SLX4_PARBD
ID SLX4_PARBD Reviewed; 869 AA.
AC C1GAZ3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 3.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=PADG_04429;
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275960; EEH48345.2; -; Genomic_DNA.
DR RefSeq; XP_010759462.1; XM_010761160.1.
DR AlphaFoldDB; C1GAZ3; -.
DR SMR; C1GAZ3; -.
DR EnsemblFungi; EEH48345; EEH48345; PADG_04429.
DR GeneID; 22583552; -.
DR KEGG; pbn:PADG_04429; -.
DR VEuPathDB; FungiDB:PADG_04429; -.
DR eggNOG; ENOG502SEB3; Eukaryota.
DR HOGENOM; CLU_016773_0_0_1; -.
DR OMA; TWHEKIL; -.
DR Proteomes; UP000001628; 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..869
FT /note="Structure-specific endonuclease subunit SLX4"
FT /id="PRO_0000388037"
FT REGION 40..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 94494 MW; 7A0C6159FEC7DDA6 CRC64;
MNPATMTRQL SSDGRMFASS IITVIPDSSP TAAEAIELSS PLSLPSPTSL LDFLSTSTSR
GPARSDTDGD KTQGKEVLDT KPILENSFRR ENRVVSGTGG KAATGKKLKR RTESPGNVCQ
SEIHIVPGER IILRQTRPDK KAAKAKRTKK EDGLINRKLY GRVSKANQTV SLQPETKKSA
PKGCNDTTQP ADNGHINDLD DGLQLEQAIQ RRLDWTPTKD TTIPVIDLVG DSPSSCEKSL
SGMRSTRTML SNYEFSGIVG TLGGSRSEGT PDAPTTKRPV ELLKVNNLKE ISGLSDSRQS
SITEDSESAT SKPRRVKAKN PPKSKLTTIT SYATAKYTVV EKSVDLDPVE TLLSDEPGKE
KNVAKRTSGA RCAKPGRKKS ATTEKKNEPP IFKVVPPLEA FKAFDGQELL FGTSSQLANG
HSEDRHEQNE GTSHISNSSA FIPLSRSESS SKAPSQTSLG SGFLKLSSSK NLWSAGARDL
TGAVLEIDEI DLSEHWMKPS IFESQPKAPL GCKADTQIPP QLGEIDFDNS CQKPLAAIDP
PELVTQSETP SEKGDLHKYI VKPTHINSCS QSGSSISVGS PEKPVQDKPI FSGFTTSELA
KKVAAYGFKP IKSRDKMIAL LEKCWENRNK TSNSVPKLTP GDGLSQVDES TQGQSLGQHL
KPNSIPQTAT TQVPKVKPDK RDTKSQGVPV PSRRSTSTSK VSRKRTESPS AILVDDDQRS
DSTGDSVPPS RPRRPSKSCT PRDRQKSPES FNLPTIPLTI RSGKIPSTGT ASETLPSLST
QITAAIKAQP RLRAFNGVKQ PTWYEKILMY DPIQLEDLAV WLNTDGFERI GEDREVCPGL
VREWCESKGV CCIWRKQRGV RAHCPLVRA
