RDH54_YEAST
ID RDH54_YEAST Reviewed; 958 AA.
AC P38086; D6VQ73;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=DNA repair and recombination protein RDH54;
DE AltName: Full=RAD homolog 54;
DE AltName: Full=Recombination factor TID1;
DE AltName: Full=Two hybrid interaction with DMC1 protein 1;
DE Includes:
DE RecName: Full=DNA topoisomerase;
DE EC=5.99.1.-;
DE Includes:
DE RecName: Full=Putative helicase;
DE EC=3.6.4.12;
GN Name=RDH54; Synonyms=TID1; OrderedLocusNames=YBR073W; ORFNames=YBR0715;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7985423; DOI=10.1002/yea.320100711;
RA van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M.,
RA Steensma H.Y.;
RT "Sequence analysis of a 31 kb DNA fragment from the right arm of
RT Saccharomyces cerevisiae chromosome II.";
RL Yeast 10:959-964(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 752.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INTERACTION WITH DMC1.
RX PubMed=9335591; DOI=10.1093/genetics/147.2.533;
RA Dresser M.E., Ewing D.J., Conrad M.N., Dominguez A.M., Barstead R.,
RA Jiang H., Kodadek T.;
RT "DMC1 functions in a Saccharomyces cerevisiae meiotic pathway that is
RT largely independent of the RAD51 pathway.";
RL Genetics 147:533-544(1997).
RN [5]
RP FUNCTION.
RX PubMed=9409819; DOI=10.1093/genetics/147.4.1533;
RA Klein H.L.;
RT "RDH54, a RAD54 homologue in Saccharomyces cerevisiae, is required for
RT mitotic diploid-specific recombination and repair and for meiosis.";
RL Genetics 147:1533-1543(1997).
RN [6]
RP FUNCTION.
RX PubMed=9409820; DOI=10.1093/genetics/147.4.1545;
RA Shinohara M., Shita-Yamaguchi E., Buerstedde J.-M., Shinagawa H., Ogawa H.,
RA Shinohara A.;
RT "Characterization of the roles of the Saccharomyces cerevisiae RAD54 gene
RT and a homologue of RAD54, RDH54/TID1, in mitosis and meiosis.";
RL Genetics 147:1545-1556(1997).
RN [7]
RP FUNCTION, ATPASE ACTIVITY, INTERACTION WITH RAD51, AND MUTAGENESIS OF
RP LYS-352.
RX PubMed=10970884; DOI=10.1101/gad.826100;
RA Petukhova G., Sung P., Klein H.;
RT "Promotion of Rad51-dependent D-loop formation by yeast recombination
RT factor Rdh54/Tid1.";
RL Genes Dev. 14:2206-2215(2000).
RN [8]
RP FUNCTION.
RX PubMed=11005857; DOI=10.1073/pnas.97.20.10814;
RA Shinohara M., Gasior S.L., Bishop D.K., Shinohara A.;
RT "Tid1/Rdh54 promotes colocalization of Rad51 and Dmc1 during meiotic
RT recombination.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10814-10819(2000).
RN [9]
RP FUNCTION.
RX PubMed=11470411; DOI=10.1016/s0960-9822(01)00296-2;
RA Lee S.E., Pellicioli A., Malkova A., Foiani M., Haber J.E.;
RT "The Saccharomyces recombination protein Tid1p is required for adaptation
RT from G2/M arrest induced by a double-strand break.";
RL Curr. Biol. 11:1053-1057(2001).
RN [10]
RP FUNCTION.
RX PubMed=12702674; DOI=10.1093/genetics/163.4.1273;
RA Shinohara M., Sakai K., Shinohara A., Bishop D.K.;
RT "Crossover interference in Saccharomyces cerevisiae requires a
RT TID1/RDH54- and DMC1-dependent pathway.";
RL Genetics 163:1273-1286(2003).
RN [11]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [17]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-649, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in the recombinational repair of double-strand
CC breaks (DSB) in DNA during mitosis and meiosis. Has DNA dependent
CC ATPase activity. Promotes D-loop (displacement loop) formation with
CC RAD51 recombinase. Modifies the topology of double-stranded DNA during
CC the D-loop reaction to facilitate the invasion of the homologous duplex
CC molecule by the initiating single-stranded DNA substrate. Required for
CC adaptation from G2/M checkpoint arrest induced by a double strand
CC break, by participating in monitoring the extent of single-stranded DNA
CC produced by resection of DNA ends. This role is distinct from its roles
CC in recombination. Promotes colocalization of RAD51 and DMC1 during
CC meiotic recombination. Involved in crossover interference.
CC {ECO:0000269|PubMed:10970884, ECO:0000269|PubMed:11005857,
CC ECO:0000269|PubMed:11470411, ECO:0000269|PubMed:12702674,
CC ECO:0000269|PubMed:9409819, ECO:0000269|PubMed:9409820}.
