SLX4_PENRW
ID SLX4_PENRW Reviewed; 884 AA.
AC B6HBG5;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, 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=Pc18g04010;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(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; AM920433; CAP94625.1; -; Genomic_DNA.
DR RefSeq; XP_002562237.1; XM_002562191.1.
DR AlphaFoldDB; B6HBG5; -.
DR SMR; B6HBG5; -.
DR STRING; 500485.B6HBG5; -.
DR EnsemblFungi; CAP94625; CAP94625; PCH_Pc18g04010.
DR GeneID; 8306877; -.
DR KEGG; pcs:Pc18g04010; -.
DR VEuPathDB; FungiDB:PCH_Pc18g04010; -.
DR eggNOG; ENOG502S832; Eukaryota.
DR HOGENOM; CLU_016773_0_0_1; -.
DR OMA; TWHEKIL; -.
DR OrthoDB; 231792at2759; -.
DR BioCyc; PCHR:PC18G04010-MON; -.
DR Proteomes; UP000000724; Contig Pc00c18.
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..884
FT /note="Structure-specific endonuclease subunit slx4"
FT /id="PRO_0000388038"
FT REGION 1..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 95645 MW; C09B71042CE28772 CRC64;
MTSMADVIIL SSSPHPPRSP GPGRHDTKPV SHALPRSATP PPIRSTSDLS QPHTRSRFFP
TPVASNKCPD GASKPKKRLT KDPASETSKQ TAPSKPRREA KKVAGAPGTT ALGEPQPEAV
GKKNDAVKPT KSRSRRNAKS KDSGNMTLAG KVTKTSGDLP SKKSSKGGKK TVATKLSPSE
DTSEKSTPKE SNALGKDEVL RLDEAMRRRM DWTPPRETAY EEIATVTDRG SQDQDRDSSS
SGGFGKLVSD YNYSGSALHP RDFVQNANGE GPTKRRRIEL VNPEIQALLN GRYSDSSDQS
SGQGENTGKP KKTTKGKPKK FTTLTARMTA QYSKNDAEED EPVIDCLAGI RTTKGRQKKA
KEIEKQSSST VLSPEAAVEF LNDQDLIFGS CSQLEKDDSP ETLRETQQAI RVPEGPSYSK
GTHNKDPSAI QESSTRFVSK LAGTRNLWCV GARDTEGSLI QPETLNVVDL TNGEESPGKK
SQDDAENPSH NTLQSDWYEL EFADIDSPSE KRPSPLPTES VLDSDTQVQA PAPIPADTAT
ATATATAVVK AAKPAKGAND TPTEAVDSQP ASSQAPPMPQ YTGFTDAELS KQVSSYGFKA
VRGRKKMIDL LRQCWESKHG SGSNAASDSQ LICQLEQQEE PASKMDNVPK STSAAKTKAT
VKPKAGTSIR NRKSLDATKS TSASRTNLQT SPKKNSREKP ITGTSTSFID VEEIQDSEEE
IIPSPSQVQK HYTDIYSKSK TGSWVQDHSL DILTKTPSPS PTKRKVVSSD IPAKRPPSSA
SIATTRMTES SKEISLAEIS AQITQAVRLQ PQLSPLSSSR GSRSRPTWHE KILMYDPIVL
EDFTAWLNIE GLGLVGEDRE VGTASVREWC ESKGICCCWK KNAS
