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Entry: Q00578
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ID   RAD25_YEAST             Reviewed;         843 AA.
AC   Q00578; D6VVE4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   01-OCT-2014, entry version 142.
DE   RecName: Full=DNA repair helicase RAD25;
DE            EC=3.6.4.12;
DE   AltName: Full=General transcription and DNA repair factor IIH subunit RAD25;
DE            Short=TFIIH subunit RAD25;
DE   AltName: Full=Suppressor of stem-loop mutation 2;
GN   Name=SSL2; Synonyms=LOM3, RAD25, UVS112; OrderedLocusNames=YIL143C;
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], AND VARIANT SUPPRESSOR MUTANT
RP   LEU-427.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1318786; DOI=10.1016/0092-8674(92)90621-I;
RA   Gulyas K.D., Donahue T.F.;
RT   "SSL2, a suppressor of a stem-loop mutation in the HIS4 leader encodes
RT   the yeast homolog of human ERCC-3.";
RL   Cell 69:1031-1042(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1333609; DOI=10.1073/pnas.89.23.11416;
RA   Park E.K., Guzder S.N., Weeda G., Hoeijmakers J.H., Prakash S.,
RA   Prakash L.;
RT   "RAD25 (SSL2), the yeast homolog of the human Xeroderma pigmentosum
RT   group B DNA repair gene, is essential for viability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:11416-11420(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
RA   Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
RA   Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
RA   Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   FUNCTION OF TFIIH IN RNA POLYMERASE II TRANSCRIPTION.
RX   PubMed=7961739;
RA   Svejstrup J.Q., Feaver W.J., LaPointe J., Kornberg R.D.;
RT   "RNA polymerase transcription factor IIH holoenzyme from yeast.";
RL   J. Biol. Chem. 269:28044-28048(1994).
RN   [7]
RP   FUNCTION OF THE TFIIH CORE COMPLEX IN DNA REPAIR.
RX   PubMed=8631896; DOI=10.1074/jbc.271.18.10821;
RA   Sung P., Guzder S.N., Prakash L., Prakash S.;
RT   "Reconstitution of TFIIH and requirement of its DNA helicase subunits,
RT   Rad3 and Rad25, in the incision step of nucleotide excision repair.";
RL   J. Biol. Chem. 271:10821-10826(1996).
RN   [8]
RP   IDENTIFICATION IN THE TFIIH CORE COMPLEX.
RX   PubMed=14500720; DOI=10.1074/jbc.C300417200;
RA   Takagi Y., Komori H., Chang W.-H., Hudmon A., Erdjument-Bromage H.,
RA   Tempst P., Kornberg R.D.;
RT   "Revised subunit structure of yeast transcription factor IIH (TFIIH)
RT   and reconciliation with human TFIIH.";
RL   J. Biol. Chem. 278:43897-43900(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
CC   -!- FUNCTION: Probably an ATP-dependent DNA helicase, which may have a
CC       DNA unwinding function. Has an essential function in translation
CC       initiation. Acts as component of the general transcription and DNA
CC       repair factor IIH (TFIIH) core, which is essential for both basal
CC       and activated transcription, and is involved in nucleotide
CC       excision repair (NER) of damaged DNA. TFIIH has CTD kinase and
CC       DNA-dependent ATPase activity, and is essential for polymerase II
CC       transcription in vitro. {ECO:0000269|PubMed:7961739,
CC       ECO:0000269|PubMed:8631896}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Component of the TFIIH core complex, which is composed of
CC       RAD3, SSL1, SSL2, TFB1, TFB2, TFB4 and TFB5.
CC       {ECO:0000269|PubMed:14500720}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: A C-terminal deletion renders yeast hypersensitive
CC       to UV light.
CC   -!- MISCELLANEOUS: Present with 825 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00541}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00542}.
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DR   EMBL; Z38059; CAA86135.1; -; Genomic_DNA.
DR   EMBL; M94176; AAA35102.1; -; Genomic_DNA.
DR   EMBL; L01414; AAA34942.1; -; Genomic_DNA.
DR   EMBL; AY692883; AAT92902.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08410.1; -; Genomic_DNA.
DR   PIR; S31272; S31272.
DR   RefSeq; NP_012123.1; NM_001179491.1.
DR   ProteinModelPortal; Q00578; -.
DR   SMR; Q00578; 362-775.
DR   BioGrid; 34849; 36.
DR   DIP; DIP-731N; -.
DR   IntAct; Q00578; 17.
DR   MINT; MINT-573804; -.
DR   STRING; 4932.YIL143C; -.
DR   MaxQB; Q00578; -.
