RAD54_DANRE
ID RAD54_DANRE Reviewed; 738 AA.
AC F1Q8K0; Q7ZV09;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=DNA repair and recombination protein RAD54-like;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q7ZV09};
GN Name=rad54l;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT SER-566 AND SER-567, SUBUNIT, FUNCTION, AND INTERACTION
RP WITH RAD51.
RX PubMed=30961891; DOI=10.1016/j.bpj.2019.03.001;
RA Lengert N., Spies J., Drossel B.;
RT "Rad54 Phosphorylation Promotes Homologous Recombination by Balancing Rad54
RT Mobility and DNA Binding.";
RL Biophys. J. 116:1406-1419(2019).
RN [4] {ECO:0007744|PDB:1Z3I}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 92-735.
RX PubMed=15806108; DOI=10.1038/nsmb919;
RA Thoma N.H., Czyzewski B.K., Alexeev A.A., Mazin A.V., Kowalczykowski S.C.,
RA Pavletich N.P.;
RT "Structure of the SWI2/SNF2 chromatin-remodeling domain of eukaryotic
RT Rad54.";
RL Nat. Struct. Mol. Biol. 12:350-356(2005).
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:30961891). 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. Also plays an essential role in RAD51-mediated synaptic
CC complex formation which consists of three strands encased in a protein
CC filament formed once homology is recognized. Once DNA strand exchange
CC occured, dissociates RAD51 from nucleoprotein filaments formed on dsDNA
CC (By similarity). {ECO:0000250|UniProtKB:P32863,
CC ECO:0000269|PubMed:30961891}.
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:0000250|UniProtKB:P32863};
CC -!- SUBUNIT: Homohexamer (PubMed:30961891). Interacts with RAD51
CC (PubMed:30961891). {ECO:0000269|PubMed:30961891}.
CC -!- PTM: Phosphorylated. Phosphorylations at Ser-566 and Ser-567 allow
CC efficient removal of RAD51 filaments from DNA.
CC {ECO:0000269|PubMed:30961891}.
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DR EMBL; CU499314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU693449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046050; AAH46050.1; -; mRNA.
DR RefSeq; NP_957438.1; NM_201144.1.
DR PDB; 1Z3I; X-ray; 3.00 A; X=92-735.
DR PDBsum; 1Z3I; -.
DR AlphaFoldDB; F1Q8K0; -.
DR SMR; F1Q8K0; -.
DR STRING; 7955.ENSDARP00000007237; -.
DR PaxDb; F1Q8K0; -.
DR Ensembl; ENSDART00000011785; ENSDARP00000007237; ENSDARG00000018623.
DR GeneID; 394119; -.
DR KEGG; dre:394119; -.
DR CTD; 8438; -.
DR ZFIN; ZDB-GENE-040426-968; rad54l.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156897; -.
DR HOGENOM; CLU_000315_10_2_1; -.
DR InParanoid; F1Q8K0; -.
DR OMA; YTEHERM; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; F1Q8K0; -.
DR TreeFam; TF101224; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000018623; Expressed in testis and 23 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:ZFIN.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISS:ZFIN.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
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; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
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 3D-structure; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..738
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000451560"
FT DOMAIN 164..339
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 493..647
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 290..293
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30961891"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30961891"
FT CONFLICT 33
FT /note="C -> S (in Ref. 2; AAH46050)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="F -> V (in Ref. 2; AAH46050)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="V -> A (in Ref. 2; AAH46050)"
FT /evidence="ECO:0000305"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:1Z3I"
FT TURN 276..281
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 366..385
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 438..452
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 455..463
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 490..505
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 509..515
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 517..530
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 543..554
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 562..566
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 579..584
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 591..598
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 610..617
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 621..634
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 652..658
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 668..673
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 700..706
FT /evidence="ECO:0007829|PDB:1Z3I"
FT HELIX 712..717
FT /evidence="ECO:0007829|PDB:1Z3I"
FT STRAND 722..731
FT /evidence="ECO:0007829|PDB:1Z3I"
SQ SEQUENCE 738 AA; 83737 MW; 278FD71A5A99478A CRC64;
MRRSLAPSQV AKRKQGPDSD DEEDWEPDME PQCKRDCREK YISPYRKPLT PLTNRPFCAD
GNEHEAFIRK ILSKPFKIPI PNYTGVLGLR ALGLRRAGVR KALHDPFEDG ALVLYEPPVI
SAHDLIKADK EKLPVHVVVD PVLSKVLRPH QREGVKFLWD CVTGRRIENS YGCIMADEMG
LGKTLQCITL IWTLLKQSPD CKPEIDKVIV VSPSSLVRNW YNEVGKWLGG RVQPVAIDGG
SKDEIDSKLV NFISQQGMRI PTPILIISYE TFRLHAEVLH KGKVGLVICD EGHRLKNSDN
QTYLALNSMN AQRRVLISGT PIQNDLLEYF SLVHFVNSGI LGTAQEFKKR FEIPILKGRD
ADASDKDRAA GEQKLQELIS IVNRCLIRRT SDILSKYLPV KIEQVVCCNL TPLQKELYKL
FLKQAKPVES LQTGKISVSS LSSITSLKKL CNHPALIYEK CLTGEEGFDG ALDLFPQNYS
TKAVEPQLSG KMLVLDYILA MTRTTTSDKV VLVSNYTQTL DLFEKLCRNR RYLYVRLDGT
MSIKKRAKIV ERFNNPSSPE FIFMLSSKAG GCGLNLIGAN RLVMFDPDWN PANDEQAMAR
VWRDGQKKTC YIYRLLSTGT IEEKILQRQA HKKALSSCVV DEEQDVERHF SLGELRELFS
LNEKTLSDTH DRFRCRRCVN GRQVRPPPDD SDCTCDLSNW HHCADKRGLR DPVLQASWDA
AVSFVFHQRS HEDQRGVV
