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Database: UniProt
Entry: SUI1_YEAST
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Original site: SUI1_YEAST 
ID   SUI1_YEAST              Reviewed;         108 AA.
AC   P32911; D6W0U9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-SEP-2017, entry version 134.
DE   RecName: Full=Eukaryotic translation initiation factor eIF-1;
DE   AltName: Full=Protein translation factor SUI1;
GN   Name=SUI1; Synonyms=RFR1; OrderedLocusNames=YNL244C; ORFNames=N0905;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1729602; DOI=10.1128/MCB.12.1.248;
RA   Yoon H., Donahue T.F.;
RT   "The sui1 suppressor locus in Saccharomyces cerevisiae encodes a
RT   translation factor that functions during tRNA(iMet) recognition of the
RT   start codon.";
RL   Mol. Cell. Biol. 12:248-260(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9234673;
RX   DOI=10.1002/(SICI)1097-0061(199707)13:9<849::AID-YEA106>3.0.CO;2-N;
RA   Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A.,
RA   Hegemann J.H.;
RT   "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from
RT   the left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL   Yeast 13:849-860(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
RA   Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA   Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA   Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA   Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA   Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA   Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA   Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA   Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA   Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA   Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA   Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA   Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA   Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT   and its evolutionary implications.";
RL   Nature 387:93-98(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   INTERACTION WITH NIP1.
RX   PubMed=9671501; DOI=10.1128/MCB.18.8.4935;
RA   Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P.,
RA   Greenberg J.R., Qin J., Hinnebusch A.G.;
RT   "Identification of a translation initiation factor 3 (eIF3) core
RT   complex, conserved in yeast and mammals, that interacts with eIF5.";
RL   Mol. Cell. Biol. 18:4935-4946(1998).
RN   [6]
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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Additional factor that functions in concert with eIF-2
CC       and the initiator tRNA in directing the ribosome to the proper
CC       start site of translation.
CC   -!- SUBUNIT: The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and
CC       methionyl-tRNAi form a multifactor complex (MFC) that may bind to
CC       the 40S ribosome. Interacts with NIP1.
CC       {ECO:0000269|PubMed:9671501}.
CC   -!- INTERACTION:
CC       P32497:NIP1; NbExp=4; IntAct=EBI-18527, EBI-8965;
CC       P06103:PRT1; NbExp=9; IntAct=EBI-18527, EBI-8973;
CC       P38249:RPG1; NbExp=2; IntAct=EBI-18527, EBI-8981;
CC   -!- SIMILARITY: Belongs to the SUI1 family. {ECO:0000305}.
DR   EMBL; M77514; AAA35131.1; -; Genomic_DNA.
DR   EMBL; X96722; CAA65499.1; -; Genomic_DNA.
DR   EMBL; Z71520; CAA96150.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10315.1; -; Genomic_DNA.
DR   PIR; S31245; S31245.
DR   RefSeq; NP_014155.1; NM_001183082.1.
DR   PDB; 2OGH; NMR; -; A=1-108.
DR   PDB; 2RVH; NMR; -; A=1-108.
DR   PDB; 3J80; EM; 3.75 A; j=1-108.
DR   PDB; 3J81; EM; 4.00 A; m=1-108.
DR   PDB; 3JAM; EM; 3.46 A; j=1-108.
DR   PDB; 3JAP; EM; 4.90 A; m=1-108.
DR   PDB; 3JAQ; EM; 6.00 A; m=1-108.
DR   PDBsum; 2OGH; -.
DR   PDBsum; 2RVH; -.
DR   PDBsum; 3J80; -.
DR   PDBsum; 3J81; -.
DR   PDBsum; 3JAM; -.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 3JAQ; -.
DR   ProteinModelPortal; P32911; -.
DR   SMR; P32911; -.
DR   BioGrid; 35595; 64.
DR   DIP; DIP-1471N; -.
DR   IntAct; P32911; 44.
DR   MINT; MINT-391861; -.
DR   STRING; 4932.YNL244C; -.
DR   iPTMnet; P32911; -.
DR   MaxQB; P32911; -.
DR   PRIDE; P32911; -.
DR   EnsemblFungi; YNL244C; YNL244C; YNL244C.
DR   GeneID; 855477; -.
DR   KEGG; sce:YNL244C; -.
DR   EuPathDB; FungiDB:YNL244C; -.
DR   SGD; S000005188; SUI1.
DR   GeneTree; ENSGT00390000015789; -.
DR   HOGENOM; HOG000279813; -.
DR   InParanoid; P32911; -.
DR   KO; K03113; -.
DR   OMA; QPTNYIH; -.
DR   OrthoDB; EOG092C585A; -.
DR   BioCyc; YEAST:G3O-33241-MONOMER; -.
DR   EvolutionaryTrace; P32911; -.
DR   PRO; PR:P32911; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:SGD.
DR   GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IDA:SGD.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:SGD.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IDA:SGD.
DR   GO; GO:1990145; P:maintenance of translational fidelity; IMP:SGD.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd11566; eIF1_SUI1; 1.
DR   Gene3D; 3.30.780.10; -; 1.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR005874; SUI1_euk.
DR   Pfam; PF01253; SUI1; 1.
DR   PIRSF; PIRSF004499; SUI1_euk; 1.
DR   SUPFAM; SSF55159; SSF55159; 1.
DR   TIGRFAMs; TIGR01160; SUI1_MOF2; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Protein biosynthesis;
KW   Reference proteome; Translation regulation.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378}.
FT   CHAIN         2    108       Eukaryotic translation initiation factor
FT                                eIF-1.
FT                                /FTId=PRO_0000130566.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   STRAND       26     32       {ECO:0000244|PDB:3JAM}.
FT   STRAND       34     36       {ECO:0000244|PDB:2OGH}.
FT   STRAND       38     44       {ECO:0000244|PDB:3JAM}.
FT   STRAND       47     49       {ECO:0000244|PDB:3JAM}.
FT   HELIX        51     62       {ECO:0000244|PDB:3JAM}.
FT   STRAND       67     69       {ECO:0000244|PDB:3JAM}.
FT   TURN         72     74       {ECO:0000244|PDB:3JAM}.
FT   STRAND       77     83       {ECO:0000244|PDB:3JAM}.
FT   HELIX        86     94       {ECO:0000244|PDB:3JAM}.
FT   STRAND      100    105       {ECO:0000244|PDB:3JAM}.
SQ   SEQUENCE   108 AA;  12312 MW;  03ECB94F3EF3A417 CRC64;
     MSIENLKSFD PFADTGDDET ATSNYIHIRI QQRNGRKTLT TVQGVPEEYD LKRILKVLKK
     DFACNGNIVK DPEMGEIIQL QGDQRAKVCE FMISQLGLQK KNIKIHGF
//
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