SLX1_SCHPO
ID SLX1_SCHPO Reviewed; 271 AA.
AC Q9P7M3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Structure-specific endonuclease subunit slx1 {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000303|PubMed:14528010, ECO:0000312|EMBL:CAB76036.1};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN Name=slx1 {ECO:0000312|EMBL:CAB76036.1}; ORFNames=SPAP27G11.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB76036.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP FUNCTION, ENZYMATIC ACTIVITY, COFACTOR, INTERACTION WITH SLX4, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-34 AND GLU-74.
RX PubMed=14528010; DOI=10.1091/mbc.e03-08-0586;
RA Coulon S., Gaillard P.-H.L., Chahwan C., McDonald W.H., Yates J.R. III,
RA Russell P.;
RT "Slx1-Slx4 are subunits of a structure-specific endonuclease that maintains
RT ribosomal DNA in fission yeast.";
RL Mol. Biol. Cell 15:71-80(2004).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=15972456; DOI=10.1534/genetics.105.044966;
RA Sheedy D.M., Dimitrova D., Rankin J.K., Bass K.L., Lee K.M.,
RA Tapia-Alveal C., Harvey S.H., Murray J.M., O'Connell M.J.;
RT "Brc1-mediated DNA repair and damage tolerance.";
RL Genetics 171:457-468(2005).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SLX4, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-34.
RX PubMed=16467377; DOI=10.1091/mbc.e05-11-1006;
RA Coulon S., Noguchi E., Noguchi C., Du L.-L., Nakamura T.M., Russell P.;
RT "Rad22Rad52-dependent repair of ribosomal DNA repeats cleaved by Slx1-Slx4
RT endonuclease.";
RL Mol. Biol. Cell 17:2081-2090(2006).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=17277362; DOI=10.1534/genetics.106.067801;
RA Lee K.M., Nizza S., Hayes T., Bass K.L., Irmisch A., Murray J.M.,
RA O'Connell M.J.;
RT "Brc1-mediated rescue of Smc5/6 deficiency: requirement for multiple
RT nucleases and a novel Rad18 function.";
RL Genetics 175:1585-1595(2007).
RN [6]
RP FUNCTION, AND COFACTOR.
RX PubMed=19596236; DOI=10.1016/j.cell.2009.06.029;
RA Fekairi S., Scaglione S., Chahwan C., Taylor E.R., Tissier A., Coulon S.,
RA Dong M.-Q., Ruse C., Yates J.R. III, Russell P., Fuchs R.P., McGowan C.H.,
RA Gaillard P.-H.L.;
RT "Human SLX4 is a Holliday junction resolvase subunit that binds multiple
RT DNA repair/recombination endonucleases.";
RL Cell 138:78-89(2009).
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. Has a preference for stem-loop (SL) and
CC splayed arm Y structures. Introduces a single-strand cut in duplex DNA
CC on the 3' side of a double-strand/single-strand junction with respect
CC to the single-strand moving 3' to 5' away from the junction. Plays a
CC critical role in maintaining the integrity of the ribosomal DNA (rDNA)
CC loci, where it has a role in re-starting stalled replication forks. The
CC complex initiates homologous recombination (HR) events, used to
CC maintain rDNA copy number, in the rDNA repeats that are processed by a
CC mechanism that requires rad22, but not rhp51. It is also required for
CC suppression of methyl methanesulfonate (MMS) and UV-C irradiation
CC hypersensitivity of the structural maintenance of chromosome (SMC)
CC protein mutant, smc6-74, by overexpression of brc1. Has Holliday
CC junction resolvase activity in vitro. {ECO:0000255|HAMAP-Rule:MF_03100,
CC ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:15972456,
CC ECO:0000269|PubMed:16467377, ECO:0000269|PubMed:17277362,
CC ECO:0000269|PubMed:19596236}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03100,
CC ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:19596236};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03100,
CC ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:19596236};
CC Note=Divalent cation. Mg(2+) is preferred. Has Holliday junction
CC resolvase activity solely in the presence of Mn(2+).
