RDH54_YEAS7
ID RDH54_YEAS7 Reviewed; 924 AA.
AC A6ZL17;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=SCY_0287;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000011; EDN64686.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZL17; -.
DR SMR; A6ZL17; -.
DR EnsemblFungi; EDN64686; EDN64686; SCY_0287.
DR HOGENOM; CLU_000315_10_1_1; -.
DR Proteomes; UP000007060; 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_0000393313"
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; 104109 MW; 49A16E74FABED75D CRC64;
MQIPKYENKP FKPPRRVGSN KYTQLKPTAT AVTTAPISKA KVTVNLKRSI SAGPTLNLAK
KPNNLSSNEN TRYFTIMYRK PTTKKHKTWS GDGYATLKAS SDKLCFYNEA GKFLGSSMLP
SDSDSLFETL FKAGSNEVQL DYELKENAEI RSAKEALSQN MGNPNPPTTS 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 NRYNEELLEK GEERSKEMIE ITKRFILRRT
NAILEKYLPP KTDIILFCKP YSQQILAFKD ILQGARLDFG QLTFSSSLGL ITLLKKVCNS
PGLVGSDPYY KSHIKDTQSQ DSYSRSLNSG KLRVLMTLLE 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
SFTDLKDSIT FAFVKPGEIC LREQ
