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Database: UniProt
Entry: P32333
LinkDB: P32333
Original site: P32333 
ID   MOT1_YEAST              Reviewed;        1867 AA.
AC   P32333; D6W3T5;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   16-OCT-2019, entry version 186.
DE   RecName: Full=TATA-binding protein-associated factor MOT1;
DE            Short=TBP-associated factor MOT1;
DE            EC=3.6.4.-;
DE   AltName: Full=Modifier of transcription 1;
GN   Name=MOT1; OrderedLocusNames=YPL082C; ORFNames=LPF4C;
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].
RX   PubMed=1312673; DOI=10.1128/mcb.12.4.1879;
RA   Davis J.L., Kunisawa R., Thorner J.;
RT   "A presumptive helicase (MOT1 gene product) affects gene expression
RT   and is required for viability in the yeast Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 12:1879-1892(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
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   [4]
RP   FUNCTION, AND ATPASE ACTIVITY.
RX   PubMed=9234740; DOI=10.1128/mcb.17.8.4842;
RA   Auble D.T., Wang D., Post K.W., Hahn S.;
RT   "Molecular analysis of the SNF2/SWI2 protein family member MOT1, an
RT   ATP-driven enzyme that dissociates TATA-binding protein from DNA.";
RL   Mol. Cell. Biol. 17:4842-4851(1997).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-1303.
RX   PubMed=11880621; DOI=10.1073/pnas.052397899;
RA   Dasgupta A., Darst R.P., Martin K.J., Afshari C.A., Auble D.T.;
RT   "Mot1 activates and represses transcription by direct, ATPase-
RT   dependent mechanisms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:2666-2671(2002).
RN   [6]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=12805227; DOI=10.1093/emboj/cdg304;
RA   Gumbs O.H., Campbell A.M., Weil P.A.;
RT   "High-affinity DNA binding by a Mot1p-TBP complex: implications for
RT   TAF-independent transcription.";
RL   EMBO J. 22:3131-3141(2003).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
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   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
RA   Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
RA   Rehling P., Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [10]
RP   MUTAGENESIS OF GLU-1226.
RX   PubMed=16387868; DOI=10.1534/genetics.105.052811;
RA   Wang Z., Jones G.M., Prelich G.;
RT   "Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in
RT   Saccharomyces cerevisiae.";
RL   Genetics 172:1499-1509(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, 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).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND IDENTIFICATION
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-677, AND
RP   IDENTIFICATION 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: Regulates transcription in association with TATA binding
CC       protein (TBP). Removes TBP from the TATA box via its C-terminal
CC       ATPase activity. Both transcription activation and repression
CC       require its ATPase activity. {ECO:0000269|PubMed:11880621,
CC       ECO:0000269|PubMed:12805227, ECO:0000269|PubMed:9234740}.
CC   -!- SUBUNIT: Forms a complex with TBP which binds TATA DNA with high
CC       affinity but with altered specificity.
CC       {ECO:0000269|PubMed:12805227}.
CC   -!- INTERACTION:
CC       P13393:SPT15; NbExp=7; IntAct=EBI-11152, EBI-19129;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus. Note=Localized on
CC       chromatin. Specifically localized to the promoters of the genes it
CC       regulates.
CC   -!- MISCELLANEOUS: Present with 6560 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; M83224; AAA34786.1; -; Genomic_DNA.
DR   EMBL; U41849; AAB68257.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11351.1; -; Genomic_DNA.
DR   PIR; S22775; S22775.
DR   RefSeq; NP_015243.1; NM_001183896.1.
DR   SMR; P32333; -.
DR   BioGrid; 36099; 429.
DR   ComplexPortal; CPX-1141; MOT1-TBP transcription regulation complex.
DR   DIP; DIP-2418N; -.
DR   IntAct; P32333; 66.
DR   MINT; P32333; -.
DR   STRING; 4932.YPL082C; -.
DR   CarbonylDB; P32333; -.
DR   iPTMnet; P32333; -.
DR   MaxQB; P32333; -.
DR   PaxDb; P32333; -.
DR   PRIDE; P32333; -.
DR   EnsemblFungi; YPL082C_mRNA; YPL082C; YPL082C.
DR   GeneID; 856023; -.
DR   KEGG; sce:YPL082C; -.
DR   EuPathDB; FungiDB:YPL082C; -.
DR   SGD; S000006003; MOT1.
DR   HOGENOM; HOG000210415; -.
DR   InParanoid; P32333; -.
DR   KO; K15192; -.
DR   OMA; ALIFCQM; -.
DR   BioCyc; YEAST:G3O-33988-MONOMER; -.
DR   PRO; PR:P32333; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IDA:SGD.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017025; F:TBP-class protein binding; IPI:SGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:SGD.
DR   GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:SGD.
DR   GO; GO:0045898; P:regulation of RNA polymerase II transcriptional preinitiation complex assembly; IMP:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:SGD.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   Gene3D; 1.25.10.10; -; 2.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR022707; DUF3535.
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; PF12054; DUF3535; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF48371; SSF48371; 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   ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase;
KW   Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1   1867       TATA-binding protein-associated factor
FT                                MOT1.
FT                                /FTId=PRO_0000074335.
FT   REPEAT      289    326       HEAT 1.
FT   REPEAT      445    482       HEAT 2.
FT   REPEAT      541    578       HEAT 3.
FT   REPEAT     1108   1145       HEAT 4.