DR   PaxDb; Q00578; -.
DR   PeptideAtlas; Q00578; -.
DR   EnsemblFungi; YIL143C; YIL143C; YIL143C.
DR   GeneID; 854663; -.
DR   KEGG; sce:YIL143C; -.
DR   CYGD; YIL143c; -.
DR   SGD; S000001405; SSL2.
DR   eggNOG; COG1061; -.
DR   GeneTree; ENSGT00390000002204; -.
DR   HOGENOM; HOG000160172; -.
DR   KO; K10843; -.
DR   OMA; RRTGTMS; -.
DR   OrthoDB; EOG7FV3ZX; -.
DR   BioCyc; YEAST:G3O-31393-MONOMER; -.
DR   NextBio; 977238; -.
DR   PRO; PR:Q00578; -.
DR   Genevestigator; Q00578; -.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005675; C:holo TFIIH complex; IDA:SGD.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0097550; C:transcriptional preinitiation complex; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:SGD.
DR   GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IDA:SGD.
DR   GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR   GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; IMP:SGD.
DR   GO; GO:0000019; P:regulation of mitotic recombination; IMP:SGD.
DR   GO; GO:0010525; P:regulation of transposition, RNA-mediated; IMP:SGD.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:SGD.
DR   GO; GO:0001113; P:transcriptional open complex formation at RNA polymerase II promoter; IMP:SGD.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR006935; Helicase/UvrB_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR001161; Helicase_Ercc3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   PRINTS; PR00851; XRODRMPGMNTB.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
DR   TIGRFAMs; TIGR00603; rad25; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1    843       DNA repair helicase RAD25.
FT                                /FTId=PRO_0000101994.
FT   DOMAIN      373    535       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      589    743       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     386    393       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        64     75       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       487    491       DEVH box.
FT   COMPBIAS    302    309       Asp/Glu-rich (acidic).
FT   MOD_RES     752    752       Phosphoserine.
FT                                {ECO:0000269|PubMed:17330950}.
FT   VARIANT     427    427       W -> L (in suppressor mutant).
FT                                {ECO:0000269|PubMed:1318786}.
FT   CONFLICT      9      9       P -> S (in Ref. 2; AAA34942).
FT                                {ECO:0000305}.
FT   CONFLICT     48     48       S -> L (in Ref. 2; AAA34942).
FT                                {ECO:0000305}.
SQ   SEQUENCE   843 AA;  95341 MW;  FA4013E8156FE1C5 CRC64;
     MTDVEGYQPK SKGKIFPDMG ESFFSSDEDS PATDAEIDEN YDDNRETSEG RGERDTGAMV
     TGLKKPRKKT KSSRHTAADS SMNQMDAKDK ALLQDTNSDI PADFVPDSVS GMFRSHDFSY
     LRLRPDHASR PLWISPSDGR IILESFSPLA EQAQDFLVTI AEPISRPSHI HEYKITAYSL
     YAAVSVGLET DDIISVLDRL SKVPVAESII NFIKGATISY GKVKLVIKHN RYFVETTQAD
     ILQMLLNDSV IGPLRIDSDH QVQPPEDVLQ QQLQQTAGKP ATNVNPNDVE AVFSAVIGGD
     NEREEEDDDI DAVHSFEIAN ESVEVVKKRC QEIDYPVLEE YDFRNDHRNP DLDIDLKPST
     QIRPYQEKSL SKMFGNGRAR SGIIVLPCGA GKTLVGITAA CTIKKSVIVL CTSSVSVMQW
     RQQFLQWCTL QPENCAVFTS DNKEMFQTES GLVVSTYSMV ANTRNRSHDS QKVMDFLTGR
     EWGFIILDEV HVVPAAMFRR VVSTIAAHAK LGLTATLVRE DDKIGDLNFL IGPKLYEANW
     MELSQKGHIA NVQCAEVWCP MTAEFYQEYL RETARKRMLL YIMNPTKFQA CQFLIQYHER
     RGDKIIVFSD NVYALQEYAL KMGKPFIYGS TPQQERMNIL QNFQYNDQIN TIFLSKVGDT
     SIDLPEATCL IQISSHYGSR RQEAQRLGRI LRAKRRNDEG FNAFFYSLVS KDTQEMYYST
     KRQAFLVDQG YAFKVITHLH GMENIPNLAY ASPRERRELL QEVLLKNEEA AGIEVGDDAD
     NSVGRGSNGH KRFKSKAVRG EGSLSGLAGG EDMAYMEYST NKNKELKEHH PLIRKMYYKN
     LKK
//
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