SLX4_PARBP
ID SLX4_PARBP Reviewed; 864 AA.
AC C0S0E2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=PABG_01057;
OS Paracoccidioides brasiliensis (strain Pb03).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=482561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb03;
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; KN305532; EEH18738.1; -; Genomic_DNA.
DR AlphaFoldDB; C0S0E2; -.
DR SMR; C0S0E2; -.
DR EnsemblFungi; EEH18738; EEH18738; PABG_01057.
DR VEuPathDB; FungiDB:PABG_01057; -.
DR HOGENOM; CLU_016773_0_0_1; -.
DR InParanoid; C0S0E2; -.
DR Proteomes; UP000002740; 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.
FT CHAIN 1..864
FT /note="Structure-specific endonuclease subunit SLX4"
FT /id="PRO_0000388036"
FT REGION 35..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar 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 625..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 94143 MW; 6C76F4B7D0E96126 CRC64;
MTRQLSSDGR MFASSIITVI PDSSPTAAEA IELSSPLSLP SPTSLLDFLS TSTSRGPARS
DTDGDKTQGK EVLDTRPILE NSFRRENRVV SGTGGKAATG KKLKRRTESP GNACQSEIHI
VPGERIILRQ TRPDKKAAKT KRTKKEDGLM NRKLYGRVSK ANQTVSLQPE TKKSAPKGCN
DTTQPAENGH INDLDDGLQL EQAIQRRLDW TPTKDTTIPV IDLVGDSPSS CEKSLSGMRS
TRTMLSNYEF SGIVGTLGGS RSEGTPDAPT TKRPVELLKV NNLKEISGLS DSRQSSITED
SESATSKPRR VKAKNPPKSK LTTITSYATA KYTVVEKSVD LDPVETLLSD EPGKEKNVAK
RTSGARYAKP GRKKSATTEK KNEPPIFKVV PPLEAFKAFD GQELLFGTSS QLANGHSEDQ
HEQNEGTSHI SNSSAFIPLS RSESSSKAPS QTSLGSGFLK LSSSKNLWSA GARDLTGAVL
EIDEIDLSEH WMKPSIFESQ PKAPLGCKAD TQIPPQLGEI DFDNSCQKPL AAIDPPELVT
QSETPSEKGD LHKYIVKPTH INSCSQSGSS ISVGSPEKPV QDKPIFSGFT TSELAKKVAA
YGFKPIKSRD KMIALLEKCW ENRNKTSNSV PKLTPGDRLS QVDESTQGQS LGPHLKPNSI
PQTATTQVPK VKPDKRDTKS QGVPVPSRRS TSTSKVSRKR TESPSAILVD DDQRSDSTGD
SVPPSRPRRP SKSCTPRDRQ KTPESFNLPT TPLTIRSGKI PSTGTASETL PSLSTQITAA
IKAQPRLRAF NGVKQPTWYE KILMYDPIQL EDLAVWLNTD GFERIGEDRE VCPGLVREWC
ESKGVCCIWR KQRGVRAHCP LVRA
