IF4A_YEAST
ID IF4A_YEAST Reviewed; 395 AA.
AC P10081; D6VW46;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 241.
DE RecName: Full=ATP-dependent RNA helicase eIF4A;
DE EC=3.6.4.13 {ECO:0000269|PubMed:12535527, ECO:0000269|PubMed:1502180};
DE AltName: Full=Eukaryotic initiation factor 4A;
DE Short=eIF-4A;
DE AltName: Full=Stimulator factor I 37 kDa component;
DE AltName: Full=Translation initiation factor 1/2 {ECO:0000303|PubMed:2648398, ECO:0000303|PubMed:3057442};
DE AltName: Full=p37;
GN Name=TIF1 {ECO:0000303|PubMed:2648398, ECO:0000303|PubMed:3057442};
GN Synonyms=TIF41A; OrderedLocusNames=YKR059W;
GN and
GN Name=TIF2 {ECO:0000303|PubMed:2648398, ECO:0000303|PubMed:3057442};
GN Synonyms=TIF41B; OrderedLocusNames=YJL138C; ORFNames=J0660;
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] (TIF1 AND TIF2).
RC STRAIN=CD11/B1830/50;
RX PubMed=3057442; DOI=10.1093/nar/16.21.10359;
RA Linder P., Slonimski P.P.;
RT "Sequence of the genes TIF1 and TIF2 from Saccharomyces cerevisiae coding
RT for a translation initiation factor.";
RL Nucleic Acids Res. 16:10359-10359(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF1 AND TIF2).
RC STRAIN=CD11/B1830/50;
RX PubMed=2648398; DOI=10.1073/pnas.86.7.2286;
RA Linder P., Slonimski P.P.;
RT "An essential yeast protein, encoded by duplicated genes TIF1 and TIF2 and
RT homologous to the mammalian translation initiation factor eIF-4A, can
RT suppress a mitochondrial missense mutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2286-2290(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TIF1).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF2).
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TIF2).
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., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [6]
RP GENOME REANNOTATION (TIF1 AND TIF2).
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93 (TIF2).
RX PubMed=8524228; DOI=10.1128/mcb.15.12.6632;
RA Cheng C., Mu J., Farkas I., Huang D., Goebl M.G., Roach P.J.;
RT "Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p
RT for glycogen accumulation in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 15:6632-6640(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-395 (TIF2).
RX PubMed=2041753; DOI=10.1093/nar/19.10.2781;
RA Foreman P.K., Davis R.W., Sachs A.B.;
RT "The Saccharomyces cerevisiae RPB4 gene is tightly linked to the TIF2
RT gene.";
RL Nucleic Acids Res. 19:2781-2781(1991).
RN [9]
RP PROTEIN SEQUENCE OF 332-340; 342-347 AND 378-391.
RX PubMed=1408806; DOI=10.1093/nar/20.18.4913;
RA Smiley J.K., Brown W.C., Campbell J.L.;
RT "The 66 kDa component of yeast SFI, stimulatory factor I, is hsp60.";
RL Nucleic Acids Res. 20:4913-4918(1992).
RN [10]
RP FUNCTION.
RX PubMed=2668952; DOI=10.1073/pnas.86.16.6043;
RA Blum S., Mueller M., Schmid S.R., Linder P., Trachsel H.;
RT "Translation in Saccharomyces cerevisiae: initiation factor 4A-dependent
RT cell-free system.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6043-6046(1989).
RN [11]
RP FUNCTION.
RX PubMed=2169890; DOI=10.1016/0167-4781(90)90158-x;
RA Altmann M., Blum S., Pelletier J., Sonenberg N., Wilson T.M., Trachsel H.;
RT "Translation initiation factor-dependent extracts from Saccharomyces
RT cerevisiae.";
RL Biochim. Biophys. Acta 1050:155-159(1990).
RN [12]
RP CHARACTERIZATION, AND MUTAGENESIS OF ALA-66; ALA-79; GLY-126; GLY-127;
RP GLY-145; ASP-170; ASP-173; SER-311 AND ARG-347.
RX PubMed=2046664; DOI=10.1128/mcb.11.7.3463-3471.1991;
RA Schmid S.R., Linder P.;
RT "Translation initiation factor 4A from Saccharomyces cerevisiae: analysis
RT of residues conserved in the D-E-A-D family of RNA helicases.";
RL Mol. Cell. Biol. 11:3463-3471(1991).
