ID   RAD26_YEAST             Reviewed;        1085 AA.
AC   P40352; D6VWK8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 194.
DE   RecName: Full=DNA repair and recombination protein RAD26;
DE            EC=3.6.4.- {ECO:0000269|PubMed:8702468};
DE   AltName: Full=DNA-dependent ATPase RAD26 {ECO:0000303|PubMed:8702468};
GN   Name=RAD26 {ECO:0000303|PubMed:7957102};
GN   Synonyms=GTA1085 {ECO:0000303|PubMed:8198589};
GN   OrderedLocusNames=YJR035W; ORFNames=J1606;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8198589; DOI=10.1006/bbrc.1994.1703;
RA   Huang M.-E., Chuat J.-C., Galibert F.;
RT   "A possible yeast homolog of human active-gene-repairing helicase ERCC6+.";
RL   Biochem. Biophys. Res. Commun. 201:310-317(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=7957102; DOI=10.1002/j.1460-2075.1994.tb06871.x;
RA   van Gool A.J., Verhage R., Swagemakers S.M.A., van de Putte P., Brouwer J.,
RA   Troelstra C., Bootsma D., Hoeijmakers J.H.J.;
RT   "RAD26, the functional S. cerevisiae homolog of the Cockayne syndrome B
RT   gene ERCC6.";
RL   EMBO J. 13:5361-5369(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   FUNCTION AS AN ATPASE, CATALYTIC ACTIVITY, LACK OF HELICASE ACTIVITY,
RP   COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=8702468; DOI=10.1074/jbc.271.31.18314;
RA   Guzder S.N., Habraken Y., Sung P., Prakash L., Prakash S.;
RT   "RAD26, the yeast homolog of human Cockayne's syndrome group B gene,
RT   encodes a DNA-dependent ATPase.";
RL   J. Biol. Chem. 271:18314-18317(1996).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: A DNA-dependent ATPase that plays a role in transcription-
CC       coupled repair (TCR) (Probable). Does not have detectable helicase
CC       activity; ATPase is more active with single-stranded (ss)DNA than
CC       double-stranded (ds)DNA (PubMed:8702468). RNA does not stimulate ATPase
CC       (PubMed:8702468). {ECO:0000269|PubMed:8702468,
CC       ECO:0000305|PubMed:7957102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:8702468};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8702468};
CC       Note=ATPase activity requires Mg(2+), no other divalent cation tested
CC       was able to substitute. {ECO:0000269|PubMed:8702468};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5, ATPase is active from pH 6-8.5.
CC         {ECO:0000269|PubMed:8702468};
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:8702468}.
CC   -!- INTERACTION:
CC       P40352; P35732: DEF1; NbExp=2; IntAct=EBI-14687, EBI-26695;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Not essential, it can be disrupted. Leads to an
CC       impairment of transcription-coupled DNA repair and slightly slower
CC       growth recovery after UV exposure. {ECO:0000269|PubMed:7957102}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; L26910; AAA34655.1; -; Genomic_DNA.
DR   EMBL; X81635; CAA57290.1; -; Genomic_DNA.
DR   EMBL; Z49535; CAA89562.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08824.1; -; Genomic_DNA.
DR   PIR; JC2227; JC2227.
DR   RefSeq; NP_012569.1; NM_001181693.1.
DR   PDB; 5VVR; EM; 5.80 A; M=1-1085.
DR   PDB; 8TVY; EM; 3.10 A; M=1-1085.
DR   AlphaFoldDB; P40352; -.
DR   EMDB; EMD-8735; -.
DR   SMR; P40352; -.
DR   BioGRID; 33788; 172.
DR   ComplexPortal; CPX-1189; RAD26-DEF1 stalled RNAPII response complex.
DR   DIP; DIP-3008N; -.
DR   FunCoup; P40352; 762.
DR   IntAct; P40352; 54.
DR   STRING; 4932.YJR035W; -.
DR   iPTMnet; P40352; -.
DR   PaxDb; 4932-YJR035W; -.
DR   PeptideAtlas; P40352; -.
DR   EnsemblFungi; YJR035W_mRNA; YJR035W; YJR035W.
DR   GeneID; 853492; -.
DR   KEGG; sce:YJR035W; -.
DR   AGR; SGD:S000003796; -.
DR   SGD; S000003796; RAD26.
DR   VEuPathDB; FungiDB:YJR035W; -.
DR   eggNOG; KOG0387; Eukaryota.
DR   HOGENOM; CLU_000315_7_0_1; -.
DR   InParanoid; P40352; -.
DR   OMA; ACHWSYV; -.
DR   OrthoDB; 413460at2759; -.
DR   BioCyc; YEAST:G3O-31672-MONOMER; -.
DR   Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR   Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   BioGRID-ORCS; 853492; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40352; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P40352; protein.
DR   GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; IDA:ComplexPortal.
