RAD54_YEAST
ID RAD54_YEAST Reviewed; 898 AA.
AC P32863; D6VTY8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=DNA repair and recombination protein RAD54;
DE EC=3.6.4.12 {ECO:0000269|PubMed:32502392};
GN Name=RAD54; OrderedLocusNames=YGL163C; ORFNames=G1821;
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].
RX PubMed=1916269; DOI=10.1016/0378-1119(91)90473-o;
RA Emery H.S., Schild D., Kellogg D.E., Mortimer R.K.;
RT "Sequence of RAD54, a Saccharomyces cerevisiae gene involved in
RT recombination and repair.";
RL Gene 104:103-106(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
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 [5]
RP CELL CYCLE REGULATION.
RX PubMed=7610042; DOI=10.1093/nar/23.12.2147;
RA Johnston L.H., Johnson A.L.;
RT "The DNA repair genes RAD54 and UNG1 are cell cycle regulated in budding
RT yeast but MCB promoter elements have no essential role in the DNA damage
RT response.";
RL Nucleic Acids Res. 23:2147-2152(1995).
RN [6]
RP INTERACTION WITH RAD51.
RX PubMed=9590697; DOI=10.1038/30037;
RA Petukhova G., Stratton S., Sung P.;
RT "Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins.";
RL Nature 393:91-94(1998).
RN [7]
RP FUNCTION.
RX PubMed=12453424; DOI=10.1016/s1097-2765(02)00743-8;
RA Solinger J.A., Kiianitsa K., Heyer W.-D.;
RT "Rad54, a Swi2/Snf2-like recombinational repair protein, disassembles
RT Rad51:dsDNA filaments.";
RL Mol. Cell 10:1175-1188(2002).
RN [8]
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 [9]
RP FUNCTION, MUTAGENESIS OF LYS-341, AND INTERACTION WITH RAD51.
RX PubMed=31492866; DOI=10.1038/s41467-019-12082-z;
RA Tavares E.M., Wright W.D., Heyer W.D., Le Cam E., Dupaigne P.;
RT "In vitro role of Rad54 in Rad51-ssDNA filament-dependent homology search
RT and synaptic complexes formation.";
RL Nat. Commun. 10:4058-4058(2019).
RN [10]
RP FUNCTION, MUTAGENESIS OF LYS-341, AND CATALYTIC ACTIVITY.
RX PubMed=32502392; DOI=10.1016/j.cell.2020.04.056;
RA Crickard J.B., Moevus C.J., Kwon Y., Sung P., Greene E.C.;
RT "Rad54 Drives ATP Hydrolysis-Dependent DNA Sequence Alignment during
RT Homologous Recombination.";
RL Cell 181:1380-1394.e18(2020).
CC -!- FUNCTION: Plays an essential role in homologous recombination (HR)
CC which is a major pathway for repairing DNA double-strand breaks (DSBs),
CC single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication
CC forks (PubMed:12453424). Acts as a molecular motor during the homology
CC search and guides RAD51 ssDNA along a donor dsDNA thereby changing the
CC homology search from the diffusion-based mechanism to a motor-guided
CC mechanism (PubMed:32502392). Also plays an essential role in RAD51-
CC mediated synaptic complex formation which consists of three strands
CC encased in a protein filament formed once homology is recognized
CC (PubMed:31492866). Once DNA strand exchange occured, dissociates RAD51
CC from nucleoprotein filaments formed on dsDNA (PubMed:12453424).
CC {ECO:0000269|PubMed:12453424, ECO:0000269|PubMed:31492866,
CC ECO:0000269|PubMed:32502392}.
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 Evidence={ECO:0000269|PubMed:32502392};
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts with RAD51; RAD51-ssDNA
CC filaments do not interact autonomously with dsDNA but do so robustly in
CC the presence of RAD54 (PubMed:9590697, PubMed:31492866).
CC {ECO:0000250|UniProtKB:Q7ZV09, ECO:0000269|PubMed:31492866,
CC ECO:0000269|PubMed:9590697}.
CC -!- INTERACTION:
CC P32863; P25454: RAD51; NbExp=2; IntAct=EBI-14728, EBI-14709;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: Expression increases in late G1 phase compared to other
CC phases of the cell cycle.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; M63232; AAA34949.1; -; Genomic_DNA.
