SLX1_MALGO
ID SLX1_MALGO Reviewed; 443 AA.
AC A8PWH1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Structure-specific endonuclease subunit SLX1 {ECO:0000255|HAMAP-Rule:MF_03100};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN Name=SLX1 {ECO:0000255|HAMAP-Rule:MF_03100}; ORFNames=MGL_1098;
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966;
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- FUNCTION: Catalytic 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_03100}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03100};
CC -!- SUBUNIT: Forms a heterodimer with SLX4. {ECO:0000255|HAMAP-
CC Rule:MF_03100}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100}.
CC -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03100}.
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DR EMBL; AAYY01000003; EDP44616.1; -; Genomic_DNA.
DR RefSeq; XP_001731830.1; XM_001731778.1.
DR AlphaFoldDB; A8PWH1; -.
DR STRING; 425265.A8PWH1; -.
DR EnsemblFungi; EDP44616; EDP44616; MGL_1098.
DR GeneID; 5856135; -.
DR KEGG; mgl:MGL_1098; -.
DR VEuPathDB; FungiDB:MGL_1098; -.
DR InParanoid; A8PWH1; -.
DR OMA; EYAYGVW; -.
DR OrthoDB; 844266at2759; -.
DR Proteomes; UP000008837; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.1440.10; -; 1.
DR HAMAP; MF_03100; Endonuc_su_Slx1; 1.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR027520; Slx1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01541; GIY-YIG; 1.
DR SUPFAM; SSF82771; SSF82771; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..443
FT /note="Structure-specific endonuclease subunit SLX1"
FT /id="PRO_0000383786"
FT DOMAIN 13..93
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 361..419
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT REGION 121..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 50029 MW; DDFBE9CBF1F47D7D CRC64;
MRISSVVEHR TPRVYVCYCL RSLSRPNQTY IGSTPDPIRR LRQHNGLVKQ GAFYTRMARP
WTMDVVVYGF PSKLAALQFE WSWQKPHASR HLRVMHDDGT RPNKSSATAA VYAGRSSKPL
FPATRSSAPS SAASHDSGLN LRKKNRRVRM RSSTVPEYKF LVLRALLASE PFCFWHLHVG
FYSEYAYGVW QFMDRANPTR YSVSRITRRP LPPSYPPVAC DFRGVQGTNT PLAPPQDATA
HTLRTSYPVL PEATTLSAAQ KKKRSTSASC APENEHMWAE EIPHARDAET LGLTWEQLEH
APTIARMEVP DGLMQASSAA RGRSRRLRSH TSFLEALDQD ASALEAHLVH ASRKDMSSSI
CGLCGGHINR HVPLSYTHCP HACDAVFHLT CLARYSLEQE TRAHARTFCL PTSAWCPMCQ
RPPVPWPEIV RRVFRRAELK VSM