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Database: UniProt
Entry: P40352
LinkDB: P40352
Original site: P40352 
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   16-OCT-2019, entry version 161.
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;
OC   Saccharomycetes; 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
RT   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.,
RA   Brouwer J., Troelstra C., Bootsma D., Hoeijmakers J.H.J.;
RT   "RAD26, the functional S. cerevisiae homolog of the Cockayne syndrome
RT   B 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.,
RA   Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA   Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA   Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA   Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA   Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA   Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA   Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA   Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA   Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA   Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION
RP   BY 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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: May be involved in the preferential repair of active
CC       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       P35732:DEF1; NbExp=2; IntAct=EBI-14687, EBI-26695;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
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   SMR; P40352; -.
DR   BioGrid; 33788; 150.
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   EuPathDB; FungiDB:YJR035W; -.
DR   SGD; S000003796; RAD26.
DR   HOGENOM; HOG000170952; -.
DR   InParanoid; P40352; -.
DR   KO; K10841; -.
DR   OMA; KRFFKMN; -.
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   PRO; PR:P40352; -.
DR   Proteomes; UP000002311; Chromosome X.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:SGD.
DR   GO; GO:0001208; P:histone H2A-H2B dimer displacement; IMP:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; IGI:SGD.
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   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_N; 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; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1   1085       DNA repair and recombination protein
FT                                RAD26.
FT                                /FTId=PRO_0000074336.
FT   DOMAIN      309    518       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      655    818       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     322    329       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       469    472       DEGH box.
FT   COMPBIAS    173    228       Asp/Glu-rich (acidic).
FT   MOD_RES      30     30       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   CONFLICT    366    366       Q -> H (in Ref. 2; CAA57290).
FT                                {ECO:0000305}.
FT   CONFLICT    963    963       K -> E (in Ref. 2; CAA57290).
FT                                {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
//
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