGKV GWDGEVAPKE LKKWCESKSI CCLWKENQGG GARSRY
