SLX4_ASPOR
ID SLX4_ASPOR Reviewed; 819 AA.
AC Q2U6E8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=slx4; ORFNames=AO090120000266;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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=BAE62867.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007166; BAE62867.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001824000.2; XM_001823948.2.
DR AlphaFoldDB; Q2U6E8; -.
DR SMR; Q2U6E8; -.
DR STRING; 510516.Q2U6E8; -.
DR VEuPathDB; FungiDB:AO090120000266; -.
DR Proteomes; UP000006564; Chromosome 5.
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..819
FT /note="Structure-specific endonuclease subunit slx4"
FT /id="PRO_0000388017"
FT REGION 1..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..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 36..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; 89197 MW; 022C91C1B9160B4C CRC64;
MSAAADVIVL SSSPDRIPNG SPVLPAHDPA KLFDLSPPSA SSSPVRSPSE 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 KSEPPKLKAI PAAKKEPSPA PGMPTIKASD 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