RN [13]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ALA-66.
RX PubMed=1502180; DOI=10.1073/pnas.89.16.7664;
RA Blum S., Schmid S.R., Pause A., Buser P., Linder P., Sonenberg N.,
RA Trachsel H.;
RT "ATP hydrolysis by initiation factor 4A is required for translation
RT initiation in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7664-7668(1992).
RN [14]
RP ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [15]
RP FUNCTION, AND INTERACTION WITH TIF4631 AND TIF4632.
RX PubMed=10409745; DOI=10.1128/mcb.19.8.5557;
RA Neff C.L., Sachs A.B.;
RT "Eukaryotic translation initiation factors 4G and 4A from Saccharomyces
RT cerevisiae interact physically and functionally.";
RL Mol. Cell. Biol. 19:5557-5564(1999).
RN [16]
RP FUNCTION, AND INTERACTION WITH TIF4631.
RX PubMed=10480875; DOI=10.1074/jbc.274.38.26720;
RA Dominguez D., Altmann M., Benz J., Baumann U., Trachsel H.;
RT "Interaction of translation initiation factor eIF4G with eIF4A in the yeast
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:26720-26726(1999).
RN [17]
RP FUNCTION, DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF PHE-24; PHE-42; SER-46; GLN-49 AND LYS-72.
RX PubMed=12535527; DOI=10.1016/s1097-2765(03)00006-6;
RA Tanner N.K., Cordin O., Banroques J., Doere M., Linder P.;
RT "The Q motif: a newly identified motif in DEAD box helicases may regulate
RT ATP binding and hydrolysis.";
RL Mol. Cell 11:127-138(2003).
RN [18]
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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-146, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND THR-146, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-73; SER-77 AND THR-146, 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).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-225.
RX PubMed=10606264; DOI=10.1017/s1355838299991410;
RA Johnson E.R., McKay D.B.;
RT "Crystallographic structure of the amino terminal domain of yeast
RT initiation factor 4A, a representative DEAD-box RNA helicase.";
RL RNA 5:1526-1534(1999).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 10-233.
RX PubMed=10404596; DOI=10.1016/s0969-2126(99)80088-4;
RA Benz J., Trachsel H., Baumann U.;
RT "Crystal structure of the ATPase domain of translation initiation factor 4A
RT from Saccharomyces cerevisiae -- the prototype of the DEAD box protein
RT family.";
RL Structure 7:671-679(1999).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 231-395.
RX PubMed=11087862; DOI=10.1073/pnas.97.24.13080;
RA Caruthers J.M., Johnson E.R., McKay D.B.;
RT "Crystal structure of yeast initiation factor 4A, a DEAD-box RNA
RT helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13080-13085(2000).
CC -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F
CC complex involved in cap recognition and is required for mRNA binding to
CC ribosome. In the current model of translation initiation, eIF4A unwinds
CC RNA secondary structures in the 5'-UTR of mRNAs which is necessary to
CC allow efficient binding of the small ribosomal subunit, and subsequent
CC scanning for the initiator codon. {ECO:0000269|PubMed:10409745,
CC ECO:0000269|PubMed:10480875, ECO:0000269|PubMed:12535527,
CC ECO:0000269|PubMed:1502180, ECO:0000269|PubMed:2169890,
CC ECO:0000269|PubMed:2668952}.
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 Evidence={ECO:0000269|PubMed:12535527, ECO:0000269|PubMed:1502180};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=470 uM for ATP {ECO:0000269|PubMed:12535527,
CC ECO:0000269|PubMed:1502180};
CC Vmax=2.6 pmol/sec/ug enzyme for ATP {ECO:0000269|PubMed:12535527,
CC ECO:0000269|PubMed:1502180};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:12535527,
CC ECO:0000269|PubMed:1502180};
CC -!- SUBUNIT: Component of the eIF4F complex, which composition varies with
CC external and internal environmental conditions. It is composed of at
CC least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632)
CC (By similarity). Interacts with eIF4G1/TIF4631 and eIF4G2/TIF4632.
CC {ECO:0000250, ECO:0000269|PubMed:10409745,
CC ECO:0000269|PubMed:10480875}.
