SLX1_USTMA
ID SLX1_USTMA Reviewed; 658 AA.
AC Q4PDF6; A0A0D1E3J3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=UMAG_01857;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003142; KIS70699.1; -; Genomic_DNA.
DR RefSeq; XP_011387796.1; XM_011389494.1.
DR AlphaFoldDB; Q4PDF6; -.
DR SMR; Q4PDF6; -.
DR STRING; 5270.UM01857P0; -.
DR EnsemblFungi; KIS70699; KIS70699; UMAG_01857.
DR GeneID; 23562742; -.
DR KEGG; uma:UMAG_01857; -.
DR VEuPathDB; FungiDB:UMAG_01857; -.
DR eggNOG; KOG3005; Eukaryota.
DR HOGENOM; CLU_432191_0_0_1; -.
DR InParanoid; Q4PDF6; -.
DR OMA; GRPWEME; -.
DR OrthoDB; 844266at2759; -.
DR Proteomes; UP000000561; Chromosome 3.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IBA:GO_Central.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01541; GIY-YIG; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..658
FT /note="Structure-specific endonuclease subunit SLX1"
FT /id="PRO_0000383801"
FT DOMAIN 12..92
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 72798 MW; CCE82A5ED8C1BF3E CRC64;
MPSSVTKHTI PPFYACYFLR SLSTPGTTYI GSTPAPPRRK RQHNGHLTQG AYKTSRARPW
EMECIVYGFS SKIAALQFEW AWAKPHLSRH LKFLTTEHSV DGTPKNTSDW AGMSLFPSTS
LTPGQTRWGR PKKRMARPPS SPNARLLAMR ALLRSEPFCG WGLKLAFFTE WSWLAYQRLD
ACDPGLVAKS ALSTLQNRYS RSGKPLHALY PVAVCDFSGV DGKREPLVHV SEPYRLDAGV
AEHPVKKRQT SSRQKPHTEE TSAWPETLPR SANLKGLDAC MQDFATFPIP QPAAPNTDLT
KKSKRAKKLS DKARPSALED HDAENGVDDD DTEVEVVATD AANGSDLALS RPLYRMRFDD
LNMEESEWKR FAESIAANVG ASRSTTQAMS EFLHTCVQRH IAAQDARTAN TALPAPTSLC
SLCSIPIDLS QQLDFVLCPN PHASTLPLIS SSSTASHETI SECRETGCDS IFHLSCLARS
FLEQQLGDQK ATASSASTVL PTHGTCPCHR GEHKEPTMWA DVVRAMYRRH ERFERLIQFL
IRSGRSLEQH LHPPLEVEMT VKGSKIKERV KASVKATEDA QVDIGDQRQV ISGTTSRTKA
ALTRKRRQPT TSSVNAIQVD PLARNGSKID GDGAGKDTKK NTTQKAKSNE TSEVIDLT
