ID   RAD54_SCHPO             Reviewed;         852 AA.
AC   P41410; O13723;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=DNA repair protein rhp54;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:P32863};
DE   AltName: Full=RAD54 homolog 1;
GN   Name=rhp54; Synonyms=rad54; ORFNames=SPAC15A10.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8834792; DOI=10.1242/jcs.109.1.73;
RA   Muris D.F.R., Vreeken K., Carr A.M., Murray J.M., Smit C., Lohman P.H.M.,
RA   Pastink A.;
RT   "Isolation of the Schizosaccharomyces pombe RAD54 homologue, rhp54+, a gene
RT   involved in the repair of radiation damage and replication fidelity.";
RL   J. Cell Sci. 109:73-81(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   INTERACTION WITH RHP51.
RX   PubMed=14551247; DOI=10.1091/mbc.e03-05-0288;
RA   Catlett M.G., Forsburg S.L.;
RT   "Schizosaccharomyces pombe Rdh54 (TID1) acts with Rhp54 (RAD54) to repair
RT   meiotic double-strand breaks.";
RL   Mol. Biol. Cell 14:4707-4720(2003).
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. Acts as a molecular motor during the homology search and guides
CC       RAD51 ssDNA along a donor dsDNA thereby changing the homology search
CC       from the diffusion-based mechanism to a motor-guided mechanism. Plays
CC       also an essential role in RAD51-mediated synaptic complex formation
CC       which consists of three strands encased in a protein filament formed
CC       once homology is recognized. Once DNA strand exchange occured,
CC       dissociates RAD51 from nucleoprotein filaments formed on dsDNA.
CC       {ECO:0000250|UniProtKB:P32863}.
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 (By similarity). Interacts with rhp51.
CC       {ECO:0000250|UniProtKB:Q7ZV09, ECO:0000269|PubMed:14551247}.
CC   -!- INTERACTION:
CC       P41410; P36601: rhp51; NbExp=3; IntAct=EBI-1167415, EBI-926960;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; Z29640; CAA82750.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB10100.1; -; Genomic_DNA.
DR   PIR; S41886; S41886.
DR   RefSeq; NP_594290.1; NM_001019713.2.
DR   AlphaFoldDB; P41410; -.
DR   SMR; P41410; -.
DR   BioGRID; 279199; 25.
DR   IntAct; P41410; 1.
DR   STRING; 4896.SPAC15A10.03c.1; -.
DR   SwissPalm; P41410; -.
DR   MaxQB; P41410; -.
DR   PaxDb; P41410; -.
DR   PRIDE; P41410; -.
DR   EnsemblFungi; SPAC15A10.03c.1; SPAC15A10.03c.1:pep; SPAC15A10.03c.
DR   GeneID; 2542749; -.
DR   KEGG; spo:SPAC15A10.03c; -.
DR   PomBase; SPAC15A10.03c; -.
DR   VEuPathDB; FungiDB:SPAC15A10.03c; -.
DR   eggNOG; KOG0390; Eukaryota.
DR   HOGENOM; CLU_000315_10_2_1; -.
DR   InParanoid; P41410; -.
DR   OMA; YTEHERM; -.
DR   PhylomeDB; P41410; -.
DR   PRO; PR:P41410; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
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; ISM:PomBase.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015616; F:DNA translocase activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IMP:PomBase.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR   GO; GO:0006311; P:meiotic gene conversion; IMP:PomBase.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
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..852
FT                   /note="DNA repair protein rhp54"
FT                   /id="PRO_0000074343"
FT   DOMAIN          281..459
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          614..767
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          187..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           35..51
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           178..181
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           410..413
FT                   /note="DEGH box"
FT   COMPBIAS        187..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         294..301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        261
FT                   /note="A -> T (in Ref. 1; CAA82750)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   852 AA;  96654 MW;  9DB3A247A57B0880 CRC64;
     MIQQPTTAKP RISTSSKLNT VLSKNKENVP GKLFKKFKCP SLVISEKRKE LPLRKKPRVN
     YSEYGSVDGK YDSAYVSENV SGLATIKEAN RLILNHERRD PSTVIKKQFS VPKPIKGHED
     ISKLCAHRPP PTLGMKRKVD FIPRPLYDPA DEFAIVLYDP TTDADEIIPD IKEVLAEKRK
     KDELLKNRKG KKEISDSEPE SDHDSCVSTD TVASCSTEQS LITSNTSKHR RPNKSLKDLL
     GIQKEKPPPP PVAVVIDPKL ARILRPHQIE GVKFLYKCVT GRIDRCANGC IMADEMGLGK
     TLQCIALLWT LLKQSPQAGK PTIEKAIITC PSSLVKNWAN ELVKWLGKDA ITPFILDGKS
     SKQELIMALQ QWASVHGRQV TRPVLIASYE TLRSYVEHLN NAEIGMLLCD EGHRLKNSDS
     LTFTALDKLN VQRRVILSGT PIQNDLSEYF SLLNFANPGL LGSRQEFRKN YEIPILKGRD
     ADGTEKDKEN GDAKLAELAK IVNRFIIRRT NDILSKYLPV KYEHVVFCNL SEFQLSLYKH
     FITSPEINKI LRGTGSQPLK AIGLLKKICN HPDLLNLTED LEGCEALFPP GFIPRELRGR
     DRNIDSSLSG KMLVLERMLY QIKQETDDKI VLISNYTSTL DLFEQLCRAR GYKALRLDGT
     MNVNKRQRLV DTFNDPEKDA FVFLLSSKAG GCGINLIGAN RLILFDPDWN PAADQQALAR
     VWRDGQKKDC FVYRFIATGT IEEKIFQRQS HKQSLSSCVV DEAQDVERHF SLDNLRQLFQ
     LNDHTVCETH ETYKCKRCRD GKQFIRAPAM LYGDTSTWNH FTNPTLDRIE DHLLKREAGK
     QQVSTVFQYK SH