RAD26_YEAST
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 03-AUG-2022, entry version 175.
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; 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;
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}.
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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 PDBsum; 5VVR; -.
DR AlphaFoldDB; P40352; -.
DR SMR; P40352; -.
DR BioGRID; 33788; 153.
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; P40352; -.
DR PRIDE; P40352; -.
DR EnsemblFungi; YJR035W_mRNA; YJR035W; YJR035W.
DR GeneID; 853492; -.
DR KEGG; sce:YJR035W; -.
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; KRFFKMN; -.
DR BioCyc; YEAST:G3O-31672-MON; -.
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 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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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:2001020; P:regulation of response to DNA damage stimulus; IDA:ComplexPortal.
DR GO; GO:0010767; P:regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage; IMP:SGD.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:SGD.
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; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
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 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