CC -!- INTERACTION:
CC P10081; P39935: TIF4631; NbExp=10; IntAct=EBI-9017, EBI-9002;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000269|PubMed:12535527}.
CC -!- MISCELLANEOUS: TIF1 and TIF2 code for the same protein.
CC -!- MISCELLANEOUS: Present with 106000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
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DR EMBL; X12813; CAA31301.1; -; Genomic_DNA.
DR EMBL; X12814; CAA31302.1; -; Genomic_DNA.
DR EMBL; X58099; CAA41110.1; -; Genomic_DNA.
DR EMBL; X87371; CAA60817.1; -; Genomic_DNA.
DR EMBL; Z49413; CAA89433.1; -; Genomic_DNA.
DR EMBL; U25436; AAA91645.1; -; Genomic_DNA.
DR EMBL; Z28284; CAA82138.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08662.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09210.1; -; Genomic_DNA.
DR PIR; S05835; FIBY1.
DR RefSeq; NP_012397.1; NM_001181571.1.
DR RefSeq; NP_012985.3; NM_001179849.3.
DR PDB; 1FUK; X-ray; 1.75 A; A=231-395.
DR PDB; 1FUU; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1QDE; X-ray; 2.00 A; A=9-232.
DR PDB; 1QVA; X-ray; 2.50 A; A=2-224.
DR PDB; 2VSO; X-ray; 2.60 A; A/B=1-395.
DR PDB; 2VSX; X-ray; 2.80 A; A/B=1-395.
DR PDBsum; 1FUK; -.
DR PDBsum; 1FUU; -.
DR PDBsum; 1QDE; -.
DR PDBsum; 1QVA; -.
DR PDBsum; 2VSO; -.
DR PDBsum; 2VSX; -.
DR AlphaFoldDB; P10081; -.
DR SMR; P10081; -.
DR BioGRID; 33619; 358.
DR BioGRID; 34190; 295.
DR ComplexPortal; CPX-430; Eukaryotic translation initiation factor 4F complex, variant TIF4631.
DR ComplexPortal; CPX-431; Eukaryotic translation initiation factor 4F complex, variant TIF4632.
DR DIP; DIP-4571N; -.
DR IntAct; P10081; 87.
DR MINT; P10081; -.
DR STRING; 4932.YJL138C; -.
DR CarbonylDB; P10081; -.
DR iPTMnet; P10081; -.
DR SWISS-2DPAGE; P10081; -.
DR MaxQB; P10081; -.
DR PaxDb; P10081; -.
DR PRIDE; P10081; -.
DR EnsemblFungi; YJL138C_mRNA; YJL138C; YJL138C.
DR EnsemblFungi; YKR059W_mRNA; YKR059W; YKR059W.
DR GeneID; 853303; -.
DR GeneID; 853933; -.
DR KEGG; sce:YJL138C; -.
DR KEGG; sce:YKR059W; -.
DR SGD; S000001767; TIF1.
DR SGD; S000003674; TIF2.
DR VEuPathDB; FungiDB:YJL138C; -.
DR VEuPathDB; FungiDB:YKR059W; -.
DR eggNOG; KOG0327; Eukaryota.
DR GeneTree; ENSGT00940000155037; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; P10081; -.
DR OMA; EHKDGQR; -.
DR BioCyc; YEAST:G3O-32027-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR SABIO-RK; P10081; -.
DR EvolutionaryTrace; P10081; -.
DR PRO; PR:P10081; -.
DR Proteomes; UP000002311; Chromosome X.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P10081; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IMP:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0005840; C:ribosome; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IDA:SGD.
DR GO; GO:0006446; P:regulation of translational initiation; IC:ComplexPortal.
DR GO; GO:0006413; P:translational initiation; IDA:SGD.
DR CDD; cd18046; DEADc_EIF4AII_EIF4AI_DDX2; 1.
DR DisProt; DP02562; -.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044728; EIF4A_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..395
FT /note="ATP-dependent RNA helicase eIF4A"
FT /id="PRO_0000054968"
FT DOMAIN 53..222
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 233..394
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 22..50
FT /note="Q motif"
FT MOTIF 170..173
FT /note="DEAD box"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 24
FT /note="F->A: Lethal in vivo and reduces ATP binding and
FT ATPase activity in vitro."
