ID   RAD57_SCHPO             Reviewed;         354 AA.
AC   Q9UUL2; Q9P7A6;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=DNA repair protein rhp57;
DE   AltName: Full=RAD57 homolog;
GN   Name=rhp57; ORFNames=SPAC145.01, SPAC20H4.07;
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], AND FUNCTION.
RX   PubMed=10747044; DOI=10.1093/genetics/154.4.1451;
RA   Tsutsui Y., Morishita T., Iwasaki H., Toh H., Shinagawa H.;
RT   "A recombination repair gene of Schizosaccharomyces pombe, rhp57, is a
RT   functional homolog of the Saccharomyces cerevisiae RAD57 gene and is
RT   phylogenetically related to the human XRCC3 gene.";
RL   Genetics 154:1451-1461(2000).
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: Involved in recombination DNA repair and in the repair of
CC       gamma-ray-induced damage. {ECO:0000269|PubMed:10747044}.
CC   -!- INTERACTION:
CC       Q9UUL2; O14129: rhp55; NbExp=4; IntAct=EBI-1996765, EBI-1996748;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000305}.
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DR   EMBL; AB024744; BAA83768.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAC19737.1; -; Genomic_DNA.
DR   PIR; T43507; T43507.
DR   RefSeq; NP_593627.1; NM_001019058.2.
DR   AlphaFoldDB; Q9UUL2; -.
DR   SMR; Q9UUL2; -.
DR   BioGRID; 278490; 237.
DR   IntAct; Q9UUL2; 3.
DR   STRING; 4896.SPAC20H4.07.1; -.
DR   PaxDb; Q9UUL2; -.
DR   PRIDE; Q9UUL2; -.
DR   EnsemblFungi; SPAC20H4.07.1; SPAC20H4.07.1:pep; SPAC20H4.07.
DR   GeneID; 2542007; -.
DR   KEGG; spo:SPAC20H4.07; -.
DR   PomBase; SPAC20H4.07; -.
DR   VEuPathDB; FungiDB:SPAC20H4.07; -.
DR   eggNOG; KOG1564; Eukaryota.
DR   HOGENOM; CLU_013059_0_0_1; -.
DR   InParanoid; Q9UUL2; -.
DR   OMA; PCLGLQW; -.
DR   PhylomeDB; Q9UUL2; -.
DR   PRO; PR:Q9UUL2; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0000150; F:DNA strand exchange activity; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0000730; P:DNA recombinase assembly; IMP:PomBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:PomBase.
DR   GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR   GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR   CDD; cd01123; Rad51_DMC1_radA; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR   InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033925; Rad51_DMC1_RadA.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   Pfam; PF08423; Rad51; 1.
DR   PIRSF; PIRSF005856; Rad51; 1.
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..354
FT                   /note="DNA repair protein rhp57"
FT                   /id="PRO_0000122957"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  39731 MW;  40131E247A087DB0 CRC64;
     MDISNYVDNF YFDEKIASAF ELGEVSTVDL LTLDITELER RTHCSQSELL QLIEQISLLL
     QPVRCSASKV TSKYLTTGDV KLDETLHGGI PVGQLTEICG ESGSGKSQFC MQLCLMVQLP
     LSLGGMNKAA VFISTESGLE TKRLFELARY LPERYPKADK KDIIIKNPGD RVYTILCPDL
     ESQEHIIQYQ LPILFNRDKI GLVILDSVAS NYRAELRYNR SKSHFRDLDN IAKRGNQLGK
     LAMTLRTLAH QHEAAVVIAN QVSDRIPRDY DAIGLFSLDY QSQWFSGWDD TDPNPKIPSL
     GLVWTNNIST RLALIKKTDS ATNNSGRIFR VVYSPNSPRL DVRICIGSVG IYSC