MOT1_YEAST
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 03-AUG-2022, entry version 200.
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; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1312673; DOI=10.1128/mcb.12.4.1879-1892.1992;
RA Davis J.L., Kunisawa R., Thorner J.;
RT "A presumptive helicase (MOT1 gene product) affects gene expression and is
RT 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., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., 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., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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 ATP-
RT 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-dependent
RT 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 TAF-
RT 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., Dephoure N.,
RA 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., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA 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 BY
RP 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 BY
RP 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 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 BY
RP 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 [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 insights
RT 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 ATPase
CC activity. Both transcription activation and repression require its
CC 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. {ECO:0000269|PubMed:12805227}.
CC -!- INTERACTION:
CC P32333; 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 medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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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 AlphaFoldDB; P32333; -.
DR SMR; P32333; -.
DR BioGRID; 36099; 435.
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 SGD; S000006003; MOT1.
DR VEuPathDB; FungiDB:YPL082C; -.
DR eggNOG; KOG0392; Eukaryota.
DR GeneTree; ENSGT00940000157500; -.
DR HOGENOM; CLU_000315_1_2_1; -.
DR InParanoid; P32333; -.
DR OMA; SYDICRN; -.
DR BioCyc; YEAST:G3O-33988-MON; -.
DR PRO; PR:P32333; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32333; protein.
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:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
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; IDA:ComplexPortal.
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 transcription 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 CDD; cd17999; DEXHc_Mot1; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR36498; PTHR36498; 1.
DR Pfam; PF12054; DUF3535; 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; 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; DNA-binding; Helicase; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1867
FT /note="TATA-binding protein-associated factor MOT1"
FT /id="PRO_0000074335"
FT REPEAT 289..326
FT /note="HEAT 1"
FT REPEAT 445..482
FT /note="HEAT 2"
FT REPEAT 541..578
FT /note="HEAT 3"
FT REPEAT 1108..1145
FT /note="HEAT 4"
FT REPEAT 1188..1225
FT /note="HEAT 5"
FT DOMAIN 1284..1457
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REPEAT 1495..1537
FT /note="HEAT 6"
FT DOMAIN 1639..1787
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 169..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 195..211
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1408..1411
FT /note="DEGH box"
FT COMPBIAS 174..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1297..1304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 1226
FT /note="E->R: Temperature sensitive in mot1-301."
FT /evidence="ECO:0000269|PubMed:16387868"
FT MUTAGEN 1303
FT /note="K->A: No ATPase activity."
FT /evidence="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