CC {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:14528010,
CC ECO:0000269|PubMed:19596236};
CC -!- SUBUNIT: Forms a heterodimer with slx4. {ECO:0000255|HAMAP-
CC Rule:MF_03100}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14528010,
CC ECO:0000269|PubMed:16467377}. Note=Associates with chromatin at rDNA
CC repeat protrusions. {ECO:0000269|PubMed:14528010,
CC ECO:0000269|PubMed:16467377}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant provokes rDNA contraction.
CC Simultaneous elimination of slx1 and rqh1 is lethal.
CC {ECO:0000269|PubMed:14528010}.
CC -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03100}.
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DR EMBL; CU329670; CAB76036.1; -; Genomic_DNA.
DR RefSeq; NP_593420.1; NM_001018853.2.
DR PDB; 4ZDT; X-ray; 2.00 A; A/C=176-247.
DR PDBsum; 4ZDT; -.
DR AlphaFoldDB; Q9P7M3; -.
DR SMR; Q9P7M3; -.
DR BioGRID; 278153; 21.
DR STRING; 4896.SPAP27G11.15.1; -.
DR PaxDb; Q9P7M3; -.
DR PRIDE; Q9P7M3; -.
DR EnsemblFungi; SPAP27G11.15.1; SPAP27G11.15.1:pep; SPAP27G11.15.
DR GeneID; 2541657; -.
DR KEGG; spo:SPAP27G11.15; -.
DR PomBase; SPAP27G11.15; slx1.
DR VEuPathDB; FungiDB:SPAP27G11.15; -.
DR eggNOG; KOG3005; Eukaryota.
DR HOGENOM; CLU_030739_1_1_1; -.
DR InParanoid; Q9P7M3; -.
DR OMA; LQFEHAW; -.
DR PhylomeDB; Q9P7M3; -.
DR PRO; PR:Q9P7M3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030875; C:rDNA protrusion; IDA:PomBase.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IDA:PomBase.
DR GO; GO:0017108; F:5'-flap endonuclease activity; ISO:PomBase.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:PomBase.
DR GO; GO:1990238; F:double-stranded DNA endodeoxyribonuclease activity; IDA:PomBase.
DR GO; GO:0106332; F:ds/ssDNA junction-specific dsDNA endonuclease activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:PomBase.
DR GO; GO:0043007; P:maintenance of rDNA; IMP:PomBase.
DR GO; GO:0031297; P:replication fork processing; TAS:PomBase.
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 SUPFAM; SSF82771; SSF82771; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..271
FT /note="Structure-specific endonuclease subunit slx1"
FT /id="PRO_0000349133"
FT DOMAIN 5..87
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 180..231
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT MUTAGEN 34
FT /note="R->A: No endonuclease activity. Increases stalled
FT replication forks in the replication fork barrier (RFB) of
FT the rDNA and the amassing of X structures in rqh1 deletion
FT mutant."
FT /evidence="ECO:0000269|PubMed:14528010,
FT ECO:0000269|PubMed:16467377"
FT MUTAGEN 74
FT /note="E->A: No endonuclease activity."
FT /evidence="ECO:0000269|PubMed:14528010"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4ZDT"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4ZDT"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:4ZDT"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:4ZDT"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4ZDT"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4ZDT"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:4ZDT"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:4ZDT"
SQ SEQUENCE 271 AA; 31701 MW; A7B363ACC0FC7EF9 CRC64;
MDLCNFYCCY LLKSNRTQSS GAVYIGSTPD PPRRLRQHNG EIVGGASKTK HGRPWSISCL
VYGFPNKVSA LKFEWNWQNL GISRYTKDCD FRSKKQKTIM YCLKGLKHLV DSDTWRRWPL
NITFLNKTAF SKWNQLGKTY GNINVYFDEE WLNGFHEKVI QKTYDHKLCL RKTISEPVKC
NLCYECIESD ELRANCPFTD CNSINHLTCL ASSFLTEECQ VLPIEGMCTK CKRVLRWREF
LSTVFTTSLE TDERDFESEN RIEIIDLELE K
