ID   SLX4_ASPTN              Reviewed;         773 AA.
AC   Q0C9R2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN   Name=slx4; ORFNames=ATEG_09572;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU29763.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476608; EAU29763.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001218194.1; XM_001218193.1.
DR   AlphaFoldDB; Q0C9R2; -.
DR   SMR; Q0C9R2; -.
DR   STRING; 341663.Q0C9R2; -.
DR   EnsemblFungi; EAU29763; EAU29763; ATEG_09572.
DR   GeneID; 4354381; -.
DR   eggNOG; ENOG502S832; Eukaryota.
DR   OrthoDB; 231792at2759; -.
DR   Proteomes; UP000007963; 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..773
FT                   /note="Structure-specific endonuclease subunit slx4"
FT                   /id="PRO_0000388018"
FT   REGION          1..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  84830 MW;  6ECD16FD0899A123 CRC64;
     MSAASNPIVL SSSPEHCAPR AAAPTTHDFN EAAAVPSRGS SPESILSPSS LCRLPTRSRY
     FQKESLSDEP RTENGPPRGP PSKTSERREK REKKVERSIS EPAAGLDGVR PPLLPQKANA
     PKRASGSNKK RGKCSKSETS TNKTLTGRVA KSGSMGSQES DKTATDASQC GSLRQKSPKP
     SDDGGNNDLQ LEAALKRRLD WTPTKDTSIE LVDASQEGAK EGSSKGFGDL LAGYSFNNNL
     LFSKCTSNDT TAEESTEDSQ NGDRASEAKR RTKQRTKKFT TLTARVTARY QSDDMHSRLQ
     TENPDGFMES ANGNMPKLKR KGTSRSKRQQ PEVVILSPEE AVKSLNEQDL IFGTCSQLER
     EDSPTMIRDL QAAIHESEQN MASQPTNSLL QRAGGGSMST STVSRFRAPK SLWSVAARDL
     DGSLIDAEVV DLTESPSFKP SMANKQVTAG SIPENPPYEE KIRESDSISQ PSKRIHNQDE
     APKPEASEHT HLSMPNYNDF TDAVLSERVT EFGFKPLKNR RKMVELLEKC WETKYGPSLY
     INDTSDQQAG PASSTSRVAS ARLQVPEGQP SKTKESREAT KPKTAAGSKR TTKSDANPCT
     AAGPTRERTK ITASGTRLNK PSSITSYRDV EEIEDSEEEI IPSPNRLQNN FRISRSSKRT
     ASLSVTDTSS SPSRMPLSAG LSGVDKRNPS DISDQITRAV RAQSSTRPGT RNCPTWHEKI
     LMYDPIIIED FTTWLNTEGL GLVREDREVN VGSVRQWCES RGICCCYRRL NRN