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Database: UniProt
Entry: P38086
LinkDB: P38086
Original site: P38086 
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   16-OCT-2019, entry version 178.
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;
GN   ORFNames=YBR0715;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA   Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA   Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA   Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA   Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA   Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA   Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA   Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA   Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA   Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA   van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA   Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA   Zagulski M., Zimmermann F.K., 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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   INTERACTION WITH DMC1.
RX   PubMed=9335591;
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;
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;
RA   Shinohara M., Shita-Yamaguchi E., Buerstedde J.-M., Shinagawa H.,
RA   Ogawa H., Shinohara A.;
RT   "Characterization of the roles of the Saccharomyces cerevisiae RAD54
RT   gene 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
RT   adaptation from G2/M arrest induced by a double-strand break.";
RL   Curr. Biol. 11:1053-1057(2001).
RN   [10]
RP   FUNCTION.
RX   PubMed=12702674;
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.,
RA   Dephoure N., 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.,
RA   Majors J., 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
RT   phosphoproteome 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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [17]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-649, AND IDENTIFICATION
RP   BY 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
CC       with RAD51 recombinase. Modifies the topology of double-stranded
CC       DNA during the D-loop reaction to facilitate the invasion of the
CC       homologous duplex molecule by the initiating single-stranded DNA
CC       substrate. Required for adaptation from G2/M checkpoint arrest
CC       induced by a double strand break, by participating in monitoring
CC       the extent of single-stranded DNA produced by resection of DNA
CC       ends. This role is distinct from its roles in recombination.
CC       Promotes colocalization of RAD51 and DMC1 during meiotic
CC       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.
CC       {ECO:0000269|PubMed:10970884, ECO:0000269|PubMed:9335591}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator.
CC       In many S.cerevisiae strains, it is not possible to extend the
CC       sequence at the N-terminus beyond Met-35 because of a frameshift
CC       in the upstream sequence when compared to strain S288c. However,
CC       experimental evidence indicates that the longer protein is made in
CC       S288c. {ECO:0000305}.
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   BioGrid; 32776; 114.
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   EuPathDB; FungiDB:YBR073W; -.
DR   SGD; S000000277; RDH54.
DR   HOGENOM; HOG000204521; -.
DR   InParanoid; P38086; -.
DR   KO; K10877; -.
DR   OMA; FTIMYRK; -.
DR   BioCyc; YEAST:G3O-29042-MONOMER; -.
DR   PRO; PR:P38086; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0008094; F:DNA-dependent ATPase 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   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_N; 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; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA-binding; Helicase; Hydrolase; Isomerase;
KW   Isopeptide bond; Meiosis; Nucleotide-binding; Nucleus;
KW   Reference proteome; Topoisomerase; Ubl conjugation.
FT   CHAIN         1    958       DNA repair and recombination protein
FT                                RDH54.
FT                                /FTId=PRO_0000074346.
FT   DOMAIN      333    521       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      665    824       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     380    387       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       506    509       DEGH box.
FT   CROSSLNK    649    649       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000244|PubMed:22106047}.
FT   MUTAGEN     352    352       K->R: 1%-2% of the ATPase activity.
FT                                {ECO:0000269|PubMed:10970884}.
FT   CONFLICT    752    752       A -> R (in Ref. 1; CAA53930 and 2;
FT                                CAA85017). {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
//
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