SLX4_ASPCL
ID SLX4_ASPCL Reviewed; 823 AA.
AC A1CEY6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=slx4; ORFNames=ACLA_091330;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027052; EAW11435.1; -; Genomic_DNA.
DR RefSeq; XP_001272861.1; XM_001272860.1.
DR AlphaFoldDB; A1CEY6; -.
DR SMR; A1CEY6; -.
DR STRING; 344612.A1CEY6; -.
DR PRIDE; A1CEY6; -.
DR EnsemblFungi; EAW11435; EAW11435; ACLA_091330.
DR GeneID; 4705099; -.
DR KEGG; act:ACLA_091330; -.
DR VEuPathDB; FungiDB:ACLA_091330; -.
DR eggNOG; ENOG502S832; Eukaryota.
DR HOGENOM; CLU_016773_0_0_1; -.
DR OMA; TWHEKIL; -.
DR OrthoDB; 231792at2759; -.
DR Proteomes; UP000006701; 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..823
FT /note="Structure-specific endonuclease subunit slx4"
FT /id="PRO_0000388012"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 90678 MW; B21362E532C457DF CRC64;
MPSSTEVIVL SSSSPDHIPS QTPAQSNYNP EKLFGLSPLS PSPPPLPSPS ELFQPPTRSR
FFKAQDEKAV VSSNTKQDSN TVAKANKPNA TKRKAAASAT GRSKKSKEDQ TKGDTQTVIR
GSNNALMKLD EEAPKKEPKA RKKRSDAGVK RTLAKNRTIT GKVAKSGSTQ TDVTGLKAEE
PVTFEPYLRK TDIEKAETRD IDDLQLDAAM KRRLDWTPTK DTRKQLVALD MVDGEPDQNR
FGNLVSGYGY SNTSSDLEAN SKRLEDGAAT KRRRIELVES RVFPNVKHVL PDSARASKAP
ALEEKPNKRS KRITTLTGRV TALYVDDATD DSDSASAFTA AFGDVVNNAS ANRSSVQQRG
KSSSRSHVID SSVLPPEAAV SFLKEQDLVF GTCSQLERED SPTMLRDMQM AIRASENDMT
AEPKAYPATR PGSKFSDRAT VSRFATPRKL WSVASRDLDG SLAQIEVLDM VNISKISELP
LKSDDSPETA ALTKGDTGYD AIETDTSFQE QSTTPAEKSP DDEKAVIKDP ELSPPADCQL
KEVVSKESAA PRIPQYAEFT DSQLSKEVKK FGFKSMRSRK KMVEVLEKCW ESKHGATKAE
NQDMGKDIHA HQKAEPDTTR GQTKKRTRKT ATLSETPKTR ANPKIEPKAS AHLKRRQAQE
ANEFSQASNS SFANVEEIED SEDELIPSPS RLQNRYTLHS SETRGSQPLL VSDSPSSQER
KNSESCIILS TFDAVAKPGM PDLSSQINKA VRAQPRSSSA GCKRPSWHEK ILMYDPIILE
DFATWLNTEG LGLVHEDREV SAGFLREWCE SNGICCCFRK NNK
