SLX4_COCIM
ID SLX4_COCIM Reviewed; 822 AA.
AC Q1DYR6; J3KE61;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110};
GN Name=SLX4 {ECO:0000255|HAMAP-Rule:MF_03110}; ORFNames=CIMG_04547;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704914; EAS33523.3; -; Genomic_DNA.
DR RefSeq; XP_001245106.2; XM_001245105.2.
DR AlphaFoldDB; Q1DYR6; -.
DR SMR; Q1DYR6; -.
DR EnsemblFungi; EAS33523; EAS33523; CIMG_04547.
DR GeneID; 4564981; -.
DR KEGG; cim:CIMG_04547; -.
DR VEuPathDB; FungiDB:CIMG_04547; -.
DR InParanoid; Q1DYR6; -.
DR OMA; TWHEKIL; -.
DR OrthoDB; 231792at2759; -.
DR Proteomes; UP000001261; 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..822
FT /note="Structure-specific endonuclease subunit SLX4"
FT /id="PRO_0000388026"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 89002 MW; 95CAFE941D3871C9 CRC64;
MSHLDLTRHR TRSPSPSQIF GSSTTPVATN STHSEPSASS ILRSILGEYA DPKRPDVSGA
DPIRCPVKRV HKTPAVRASS PGRENVPVRT LQSSKDAEGD NFSGDGQLTP CGGPRPLAER
LSPKLLAKQT RRKGVGAQKR TKGCDLVDRI LTGRSIKASA TAASKSSDLP QPQRKGIPTL
VKEANPGEAD WEDEGLQLEP ATKRKYSWTP VKDTNLSIID LTANSGSSPP SIPGREAQKF
TSLVSRYGFA ETSPLAMKNE FPEDFPTRKR QLDLLQGTTN SSSSEGSSNK SSGKCPLKVN
GTKGRRSRKV TTITSLSTAQ YGLKDSPVES FPSVDTTERP SGKRSKSQTK KGGNKKPAGV
SDFKVAPTTD ALKSLEDQVY LFGTSSQLER VSSDEDKLGV PSAPASSRQS ARDRTSVSTL
SKYKVSRNLW AAGWRDLDGS VADIEIVDMV NIDTPKSHES STLTLPSTST NASNQGFSSQ
NTINDRSKPS QTTSTTTEST GVESGQLVVP SLCEDLSEKA GYPAVPERET LSSREIASSE
SAYIETMPSF RGFTTAELAQ KVAAFGFKPI KSREKMISLL EKCWQSQHKN SAPTSLPANN
ANPPDSHASG QKNVVRCDTG GSNASHTTKR ASKAPQKKQS TSSTSHSAKA GPKQVDCSQE
RPNHAYLPHD STQASSQPVI VIPDSEESGD DFQDTYLGSL NRTSSTNYHP LSANSIPDGS
PLFLRTISQA STEEKTSDPS DINQQITRAI KAQPRMTAIN GMKRPTWLEK ILMYDPIWLE
DLTVWLNTEG LDRVGEDREV SRLTVREWCE SKGICCTWKK PT
