RAD51_SCHPO
ID RAD51_SCHPO Reviewed; 365 AA.
AC P36601;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=DNA repair protein rhp51;
DE AltName: Full=RAD51 homolog;
GN Name=rhp51; Synonyms=rad51; ORFNames=SPAC644.14c;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8358431; DOI=10.1038/ng0793-239;
RA Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T.;
RT "Cloning of human, mouse and fission yeast recombination genes homologous
RT to RAD51 and recA.";
RL Nat. Genet. 4:239-243(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8233794; DOI=10.1093/nar/21.19.4586;
RA Muris D.F.R., Vreeken K., Carr A.M., Broughton B.C., Lehmann A.R.,
RA Lohman P.H.M., Pastink A.;
RT "Cloning the RAD51 homologue of Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 21:4586-4591(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8194753; DOI=10.1016/0378-1119(94)90262-3;
RA Jang Y.K., Jin Y.H., Kim E.M., Hong S.H., Fabre F., Park S.D.;
RT "Cloning and sequence analysis of rhp51+, a Schizosaccharomyces pombe
RT homolog of the Saccharomyces cerevisiae RAD51 gene.";
RL Gene 142:207-211(1994).
RN [4]
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 [5]
RP HOMODIMERIZATION, AND INTERACTION WITH RAD22; RAD54; RDH54; RHP54 AND RTI1.
RX PubMed=14551247; DOI=10.1091/mbc.e03-05-0288;
RA Catlett M.G., Forsburg S.L.;
RT "Schizosaccharomyces pombe Rdh54 (TID1) acts with Rhp54 (RAD54) to repair
RT meiotic double-strand breaks.";
RL Mol. Biol. Cell 14:4707-4720(2003).
RN [6]
RP INTERACTION WITH SWI2 AND SWI5.
RX PubMed=14663140; DOI=10.1073/pnas.2632890100;
RA Akamatsu Y., Dziadkowiec D., Ikeguchi M., Shinagawa H., Iwasaki H.;
RT "Two different Swi5-containing protein complexes are involved in mating-
RT type switching and recombination repair in fission yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15770-15775(2003).
RN [7]
RP FUNCTION, AND HOMOOLIGOMERIZATION.
RX PubMed=15899844; DOI=10.1128/mcb.25.11.4377-4387.2005;
RA Sauvageau S., Stasiak A.Z., Banville I., Ploquin M., Stasiak A.,
RA Masson J.-Y.;
RT "Fission yeast rad51 and dmc1, two efficient DNA recombinases forming
RT helical nucleoprotein filaments.";
RL Mol. Cell. Biol. 25:4377-4387(2005).
CC -!- FUNCTION: Required both for recombination and for the repair of DNA
CC damage caused by X-rays. Binds to single and double-stranded DNA, in
CC the presence of magnesium, and exhibits DNA-dependent ATPase activity.
CC Promotes DNA strand annealing and strand exchange via DNA recombinase
CC activity and forms helical nucleoprotein filaments.
CC {ECO:0000269|PubMed:15899844}.
CC -!- SUBUNIT: Interacts with rad22, rad54, rdh54, rhp54, rti1, swi2 and
CC swi5. Forms homooiligomers. {ECO:0000269|PubMed:14551247,
CC ECO:0000269|PubMed:14663140}.
CC -!- INTERACTION:
CC P36601; P36592: rad22; NbExp=5; IntAct=EBI-926960, EBI-966242;
CC P36601; P36601: rhp51; NbExp=7; IntAct=EBI-926960, EBI-926960;
CC P36601; P41410: rhp54; NbExp=3; IntAct=EBI-926960, EBI-1167415;
CC P36601; O42905: rti1; NbExp=3; IntAct=EBI-926960, EBI-1167500;
CC P36601; Q9USV1: sfr1; NbExp=6; IntAct=EBI-926960, EBI-927233;
CC P36601; Q10668: swi2; NbExp=3; IntAct=EBI-926960, EBI-926914;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA80878.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D13805; BAA02963.1; -; Genomic_DNA.
DR EMBL; Z22691; CAA80399.1; -; Genomic_DNA.
DR EMBL; Z24756; CAA80879.1; -; Genomic_DNA.
DR EMBL; Z24756; CAA80878.1; ALT_INIT; Genomic_DNA.
DR EMBL; CU329670; CAB90141.1; -; Genomic_DNA.
DR PIR; S42107; S42107.
DR RefSeq; NP_593882.1; NM_001019312.2.
DR AlphaFoldDB; P36601; -.
DR SMR; P36601; -.
DR DIP; DIP-29235N; -.
DR IntAct; P36601; 21.
DR MINT; P36601; -.
DR STRING; 4896.SPAC644.14c.1; -.
DR MaxQB; P36601; -.
DR PaxDb; P36601; -.
DR GeneID; 2543580; -.
DR KEGG; spo:SPAC644.14c; -.
DR PomBase; SPAC644.14c; -.
DR eggNOG; KOG1433; Eukaryota.
DR HOGENOM; CLU_041732_0_0_1; -.
DR InParanoid; P36601; -.
DR PhylomeDB; P36601; -.
DR Reactome; R-SPO-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR PRO; PR:P36601; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:1905334; F:Swi5-Sfr1 complex binding; IDA:PomBase.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; IDA:UniProtKB.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:PomBase.
DR GO; GO:0007533; P:mating type switching; IGI:PomBase.
DR GO; GO:0000708; P:meiotic strand invasion; IDA:PomBase.
DR GO; GO:0006312; P:mitotic recombination; IGI:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0110027; P:negative regulation of DNA strand resection involved in replication fork processing; EXP:PomBase.
DR GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR GO; GO:0042148; P:strand invasion; IDA:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IGI:PomBase.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02239; recomb_RAD51; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Magnesium; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..365
FT /note="DNA repair protein rhp51"
FT /id="PRO_0000122924"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 15
FT /note="T -> M (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 39823 MW; 9F26EB9FA4F3C2BA CRC64;
MADTEVEMQV SAADTNNNEN GQAQSNYEYD VNVQDEEDEA AAGPMPLQML EGNGITASDI
KKIHEAGYYT VESIAYTPKR QLLLIKGISE AKADKLLGEA SKLVPMGFTT ATEYHIRRSE
LITITTGSKQ LDTLLQGGVE TGSITELFGE FRTGKSQICH TLAVTCQLPI DMGGGEGKCL
YIDTEGTFRP VRLLAVADRY GLNGEEVLDN VAYARAYNAD HQLELLQQAA NMMSESRFSL
LVVDSCTALY RTDFSGRGEL SARQMHLARF MRTLQRLADE FGIAVVITNQ VVAQVDGISF
NPDPKKPIGG NILAHSSTTR LSLRKGRGEQ RICKIYDSPC LPESEAIFAI NSDGVGDPKE
IIAPV
