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SLX4_ASPFN
ID   SLX4_ASPFN              Reviewed;         819 AA.
AC   B8NLN6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, 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=AFLA_092520;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963480; EED49171.1; -; Genomic_DNA.
DR   RefSeq; XP_002381072.1; XM_002381031.1.
DR   AlphaFoldDB; B8NLN6; -.
DR   SMR; B8NLN6; -.
DR   STRING; 332952.B8NLN6; -.
DR   EnsemblFungi; EED49171; EED49171; AFLA_092520.
DR   VEuPathDB; FungiDB:AFLA_092520; -.
DR   eggNOG; ENOG502S832; Eukaryota.
DR   HOGENOM; CLU_016773_0_0_1; -.
DR   OMA; TWHEKIL; -.
DR   Proteomes; UP000001875; 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.
FT   CHAIN           1..819
FT                   /note="Structure-specific endonuclease subunit slx4"
FT                   /id="PRO_0000388013"
FT   REGION          1..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  89189 MW;  851ACB95421BC1A2 CRC64;
     MSAAADVIVL SSSPDRIPNG SPVLPAHDPA KLFDLSPPSA SPSPVRSPSE LFQISTRSRF
     FELETPSRNK ENKTPKEPPV RKVNTTSKAK SASSQDKPKR RGRKPASESQ TVLGDSGLAG
     LAQQSAPKKT AGARKKRVDS EGKRGKATNR TIMGRVAKSG NVQAKPPQEK IMDVSTPNAL
     PPTKPASGVV SLEIDGLQLE TAMKRRIDWT PTKDTTARTV ESSQQEVAEA NPQSFGSLLS
     EYGFNDISSA QSDVRNLGDD GPTKRRRIEL VDSRLFGSSK PASHDIDDKN LTEDSQQKQP
     EPKQKPKKQT KKFTTLTARV TASYLNNSHE GSDSSSKETT TSRENAATSR TRGSKRKGKA
     TSKPKEPEFI VLSPEAAAKS LENQELIFGT CSQLEREDSP TSLKELQAAI SESERYAVAE
     PSPLSSTLCA TPTSRFTTAR GLWSVAARDL EGSLIRQTEV VDLVDTPEPA KMTTSTNDSR
     NEKALEDAAT VPPKEPFDLP QSEPPKLKAI PAAKKEPSPA PGLPTIKASD NLKGTTSQHS
     KPQPKMPNYN GFTDAELSRQ VASYGFKPVK NRKAMIDLLQ KCWVSKHGKG TTFETQAGSQ
     NTSTEPTPVL TSSEPNTSQK QPRKTATSRK TAAKSKTNPD SNPPPKINSR KTPSSSDATK
     APSIQSKPTQ PPPIQSLSNV EEIEDSEEET LPSPFRIQNR YTPQPPETRQ ALPVSKTLYS
     PSRPKPRTTK STTNNSATLN QKQPDLADQI FKAMHAQPAG TPSRPSWHEK ILMYDPIILE
     DFATWLNTEG LGLVGEDREV SAAFLRKWCE SRGICCCYR
 
 
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