SLX4_PARBA
ID SLX4_PARBA Reviewed; 864 AA.
AC C1H7M6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=PAAG_06767;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
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; KN294011; EEH36349.2; -; Genomic_DNA.
DR RefSeq; XP_002791221.2; XM_002791175.2.
DR AlphaFoldDB; C1H7M6; -.
DR SMR; C1H7M6; -.
DR EnsemblFungi; EEH36349; EEH36349; PAAG_06767.
DR GeneID; 9094473; -.
DR KEGG; pbl:PAAG_06767; -.
DR VEuPathDB; FungiDB:PAAG_06767; -.
DR eggNOG; ENOG502SEB3; Eukaryota.
DR HOGENOM; CLU_016773_0_0_1; -.
DR OMA; TWHEKIL; -.
DR OrthoDB; 231792at2759; -.
DR Proteomes; UP000002059; Partially assembled 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..864
FT /note="Structure-specific endonuclease subunit SLX4"
FT /id="PRO_0000388035"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 93987 MW; A46296139C6C8AD8 CRC64;
MTTQSSSDGR MFTSSIIPVI PDSSPTAAEV IELSSQLSLP SPTSLLDFLS TSTSRGPTRS
DTVGDKTQGK EVLDTRPILE NSFRRENRVV TGTGGKAATG KRLKRRTESP GNACQSKIHI
VSGEQIILGQ SRPEKKAAKT KRTKKEDGLI NYKLHGRVSK ANQTVSRQPE TKISAPKECN
DTTQPAGNDH INDLDDGLQL EQATQRRFDW TPTKDTTIPV IDLVGDSPSS CEKSLSGMRS
TRTMLSNYEF SGVVGTLGGS RSEGTPDAPT TKRPIELLKV NNFKEISGLS DDRQSSITED
SESATSKPRR VKAKNRPKSK LTTITSYATA KYTVVEKSVN LDPVETLLSD EPGKEKSAAK
RTSGARCAKP GRKKSTTTEK KNEPPIFKVV HPLEAFKAFG GQELLFGTSS QLANGHSEDQ
HEQNEGTSHI SNSSAFLPLS RSESSSKALS QASLGSGFLK LSSSKNLWSA GARDLTGAVL
EIDEIDLSEH RMKPSIFAFQ PKAPLGCKAD TQIPPQLGEI DSDNSCQKPL AAIDPPEFVT
RSETPSEKGV LHKYIVKPTH TNSCSQSGSS ISVGSPEKPV QDKPIFNGFT TSELAKKVAA
YGFKPIKSRD KMISLLEKCW ENRNKAPNSV PKLTPGDGLS KVDEPTKGQS LGPHLQPNSI
SQKATTQVPK VKPAKRATKS QGVPVSSRRS TSTSKVSRKR TVSPSAILVD DDQTSDSTGD
SVPPSRPRQP SKSCTPRDRE NTPESFNLPT TPLTIRSGKV PSTVTSSESL PSLYTQITAA
IKAQPRLRAF NGVKQPTWYE KILMYDPIQL EDLAVWLNTD GFERIGEDRE VWPGLLREWC
ESKGVCCIWR KQRGARAHCP LVRA
