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   27-MAR-2024, entry version 183.
DE   RecName: Full=DNA repair and recombination protein RAD26;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase RAD26;
GN   Name=RAD26; Synonyms=GTA1085; OrderedLocusNames=YJR035W;
GN   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].
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   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   [6]
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: May be involved in the preferential repair of active genes.
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   -!- INTERACTION:
CC       P40352; P35732: DEF1; NbExp=2; IntAct=EBI-14687, EBI-26695;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PDBsum; 5VVR; -.
DR   AlphaFoldDB; P40352; -.
DR   EMDB; EMD-8735; -.
DR   SMR; P40352; -.
DR   BioGRID; 33788; 161.
DR   ComplexPortal; CPX-1189; RAD26-DEF1 stalled RNAPII response complex.
DR   DIP; DIP-3008N; -.
DR   IntAct; P40352; 53.
DR   MINT; P40352; -.
DR   STRING; 4932.YJR035W; -.
DR   iPTMnet; P40352; -.
DR   MaxQB; 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   GeneTree; ENSGT00940000158057; -.
DR   HOGENOM; CLU_000315_7_0_1; -.
DR   InParanoid; P40352; -.
DR   OMA; PREWGYC; -.
DR   OrthoDB; 5488252at2759; -.
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:UniProtKB-KW.
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; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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   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.
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   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   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; Helicase;
KW   Hydrolase; 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   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"
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
//