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 RAD51 and DMC1. {ECO:0000269|PubMed:10970884,
CC ECO:0000269|PubMed:9335591}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator. In
CC many S.cerevisiae strains, it is not possible to extend the sequence at
CC the N-terminus beyond Met-35 because of a frameshift in the upstream
CC sequence when compared to strain S288c. However, experimental evidence
CC indicates that the longer protein is made in S288c. {ECO:0000305}.
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DR EMBL; X76294; CAA53930.1; -; Genomic_DNA.
DR EMBL; Z35942; CAA85017.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07193.2; -; Genomic_DNA.
DR PIR; S45466; S45466.
DR RefSeq; NP_009629.6; NM_001178421.4.
DR AlphaFoldDB; P38086; -.
DR SMR; P38086; -.
DR BioGRID; 32776; 139.
DR DIP; DIP-792N; -.
DR IntAct; P38086; 4.
DR MINT; P38086; -.
DR STRING; 4932.YBR073W; -.
DR CarbonylDB; P38086; -.
DR iPTMnet; P38086; -.
DR MaxQB; P38086; -.
DR PaxDb; P38086; -.
DR PRIDE; P38086; -.
DR EnsemblFungi; YBR073W_mRNA; YBR073W; YBR073W.
DR GeneID; 852365; -.
DR KEGG; sce:YBR073W; -.
DR SGD; S000000277; RDH54.
DR VEuPathDB; FungiDB:YBR073W; -.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156966; -.
DR HOGENOM; CLU_000315_10_1_1; -.
DR InParanoid; P38086; -.
DR OMA; FTIMYRK; -.
DR BioCyc; YEAST:G3O-29042-MON; -.
DR PRO; PR:P38086; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38086; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:SGD.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003916; F:DNA topoisomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0015616; F:DNA translocase activity; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:SGD.
DR GO; GO:0032392; P:DNA geometric change; IDA:SGD.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0030491; P:heteroduplex formation; IDA:SGD.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
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; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Isomerase; Isopeptide bond; Meiosis;
KW Nucleotide-binding; Nucleus; Reference proteome; Topoisomerase;
KW Ubl conjugation.
FT CHAIN 1..958
FT /note="DNA repair and recombination protein RDH54"
FT /id="PRO_0000074346"
FT DOMAIN 333..521
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 665..824
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 189..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 506..509
FT /note="DEGH box"
FT BINDING 380..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 352
FT /note="K->R: 1%-2% of the ATPase activity."
FT /evidence="ECO:0000269|PubMed:10970884"
FT CONFLICT 752
FT /note="A -> R (in Ref. 1; CAA53930 and 2; CAA85017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 958 AA; 107946 MW; B797375C08FA14FA CRC64;
MAVISVKPRR REKILQEVKN SSVYQTVFDS GTTQMQIPKY ENKPFKPPRR VGSNKYTQLK
PTATAVTTAP ISKAKVTVNL KRSISAGPTL NLAKKPNNLS SNENTRYFTI MYRKPTTKKH
KTWSGDGYAT LKASSDKLCF YNEAGKFLGS SMLPSDSDSL FETLFKAGSN EVQLDYELKE
NAEIRSAKEA LSQNMGNPSP PTTSTTETVP STKNDGGKYQ MPLSQLFSLN TVKRFKSVTK
QTNEHMTTVP KTSQNSKAKK YYPVFDVNKI DNPIVMNKNA AAEVDVIVDP LLGKFLRPHQ
REGVKFMYDC LMGLARPTIE NPDIDCTTKS LVLENDSDIS GCLLADDMGL GKTLMSITLI
WTLIRQTPFA SKVSCSQSGI PLTGLCKKIL VVCPVTLIGN WKREFGKWLN LSRIGVLTLS
SRNSPDMDKM AVRNFLKVQR TYQVLIIGYE KLLSVSEELE KNKHLIDMLV CDEGHRLKNG
ASKILNTLKS LDIRRKLLLT GTPIQNDLNE FFTIIDFINP GILGSFASFK RRFIIPITRA
RDTANRYNEE LLEKGEERSK EMIEITKRFI LRRTNAILEK YLPPKTDIIL FCKPYSQQIL
AFKDILQGAR LDFGQLTFSS SLGLITLLKK VCNSPGLVGS DPYYKSHIKD TQSQDSYSRS
LNSGKLKVLM TLLEGIRKGT KEKVVVVSNY TQTLDIIENL MNMAGMSHCR LDGSIPAKQR
DSIVTSFNRN PAIFGFLLSA KSGGVGLNLV GASRLILFDN DWNPSVDLQA MSRIHRDGQK
KPCFIYRLVT TGCIDEKILQ RQLMKNSLSQ KFLGDSEMRN KESSNDDLFN KEDLKDLFSV
HTDTKSNTHD LICSCDGLGE EIEYPETNQQ QNTVELRKRS TTTWTSALDL QKKMNEAATN
DDAKKSQYIR QCLVHYKHID PARQDELFDE VITDSFTELK DSITFAFVKP GEICLREQ
