ECM32_YEAST
ID ECM32_YEAST Reviewed; 1121 AA.
AC P32644; D3DM85;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Putative ATP-dependent RNA helicase ECM32;
DE EC=3.6.4.13;
DE AltName: Full=DNA helicase B;
DE Short=Hcs B;
DE AltName: Full=DNA helicase III;
DE AltName: Full=Extracellular mutant protein 32;
DE AltName: Full=Helicase 1;
DE Short=scHelI;
DE AltName: Full=Modulator of translation termination protein 1;
GN Name=ECM32; Synonyms=HEL1, MTT1; OrderedLocusNames=YER176W;
GN ORFNames=SYGP-ORF61;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 28-46; 339-341; 472-510; 752-763; 778-780; 898-904;
RP 993-1007 AND 1083-1090, AND FUNCTION.
RX PubMed=9990119; DOI=10.1093/oxfordjournals.jbchem.a022279;
RA Kamimura Y.I., Kawasaki Y., Ohara T., Sugino A.;
RT "DNA helicase III of Saccharomyces cerevisiae, encoded by YER176w (HEL1),
RT highly unwinds covalently closed, circular DNA in the presence of a DNA
RT topoisomerase and yRF-A.";
RL J. Biochem. 125:236-244(1999).
RN [4]
RP PROTEIN SEQUENCE OF 277-282 AND 624-642, AND PRELIMINARY CHARACTERIZATION.
RX PubMed=7832796; DOI=10.1006/bbrc.1995.1121;
RA Biswas E.E., Chen P.H., Leszyk J., Biswas S.B.;
RT "Biochemical and genetic characterization of a replication protein A
RT dependent DNA helicase from the yeast, Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 206:850-856(1995).
RN [5]
RP IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [6]
RP FUNCTION, INTERACTION WITH SUP35 AND SUP45, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=10836794; DOI=10.1017/s1355838200992392;
RA Czaplinski K., Majlesi N., Banerjee T., Peltz S.W.;
RT "Mtt1 is a Upf1-like helicase that interacts with the translation
RT termination factors and whose overexpression can modulate termination
RT efficiency.";
RL RNA 6:730-743(2000).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-392 AND THR-465, AND
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 [11]
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: Probable RNA helicase, which may be involved in modulation of
CC the translation termination process. Probably unwinds double-stranded
CC RNA. In vitro, unwinds covalently closed, circular DNA in the presence
CC of a DNA topoisomerase TOP1 and replication factor-A protein RFA1.
CC {ECO:0000269|PubMed:10836794, ECO:0000269|PubMed:9990119}.
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=3.6.4.13;
CC -!- SUBUNIT: Interacts with the peptidyl release factors SUP35 and weakly
CC with SUP45. {ECO:0000269|PubMed:10836794}.
CC -!- INTERACTION:
CC P32644; P05453: SUP35; NbExp=3; IntAct=EBI-22223, EBI-6540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10836794,
CC ECO:0000269|PubMed:14562095}. Note=Associated with polyribosomes.
CC -!- DISRUPTION PHENOTYPE: Sensitivity to drugs that affect translation
CC fidelity. Overexpression results in a nonsense suppression phenotype.
CC {ECO:0000269|PubMed:10836794}.
CC -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC -!- CAUTION: ECM32 was originally identified as a DNA helicase and as
CC component of DNA polymerase I. {ECO:0000305}.
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DR EMBL; U18922; AAB64703.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07839.1; -; Genomic_DNA.
DR PIR; S30862; S30862.
DR RefSeq; NP_011103.1; NM_001179066.1.
DR AlphaFoldDB; P32644; -.
DR SMR; P32644; -.
DR BioGRID; 36929; 95.
DR DIP; DIP-5404N; -.
DR IntAct; P32644; 3.
DR STRING; 4932.YER176W; -.
DR iPTMnet; P32644; -.
DR MaxQB; P32644; -.
DR PaxDb; P32644; -.
DR PRIDE; P32644; -.
DR EnsemblFungi; YER176W_mRNA; YER176W; YER176W.
DR GeneID; 856923; -.
DR KEGG; sce:YER176W; -.
DR SGD; S000000978; ECM32.
DR VEuPathDB; FungiDB:YER176W; -.
DR eggNOG; KOG1802; Eukaryota.
DR HOGENOM; CLU_010015_0_0_1; -.
DR InParanoid; P32644; -.
DR OMA; HPLGKIC; -.
DR BioCyc; YEAST:G3O-30335-MON; -.
DR PRO; PR:P32644; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32644; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0006449; P:regulation of translational termination; IMP:SGD.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..1121
FT /note="Putative ATP-dependent RNA helicase ECM32"
FT /id="PRO_0000080725"
FT REGION 157..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..182
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 670..677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1121 AA; 126970 MW; 641C4AA6810282A0 CRC64;
MDFQCRTCSQ AYDAEQMMKH LSSTRHKTVF DTSNDEDICC EECQDKNIHQ LQIIRFGGED
MVLLCNSCFR KEYSETERPS TSYSLQNGSI LKFWEKYVKV RECCCDECGE ESNLNANRNG
EVLCDKCLPK SNRAKDFVSE KSGRFLYIYL GLNETQNSTR KPRKKGGRRV GRGKKGRKGA
KIKKEKKETF EAKISRIAYE VKKENSTIQS SSSSNLRNFK GFKAVESDPV VAAKVSKSET
SRSNPGPSNR NKGKGNKANH KKNSGNGIGK EKERKTNIRN NVRNSQPIPE DRKNTNSHVT
TNSGGKGKNE SVDKHQLPQP KALNGNGSGS TNTTGLKKGK KDHAGQKTKG NDKTGNKNPR
EAKLNSAGRK NALGKKSNNQ PNKGTSRWTI GSDTESSREP SISPNENTTS ITKSRNRNKK
ASKPTLNEKS KTTTMPKKLE TKNQEKNNGK TKDGKLIYEE GEPLTRYNTF KSTLSYPDLN
TYLNDYSFAL FLEQKLENEF VQNFNILWPR NEKDTAFIIN VEKNNNSELE KLLPANLLAL
GRPAFNERQP FFFCTQDEQK VWYIFIKELS IQRGKYVLLV ELFSWNNLSL PTKNGSSQFK
LLPTSAQTSR ILFAMTRITN PKFIDLLLGQ KPIKEIYFDN RLKFSSDKLN RSQKTAVEHV
LNNSITILQG PPGTGKTSTI EEIIIQVIER FHAFPILCVA ASNIAIDNIA EKIMENRPQI
KILRILSKKK EQQYSDDHPL GEICLHNIVY KNLSPDMQVV ANKTRRGEMI SKSEDTKFYK
EKNRVTNKVV SQSQIIFTTN IAAGGRELKV IKECPVVIMD EATQSSEAST LVPLSLPGIR
NFVFVGDEKQ LSSFSNIPQL ETSLFERVLS NGTYKNPLML DTQYRMHPKI SEFPIKKIYN
GELKDGVTDE QKAWPGVQHP LFFYQCDLGP ESRVRSTQRD IVGFTYENKH ECVEIVKIIQ
ILMLDKKVPL EEIGVITPYS AQRDLLSDIL TKNVVINPKQ ISMQQEYDEI ELFNAAGSQG
TAGSLQNNVI NIINGLHVAT VDSFQGHEKS FIIFSCVRNN TENKIGFLRD KRRLNVALTR
AKHGLIVVGN KNVLRKGDPL WKDYITYLEE QEVIFTDLTA Y