DR   GO; GO:0006289; P:nucleotide-excision repair; IGI:SGD.
DR   GO; GO:0061635; P:regulation of protein complex stability; IDA:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:SGD.
DR   CDD; cd18000; DEXHc_ERCC6; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   FunFam; 3.40.50.300:FF:000863; DNA excision repair protein ERCC-6; 1.
DR   FunFam; 3.40.50.10810:FF:000039; DNA repair protein Rhp26/Rad26; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR050496; SNF2_RAD54_helicase_repair.
DR   InterPro; IPR058951; WHD_Rad26_CSB-like.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF25875; WHD_Rad26_CSB; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1085
FT                   /note="DNA repair and recombination protein RAD26"
FT                   /id="PRO_0000074336"
FT   DOMAIN          309..518
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          655..818
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          118..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           469..472
FT                   /note="DEGH box"
FT   COMPBIAS        128..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..219
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         322..329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        366
FT                   /note="Q -> H (in Ref. 2; CAA57290)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        963
FT                   /note="K -> E (in Ref. 2; CAA57290)"
FT                   /evidence="ECO:0000305"
FT   HELIX           217..225
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           234..249
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   TURN            263..266
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   TURN            280..282
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          287..289
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           292..296
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           301..314
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          316..320
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   TURN            330..332
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           333..341
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          349..352
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           355..368
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          376..379
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           383..385
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          443..446
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           448..453
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           457..460
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          464..469
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           471..474
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           480..487
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          491..495
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          498..500
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           505..515
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           525..529
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           534..536
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   TURN            538..542
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           554..561
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           562..564
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           570..573
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           591..604
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          606..609
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          612..616
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           619..628
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   TURN            638..643
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           647..649
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           651..665
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          670..676
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           677..685
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           686..690
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           692..695
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           708..719
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          724..733
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          744..747
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           754..762
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   STRAND          774..777
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           784..804
FT                   /evidence="ECO:0007829|PDB:8TVY"
FT   HELIX           814..820
FT                   /evidence="ECO:0007829|PDB:8TVY"
SQ   SEQUENCE   1085 AA;  124528 MW;  2A8C34A7300148E3 CRC64;
     MEDKEQQDNA KLENNESLKD LGVNVLSQSS LEEKIANDVT NFSNLQSLQQ EETRLERSKT
     ALQRYVNKKN HLTRKLNNTT RISVKQNLRD QIKNLQSDDI ERVLKDIDDI QSRIKELKEQ
     VDQGAENKGS KEGLQRPGET EKEFLIRTGK ITAFGHKAGF SLDTANREYA KNDEQKDEDF
     EMATEQMVEN LTDEDDNLSD QDYQMSGKES EDDEEEENDD KILKELEDLR FRGQPGEAKD
     DGDELYYQER LKKWVKQRSC GSQRSSDLPE WRRPHPNIPD AKLNSQFKIP GEIYSLLFNY
     QKTCVQWLYE LYQQNCGGII GDEMGLGKTI QVIAFIAALH HSGLLTGPVL IVCPATVMKQ
     WCNEFQHWWP PLRTVILHSM GSGMASDQKF KMDENDLENL IMNSKPSDFS YEDWKNSTRT
     KKALESSYHL DKLIDKVVTD GHILITTYVG LRIHSDKLLK VKWQYAVLDE GHKIRNPDSE
     ISLTCKKLKT HNRIILSGTP IQNNLTELWS LFDFIFPGKL GTLPVFQQQF VIPINIGGYA
     NATNIQVQTG YKCAVALRDL ISPYLLRRVK ADVAKDLPQK KEMVLFCKLT KYQRSKYLEF
     LHSSDLNQIQ NGKRNVLFGI DILRKICNHP DLLDRDTKRH NPDYGDPKRS GKMQVVKQLL
     LLWHKQGYKA LLFTQSRQML DILEEFISTK DPDLSHLNYL RMDGTTNIKG RQSLVDRFNN
     ESFDVFLLTT RVGGLGVNLT GANRIIIFDP DWNPSTDMQA RERAWRIGQK REVSIYRLMV
     GGSIEEKIYH RQIFKQFLTN RILTDPKQKR FFKIHELHDL FSLGGENGYS TEELNEEVQK
     HTENLKNSKS EESDDFEQLV NLSGVSKLES FYNGKEKKEN SKTEDDRLIE GLLGGESNLE
     TVMSHDSVVN SHAGSSSSNI ITKEASRVAI EAVNALRKSR KKITKQYEIG TPTWTGRFGK
     AGKIRKRDPL KNKLTGSAAI LGNITKSQKE ASKEARQENY DDGITFARSK EINSNTKTLE
     NIRAYLQKQN NFFSSSVSIL NSIGVSLSDK EDVIKVRALL KTIAQFDKER KGWVLDEEFR
     NNNAS
//