SLX4_ASPNC
ID SLX4_ASPNC Reviewed; 828 AA.
AC A5AAW6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=slx4; ORFNames=An07g07650;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK39581.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM270139; CAK39581.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001391840.2; XM_001391803.2.
DR AlphaFoldDB; A5AAW6; -.
DR SMR; A5AAW6; -.
DR PaxDb; A5AAW6; -.
DR PRIDE; A5AAW6; -.
DR EnsemblFungi; CAK39581; CAK39581; An07g07650.
DR GeneID; 4982034; -.
DR KEGG; ang:ANI_1_2014064; -.
DR Proteomes; UP000006706; Chromosome 4L.
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..828
FT /note="Structure-specific endonuclease subunit slx4"
FT /id="PRO_0000388016"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 90287 MW; 1A26845C168604F8 CRC64;
MSATAEVLVI SSSPERNPVH TPAPPAYDPE RLFGLSPVDV ETTPLPSPSD LFCPPTHSRF
FEVGNQVDEL RRDETRKKSS TLTNDDSAVT TLEGEPATDK PKRRGRPKKE QKRATEELGP
CVTGNEKTTT KKTITGTSKK RAQPATKRSK QANKTISGRV AKAGTPQVKE AGEKAICPST
PTTALPLKAT NDVLEWERDG LQLEQAMTRR LDWTPTVNKV KEVVELEGKS GSDDNTRGFG
NLLSEYGFNG AAAPVNDFMA SVEGGPTKRR RIELVDPGVY PAPRQSVADD SEKDNTEGTR
KSTPAARKKP TKRANKFTTL TARVTAKYIN ESTEGSDVVD EETPKAKPKV SRSKKKGQAS
KSYEPEFVVL SPEEAAKSLD DQELVFGTCS QLEREDSPTT IRELQAAISE SERSMTLEAS
GRPHRTQSKG SSSTVSRFNG SGNLWSVASR DVDGSLMQVE VVDLVNSPDR SGTITLDERP
SNAKRVAEAE CNTSDINPTQ KGSDQAKAAS TSETQPVVPS TTQSKNKKAE NTTSIARKPD
PKMPQYDNFT DAQLSKQAAS FGFKPLKNRK KMIELLEKCW KAKNSISSEA NNENTDQETP
AEPESAPEPG NKPKGKGTTR KTTTKAKAKT QPSTSSKSTT EAISTTKSPS NPNSNTTTST
STSISKPTPS YANVEEIEDS EEDSDPISFP SPSRLLPQTL QTNHKHAHTL PTSNLPSSPN
RTTSTSVPKE PEPPAILLPL TEQITKAVRA QSAAHPASSN SNKTHTRKQT WHEKILMYDP
IPLEEFTTWL NTEGLGLVNE DREVGAGFVR RWCESKGVVC CYRPRKKE
