ID   RDH54_YEAS2             Reviewed;         924 AA.
AC   C7GQI8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 45.
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; ORFNames=C1Q_02585;
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291;
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA   Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA   Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA   Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA   Pereira G.A.G.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(2009).
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 (By
CC       similarity). {ECO:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; ACFL01000124; EEU06936.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7GQI8; -.
DR   SMR; C7GQI8; -.
DR   PRIDE; C7GQI8; -.
DR   Proteomes; UP000008073; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Isomerase; Isopeptide bond; Meiosis;
KW   Nucleotide-binding; Nucleus; Topoisomerase; Ubl conjugation.
FT   CHAIN           1..924
FT                   /note="DNA repair and recombination protein RDH54"
FT                   /id="PRO_0000393311"
FT   DOMAIN          299..487
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          631..790
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           472..475
FT                   /note="DEGH box"
FT   BINDING         346..353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CROSSLNK        615
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P38086"
SQ   SEQUENCE   924 AA;  104080 MW;  5C204CFEAC276A43 CRC64;
     MQIPKYENKP FKPPRRVGSN KYTQLKPTAT AVTTAPISKA KVTANLKRSI SAGPTLNLAK
     KPNNLTSNEN TRYFTIMYRK PTTKKHKTWS GDGYATLKAN SDKLCFYNEA GKFLGSSMLP
     SDSDSLFETL FKAGSNEVQL DYELKENAEI RSAKEALSQN MGNPSPPTTS TTETVPSTKN
     DGGKYQMPLS QLFSLNTVKR FKSVTKQTNE HMTTVPKTSQ NSKAKKYYPV FDVNKIDNPI
     VMNKNAAAEV DVIVDPLLGK FLRPHQREGV KFMYDCLMGL ARPTIENPDI DCTTKSLVLE
     NDSDISGCLL ADDMGLGKTL MSITLIWTLI RQTPFASKVS CSQSGIPLTG LCKKILVVCP
     VTLIGNWKRE FGKWLNLSRI GVLTLSSRNS PDMDKMAVRN FLKVQRTYQV LIIGYEKLLS
     VSEELEKNKH LIDMLVCDEG HRLKNGASKI LNTLKSLDIR RKLLLTGTPI QNDLNEFFTI
     IDFINPGILG SFASFKRRFI IPITRARDTA NRYNEELLKK GEERSKEMIE ITKRFILRRT
     NAILEKYLPP KTDIILFCKP YSQQILAFKD ILQGARLDFG QLTFSSSLGL ITLLKKVCNS
     PGLVGSDPYY KSHIKDTQSQ DSYSRSLNSG KLKVLMTLLE GIRKGTKEKV VVVSNYTQTL
     DIIENLMNMA GMSHCRLDGS IPAKQRDSIV TSFNRNPAIF GFLLSAKSGG VGLNLVGASR
     LILFDNDWNP SVDLQAMSRI HRDGQKKPCF IYRLVTTGCI DEKILQRQLM KNSLSQKFLG
     DSEMRNKESS NDDLFNKEDL KDLFSVHTDT KSNTHDLICS CDGLGEEIEY PETNQQQNTV
     ELRKRSTTTW TSALDLQKKM NEAATNDDAK KSQYIRQCLV HYKHIDPARQ DELFDEVITD
     SFTELKDSIT FAFVKPGEIC LREQ