FT /evidence="ECO:0000269|PubMed:12535527"
FT MUTAGEN 42
FT /note="F->A: Slow growth in vivo and reduces ATP binding
FT and ATPase activity in vitro."
FT /evidence="ECO:0000269|PubMed:12535527"
FT MUTAGEN 46
FT /note="S->A: Reduces ATP binding and ATPase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:12535527"
FT MUTAGEN 49
FT /note="Q->A: Reduces ATP binding and ATPase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:12535527"
FT MUTAGEN 49
FT /note="Q->E: Increases about 3-fold ATP binding but reduces
FT about 2-fold ATPase activity in vitro."
FT /evidence="ECO:0000269|PubMed:12535527"
FT MUTAGEN 66
FT /note="A->D: Slow growth."
FT /evidence="ECO:0000269|PubMed:1502180,
FT ECO:0000269|PubMed:2046664"
FT MUTAGEN 66
FT /note="A->V: Lethal and dominant negative if overexpressed
FT in vivo. Impairs ATP hydrolysis, RNA-helicase and
FT translation activity in vitro."
FT /evidence="ECO:0000269|PubMed:1502180,
FT ECO:0000269|PubMed:2046664"
FT MUTAGEN 72
FT /note="K->A: Lethal in vivo and reduces ATP binding and
FT ATPase activity in vitro."
FT /evidence="ECO:0000269|PubMed:12535527"
FT MUTAGEN 79
FT /note="A->V: In TIF1-1; no growth at 36 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:2046664"
FT MUTAGEN 126
FT /note="G->D: Lethal."
FT /evidence="ECO:0000269|PubMed:2046664"
FT MUTAGEN 127
FT /note="G->D: Slow growth."
FT /evidence="ECO:0000269|PubMed:2046664"
FT MUTAGEN 145
FT /note="G->D: Lethal."
FT /evidence="ECO:0000269|PubMed:2046664"
FT MUTAGEN 145
FT /note="G->S: Slow growth."
FT /evidence="ECO:0000269|PubMed:2046664"
FT MUTAGEN 170
FT /note="D->E: Lethal."
FT /evidence="ECO:0000269|PubMed:2046664"
FT MUTAGEN 173
FT /note="D->H: Lethal."
FT /evidence="ECO:0000269|PubMed:2046664"
FT MUTAGEN 311
FT /note="S->F: Slow growth."
FT /evidence="ECO:0000269|PubMed:2046664"
FT MUTAGEN 347
FT /note="R->E,G,I,S,T: Lethal and dominant negative if
FT overexpressed."
FT /evidence="ECO:0000269|PubMed:2046664"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1FUU"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:1QDE"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:1QDE"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:1QDE"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1QDE"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:1FUU"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:1QDE"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:1QDE"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:1QDE"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:1QDE"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1QDE"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:1FUK"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1FUK"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:1FUK"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:1FUK"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:1FUK"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1FUK"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:1FUK"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:1FUK"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1FUK"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:1FUK"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:1FUK"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:1FUK"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:1FUK"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:1FUK"
FT HELIX 369..378
FT /evidence="ECO:0007829|PDB:1FUK"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:1FUU"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:1FUK"
SQ SEQUENCE 395 AA; 44697 MW; 19D8C133C815DD48 CRC64;
MSEGITDIEE SQIQTNYDKV VYKFDDMELD ENLLRGVFGY GFEEPSAIQQ RAIMPIIEGH
DVLAQAQSGT GKTGTFSIAA LQRIDTSVKA PQALMLAPTR ELALQIQKVV MALAFHMDIK
VHACIGGTSF VEDAEGLRDA QIVVGTPGRV FDNIQRRRFR TDKIKMFILD EADEMLSSGF
KEQIYQIFTL LPPTTQVVLL SATMPNDVLE VTTKFMRNPV RILVKKDELT LEGIKQFYVN
VEEEEYKYEC LTDLYDSISV TQAVIFCNTR RKVEELTTKL RNDKFTVSAI YSDLPQQERD
TIMKEFRSGS SRILISTDLL ARGIDVQQVS LVINYDLPAN KENYIHRIGR GGRFGRKGVA
INFVTNEDVG AMRELEKFYS TQIEELPSDI ATLLN