DR EMBL; Z48618; CAA88534.1; -; Genomic_DNA.
DR EMBL; Z72685; CAA96875.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07949.1; -; Genomic_DNA.
DR PIR; JH0440; JH0440.
DR RefSeq; NP_011352.1; NM_001181028.1.
DR AlphaFoldDB; P32863; -.
DR SMR; P32863; -.
DR BioGRID; 33090; 306.
DR DIP; DIP-509N; -.
DR IntAct; P32863; 29.
DR MINT; P32863; -.
DR STRING; 4932.YGL163C; -.
DR iPTMnet; P32863; -.
DR PaxDb; P32863; -.
DR PRIDE; P32863; -.
DR EnsemblFungi; YGL163C_mRNA; YGL163C; YGL163C.
DR GeneID; 852713; -.
DR KEGG; sce:YGL163C; -.
DR SGD; S000003131; RAD54.
DR VEuPathDB; FungiDB:YGL163C; -.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156897; -.
DR HOGENOM; CLU_000315_10_2_1; -.
DR InParanoid; P32863; -.
DR OMA; YTEHERM; -.
DR BioCyc; YEAST:G3O-30652-MON; -.
DR PRO; PR:P32863; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32863; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IMP:SGD.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0032392; P:DNA geometric change; IDA:SGD.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0030491; P:heteroduplex formation; IDA:SGD.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013967; Rad54_N.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08658; Rad54_N; 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 repair; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..898
FT /note="DNA repair and recombination protein RAD54"
FT /id="PRO_0000074344"
FT DOMAIN 322..504
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 659..812
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 21..25
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 41..45
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 455..458
FT /note="DEGH box"
FT COMPBIAS 188..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 341
FT /note="K->R: Complete loss of ability to support homology
FT search."
FT /evidence="ECO:0000269|PubMed:31492866,
FT ECO:0000269|PubMed:32502392"
SQ SEQUENCE 898 AA; 101754 MW; 2EC0A9B7E3D66292 CRC64;
MARRRLPDRP PNGIGAGERP RLVPRPINVQ DSVNRLTKPF RVPYKNTHIP PAAGRIATGS
DNIVGGRSLR KRSATVCYSG LDINADEAEY NSQDISFSQL TKRRKDALSA QRLAKDPTRL
SHIQYTLRRS FTVPIKGYVQ RHSLPLTLGM KKKITPEPRP LHDPTDEFAI VLYDPSVDGE
MIVHDTSMDN KEEESKKMIK STQEKDNINK EKNSQEERPT QRIGRHPALM TNGVRNKPLR
ELLGDSENSA ENKKKFASVP VVIDPKLAKI LRPHQVEGVR FLYRCVTGLV MKDYLEAEAF
NTSSEDPLKS DEKALTESQK TEQNNRGAYG CIMADEMGLG KTLQCIALMW TLLRQGPQGK
RLIDKCIIVC PSSLVNNWAN ELIKWLGPNT LTPLAVDGKK SSMGGGNTTV SQAIHAWAQA
QGRNIVKPVL IISYETLRRN VDQLKNCNVG LMLADEGHRL KNGDSLTFTA LDSISCPRRV
ILSGTPIQND LSEYFALLSF SNPGLLGSRA EFRKNFENPI LRGRDADATD KEITKGEAQL
QKLSTIVSKF IIRRTNDILA KYLPCKYEHV IFVNLKPLQN ELYNKLIKSR EVKKVVKGVG
GSQPLRAIGI LKKLCNHPNL LNFEDEFDDE DDLELPDDYN MPGSKARDVQ TKYSAKFSIL
ERFLHKIKTE SDDKIVLISN YTQTLDLIEK MCRYKHYSAV RLDGTMSINK RQKLVDRFND
PEGQEFIFLL SSKAGGCGIN LIGANRLILM DPDWNPAADQ QALARVWRDG QKKDCFIYRF
ISTGTIEEKI FQRQSMKMSL SSCVVDAKED VERLFSSDNL RQLFQKNENT ICETHETYHC
KRCNAQGKQL KRAPAMLYGD ATTWNHLNHD ALEKTNDHLL KNEHHYNDIS FAFQYISH
