RDH54_SCHPO
ID RDH54_SCHPO Reviewed; 811 AA.
AC Q09772; Q7ZA42;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Meiotic recombination protein rdh54;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase rdh54;
DE AltName: Full=Meiotically up-regulated gene 34 protein;
DE AltName: Full=RAD54 protein homolog 2;
GN Name=rdh54; Synonyms=mug34, tid1; ORFNames=SPAC22F3.03c;
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], FUNCTION, AND INTERACTION WITH DMC1 AND RHP51.
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 [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).
RN [3]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Acts with rhp54 to repair meiotic double strand breaks via
CC homologous recombination. Involved in meiotic DNA recombination.
CC {ECO:0000269|PubMed:14551247, ECO:0000269|PubMed:16303567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts with dmc1 and rhp51. {ECO:0000269|PubMed:14551247}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AY293737; AAP44116.1; -; mRNA.
DR EMBL; CU329670; CAA91068.3; -; Genomic_DNA.
DR PIR; S62418; S62418.
DR PIR; T38188; T38188.
DR RefSeq; NP_593038.2; NM_001018437.2.
DR AlphaFoldDB; Q09772; -.
DR SMR; Q09772; -.
DR BioGRID; 278289; 23.
DR IntAct; Q09772; 2.
DR STRING; 4896.SPAC22F3.03c.1; -.
DR iPTMnet; Q09772; -.
DR PaxDb; Q09772; -.
DR PRIDE; Q09772; -.
DR EnsemblFungi; SPAC22F3.03c.1; SPAC22F3.03c.1:pep; SPAC22F3.03c.
DR GeneID; 2541798; -.
DR KEGG; spo:SPAC22F3.03c; -.
DR PomBase; SPAC22F3.03c; rdh54.
DR VEuPathDB; FungiDB:SPAC22F3.03c; -.
DR eggNOG; KOG0390; Eukaryota.
DR HOGENOM; CLU_000315_10_1_1; -.
DR InParanoid; Q09772; -.
DR OMA; QFLYECV; -.
DR PhylomeDB; Q09772; -.
DR PRO; PR:Q09772; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IC:PomBase.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:PomBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IDA:PomBase.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR018838; DUF2439.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF10382; DUF2439; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..811
FT /note="Meiotic recombination protein rdh54"
FT /id="PRO_0000074345"
FT DOMAIN 222..391
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 540..693
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 20..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 811 AA; 92965 MW; C5C88292A8E93604 CRC64;
MKRRATFQCP LIESTIKHQS TNYTKTETAT TSHEVSENAN EHKGKSNIDI NKIAYYNVVW
RKITMKKHKT WEGDGFLVRE DSNLTLYNSD FTRLGSCHSR VPQIKEGELL RISGKEISIE
KEISAESYEA GTHIDDSLRD VHMPEMKRKF KPPLRPNTMY QTISALPKPR HDPTVLGALV
MSRPKTWDPR THVDVVIDPF LSKHLYSHQR EGVSFLYDCL LGMEGKCGYS AILADEMGLG
KTLQTITVVW TLLKQSYYAN RSSTINNAMV VAPVTLLKNW ENEFYNWLGH ERIHVYIARC
AEDFQEFTSN KTYSIIITGY ETVCTYLRNY GCGIDIDLLI CDEAHRLKSM SSQTWITLNK
LKTRKRLLLT GTPLQNDLSE YFSMVNFIIP GSLGTPNSFK AQYERPILRS RSMNASSRDI
SLGAARLQRL FEFTSNFTLR RKANILAKHL PPRTDIVLFI KPTHQQENVY GHVLDGFKSS
VDQKGYYLKI LTRLSKICNS TILLRNEKEN FLSTELQDKH VFEQENMLLS SSKLQILAAL
LKSFQRGCQK AVIVSQYKET LELIELFLSI LHVRFCKLLG STPFSERDLI VHNFNTSSFK
EFSVLLLSSK AGGCGLNLTG STRLIIYEPS WNPAQDLQAL SRIYRSGQKR PVCIYTFLSS
GMLDERIFIR QNTKQGLSSS FIDSDASQKK NFFTGEDIKT LFSYSKTETC LTYELAFDSD
EIDSLTKKKD PLTKIDHTID SPNTKEKDKE ISSWKKASEY MDTNLGKKCP ENAFQGWTWQ
FPNDLSIMNG VEDYIPLEPL PINCLMHKKF E
