ID   RAD55_SCHPO             Reviewed;         350 AA.
AC   O14129;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=DNA repair protein rhp55;
DE   AltName: Full=RAD55 homolog;
GN   Name=rhp55; ORFNames=SPAC3C7.03c;
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 [MRNA], AND FUNCTION.
RX   PubMed=10430583; DOI=10.1093/genetics/152.4.1557;
RA   Khasanov F.K., Savchenko G.V., Bashkirova E.V., Korolev V.G., Heyer W.-D.,
RA   Bashkirov V.I.;
RT   "A new recombinational DNA repair gene from Schizosaccharomyces pombe with
RT   homology to Escherichia coli RecA.";
RL   Genetics 152:1557-1572(1999).
RN   [2]
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).
CC   -!- FUNCTION: Required for radiation resistance and meiotic viability and
CC       acts in recombination and recombinational DNA repair pathways.
CC       {ECO:0000269|PubMed:10430583}.
CC   -!- INTERACTION:
CC       O14129; Q9UUL2: rhp57; NbExp=4; IntAct=EBI-1996748, EBI-1996765;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RecA family. RAD55 subfamily. {ECO:0000305}.
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DR   EMBL; AF053410; AAC17871.1; -; mRNA.
DR   EMBL; CU329670; CAB16734.1; -; Genomic_DNA.
DR   PIR; T43680; T43680.
DR   RefSeq; NP_593604.1; NM_001019035.2.
DR   AlphaFoldDB; O14129; -.
DR   SMR; O14129; -.
DR   BioGRID; 280099; 180.
DR   IntAct; O14129; 2.
DR   STRING; 4896.SPAC3C7.03c.1; -.
DR   MaxQB; O14129; -.
DR   PaxDb; O14129; -.
DR   EnsemblFungi; SPAC3C7.03c.1; SPAC3C7.03c.1:pep; SPAC3C7.03c.
DR   GeneID; 2543685; -.
DR   KEGG; spo:SPAC3C7.03c; -.
DR   PomBase; SPAC3C7.03c; -.
DR   VEuPathDB; FungiDB:SPAC3C7.03c; -.
DR   eggNOG; KOG1433; Eukaryota.
DR   HOGENOM; CLU_792632_0_0_1; -.
DR   InParanoid; O14129; -.
DR   OMA; TQMTSKV; -.
DR   PhylomeDB; O14129; -.
DR   PRO; PR:O14129; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; IBA:GO_Central.
DR   GO; GO:0033065; C:Rad51C-XRCC3 complex; IBA:GO_Central.
DR   GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR   GO; GO:0033062; C:Rhp55-Rhp57 complex; NAS:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISM:PomBase.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR   GO; GO:0000707; P:meiotic DNA recombinase assembly; IBA:GO_Central.
DR   GO; GO:0000709; P:meiotic joint molecule formation; TAS:PomBase.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR   GO; GO:0042148; P:strand invasion; TAS:PomBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA repair; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..350
FT                   /note="DNA repair protein rhp55"
FT                   /id="PRO_0000122955"
FT   REGION          331..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   350 AA;  38996 MW;  53DC65C0EC3836E1 CRC64;
     MLSSQHRLVT QPAIRAYEAF SAPGFGFNSK LLDDAFGGSG LKRGYISEVC GAPGMGKTSL
     ALQITANALL SGSRVIWVET CQPIPMERLR QLLDNHVPSS QDEEEKCDTD ELLNLLDVVY
     APNLVNILAF LRNFDQEKHL KEIGLLIIDN LSMPIQLAYP TSPEDYAYLR LRRNTSKKSS
     LSDSSQKENT LTLNKENEFS SKDDSNFAFH NSSTKTTINR RKKAIGTISS LLSKITSSCY
     VAIFVTTQMT SKVVSGIGAK LIPLLSTNWL DNLSYRLILY SRHSTEESKD GQSRPSHQLL
     RYAFMAKQPP AHSAESELAF QLTSTGIQDY QSIPTNSSQR RKRSILECES