FT   REPEAT     1188   1225       HEAT 5.
FT   DOMAIN     1284   1457       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   REPEAT     1495   1537       HEAT 6.
FT   DOMAIN     1639   1787       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND    1297   1304       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       195    211       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF      1408   1411       DEGH box.
FT   MOD_RES      93     93       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     677    677       Phosphoserine.
FT                                {ECO:0000244|PubMed:17287358,
FT                                ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MUTAGEN    1226   1226       E->R: Temperature sensitive in mot1-301.
FT                                {ECO:0000269|PubMed:16387868}.
FT   MUTAGEN    1303   1303       K->A: No ATPase activity.
FT                                {ECO:0000269|PubMed:11880621}.
SQ   SEQUENCE   1867 AA;  209977 MW;  1A00005148D5632B CRC64;
     MTSRVSRLDR QVILIETGST QVVRNMAADQ MGDLAKQHPE DILSLLSRVY PFLLVKKWET
     RVTAARAVGG IVAHAPSWDP NESDLVGGTN EGSPLDNAQV KLEHEMKIKL EEATQNNQLN
     LLQEDHHLSS LSDWKLNEIL KSGKVLLASS MNDYNVLGKA DDNIRKQAKT DDIKQETSML
     NASDKANENK SNANKKSARM LAMARRKKKM SAKNTPKHPV DITESSVSKT LLNGKNMTNS
     AASLATSPTS NQLNPKLEIT EQADESKLMI ESTVRPLLEQ HEIVAGLVWQ FQGIYELLLD
     NLMSENWEIR HGAALGLREL VKKHAYGVSR VKGNTREENN LRNSRSLEDL ASRLLTVFAL
     DRFGDYVYDT VVAPVRESVA QTLAALLIHL DSTLSIKIFN CLEQLVLQDP LQTGLPNKIW
     EATHGGLLGI RYFVSIKTNF LFAHGLLENV VRIVLYGLNQ SDDDVQSVAA SILTPITSEF
     VKLNNSTIEI LVTTIWSLLA RLDDDISSSV GSIMDLLAKL CDHQEVLDIL KNKALEHPSE
     WSFKSLVPKL YPFLRHSISS VRRAVLNLLI AFLSIKDDST KNWLNGKVFR LVFQNILLEQ
     NPELLQLSFD VYVALLEHYK VKHTEKTLDH VFSKHLQPIL HLLNTPVGEK GKNYAMESQY
     ILKPSQHYQL HPEKKRSISE TTTDSDIPIP KNNEHINIDA PMIAGDITLL GLDVILNTRI
     MGAKAFALTL SMFQDSTLQS FFTNVLVRCL ELPFSTPRML AGIIVSQFCS SWLQKHPEGE
     KLPSFVSEIF SPVMNKQLLN RDEFPVFREL VPSLKALRTQ CQSLLATFVD VGMLPQYKLP
     NVAIVVQGET EAGPHAFGVE TAEKVYGEYY DKMFKSMNNS YKLLAKKPLE DSKHRVLMAI
     NSAKESAKLR TGSILANYAS SILLFDGLPL KLNPIIRSLM DSVKEERNEK LQTMAGESVV
     HLIQQLLENN KVNVSGKIVK NLCGFLCVDT SEVPDFSVNA EYKEKILTLI KESNSIAAQD
     DINLAKMSEE AQLKRKGGLI TLKILFEVLG PSILQKLPQL RSILFDSLSD HENEEASKVD
     NEQGQKIVDS FGVLRALFPF MSDSLRSSEV FTRFPVLLTF LRSNLSVFRY SAARTFADLA
     KISSVEVMAY TIREILPLMN SAGSLSDRQG STELIYHLSL SMETDVLPYV IFLIVPLLGR
     MSDSNEDVRN LATTTFASII KLVPLEAGIA DPKGLPEELV ASRERERDFI QQMMDPSKAK
     PFKLPIAIKA TLRKYQQDGV NWLAFLNKYH LHGILCDDMG LGKTLQTICI IASDQYLRKE
     DYEKTRSVES RALPSLIICP PSLTGHWENE FDQYAPFLKV VVYAGGPTVR LTLRPQLSDA
     DIIVTSYDVA RNDLAVLNKT EYNYCVLDEG HIIKNSQSKL AKAVKEITAN HRLILTGTPI
     QNNVLELWSL FDFLMPGFLG TEKMFQERFA KPIAASRNSK TSSKEQEAGV LALEALHKQV
     LPFMLRRLKE DVLSDLPPKI IQDYYCELGD LQKQLYMDFT KKQKNVVEKD IENSEIADGK
     QHIFQALQYM RKLCNHPALV LSPNHPQLAQ VQDYLKQTGL DLHDIINAPK LSALRTLLFE
     CGIGEEDIDK KASQDQNFPI QNVISQHRAL IFCQLKDMLD MVENDLFKKY MPSVTYMRLD
     GSIDPRDRQK VVRKFNEDPS IDCLLLTTKV GGLGLNLTGA DTVIFVEHDW NPMNDLQAMD
     RAHRIGQKKV VNVYRIITKG TLEEKIMGLQ KFKMNIASTV VNQQNSGLAS MDTHQLLDLF
     DPDNVTSQDN EEKNNGDSQA AKGMEDIANE TGLTGKAKEA LGELKELWDP SQYEEEYNLD
     TFIKTLR
//
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