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Elongation factor 1-gamma 1 (EF-1-gamma 1) (Calcium and membrane-binding protein 1) (Calcium phospholipid-binding protein) (CPBP) (Eukaryotic elongation factor 1Bgamma 1) (eEF1Bgamma 1) (Translation elongation factor 1B gamma 1)

 EF1G1_YEAST             Reviewed;         415 AA.
P29547; D6W3W6; Q9URC6;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
07-NOV-2018, entry version 181.
RecName: Full=Elongation factor 1-gamma 1;
Short=EF-1-gamma 1;
AltName: Full=Calcium and membrane-binding protein 1;
AltName: Full=Calcium phospholipid-binding protein;
Short=CPBP;
AltName: Full=Eukaryotic elongation factor 1Bgamma 1;
Short=eEF1Bgamma 1;
AltName: Full=Translation elongation factor 1B gamma 1;
Name=CAM1; Synonyms=TEF3; OrderedLocusNames=YPL048W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8247005; DOI=10.1128/MCB.13.12.7901;
Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr.;
"DRS1 to DRS7, novel genes required for ribosome assembly and function
in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 13:7901-7912(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8465602; DOI=10.1002/yea.320090206;
Kambouris N.G., Burke D.J., Creutz C.E.;
"Cloning and genetic characterization of a calcium- and phospholipid-
binding protein from Saccharomyces cerevisiae that is homologous to
translation elongation factor-1 gamma.";
Yeast 9:151-163(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
PROTEIN SEQUENCE OF 357-373.
PubMed=1882548; DOI=10.1002/yea.320070305;
Creutz C.E., Snyder S.L., Kambouris N.G.;
"Calcium-dependent secretory vesicle-binding and lipid-binding
proteins of Saccharomyces cerevisiae.";
Yeast 7:229-244(1991).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
FUNCTION IN TRANSCRIPTIONAL REGULATION, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12824466; DOI=10.1073/pnas.1432898100;
Hanbauer I., Boja E.S., Moskovitz J.;
"A homologue of elongation factor 1 gamma regulates methionine
sulfoxide reductase A gene expression in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 100:8199-8204(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-219, INTERACTION WITH EFB1,
AND PUTATIVE STRUCTURE OF THE EEF1 COMPLEX.
PubMed=12972429; DOI=10.1074/jbc.M306630200;
Jeppesen M.G., Ortiz P.A., Shepard W., Kinzy T.G., Nyborg J.,
Andersen G.R.;
"The crystal structure of the glutathione S-transferase-like domain of
elongation factor 1Bgamma from Saccharomyces cerevisiae.";
J. Biol. Chem. 278:47190-47198(2003).
-!- FUNCTION: Subunit of the eukaryotic elongation factor 1 complex
(eEF1). Probably plays a role in anchoring the complex to other
cellular components. May be involved in transcriptional regulation
of MXR1. {ECO:0000269|PubMed:12824466}.
-!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
-!- SUBUNIT: The eukaryotic elongation factor 1 complex (eEF1) is
probably a heterohexamer. Two trimeric complexes, each composed of
eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or
TEF4), are probably dimerized via the eF1Bgamma subunits. The
eEF1B subcomplex with the GEF activity is formed of eEF1Balpha and
eEF1Bgamma. CAM1 interacts with EFB1. Component of a complex bound
to MXR1 promoter region. {ECO:0000269|PubMed:12972429}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- DOMAIN: Ths GST-like domain mediates the interaction to eEFB1 and
may be responsible for dimerization of the eEF1 complex.
-!- MISCELLANEOUS: Present with 60865 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: There are 2 isoforms for eEF1Bgamma in yeast.
-----------------------------------------------------------------------
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EMBL; L01879; AAA16892.1; -; Unassigned_DNA.
EMBL; X67917; CAA48116.1; -; Genomic_DNA.
EMBL; U44030; AAB68173.1; -; Genomic_DNA.
EMBL; BK006949; DAA11382.1; -; Genomic_DNA.
PIR; S29345; S29345.
RefSeq; NP_015277.1; NM_001183862.1.
PDB; 1NHY; X-ray; 3.00 A; A=1-219.
PDBsum; 1NHY; -.
ProteinModelPortal; P29547; -.
SMR; P29547; -.
BioGrid; 36132; 176.
ComplexPortal; CPX-2854; Elongation Factor eEF1 complex, variant CAM1.
DIP; DIP-6813N; -.
IntAct; P29547; 11.
MINT; P29547; -.
STRING; 4932.YPL048W; -.
CarbonylDB; P29547; -.
iPTMnet; P29547; -.
MaxQB; P29547; -.
PaxDb; P29547; -.
PRIDE; P29547; -.
EnsemblFungi; YPL048W; YPL048W; YPL048W.
GeneID; 856059; -.
KEGG; sce:YPL048W; -.
SGD; S000005969; CAM1.
GeneTree; ENSGT00390000007552; -.
HOGENOM; HOG000201196; -.
InParanoid; P29547; -.
KO; K03233; -.
OMA; DYEVYDW; -.
OrthoDB; EOG092C37XH; -.
BioCyc; YEAST:G3O-33961-MONOMER; -.
Reactome; R-SCE-156842; Eukaryotic Translation Elongation.
UniPathway; UPA00345; -.
EvolutionaryTrace; P29547; -.
PRO; PR:P29547; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005509; F:calcium ion binding; IDA:SGD.
GO; GO:0001047; F:core promoter binding; IDA:SGD.
GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:SGD.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
GO; GO:0005543; F:phospholipid binding; IDA:SGD.
GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
GO; GO:0006449; P:regulation of translational termination; IGI:SGD.
GO; GO:0042254; P:ribosome biogenesis; IGI:SGD.
GO; GO:0006414; P:translational elongation; IDA:SGD.
Gene3D; 3.30.70.1010; -; 1.
InterPro; IPR001662; EF1B_G_C.
InterPro; IPR036433; EF1B_G_C_sf.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR040079; Glutathione_S-Trfase.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00647; EF1G; 1.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
SMART; SM01183; EF1G; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF89942; SSF89942; 1.
PROSITE; PS50040; EF1G_C; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Elongation factor; Nucleus; Phosphoprotein;
Protein biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 415 Elongation factor 1-gamma 1.
/FTId=PRO_0000208831.
DOMAIN 2 78 GST N-terminal.
DOMAIN 89 215 GST C-terminal.
DOMAIN 254 415 EF-1-gamma C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00519}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 32 32 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
CONFLICT 191 191 W -> C (in Ref. 1; AAA16892).
{ECO:0000305}.
STRAND 5 7 {ECO:0000244|PDB:1NHY}.
HELIX 12 24 {ECO:0000244|PDB:1NHY}.
STRAND 29 31 {ECO:0000244|PDB:1NHY}.
HELIX 33 35 {ECO:0000244|PDB:1NHY}.
HELIX 37 43 {ECO:0000244|PDB:1NHY}.
STRAND 49 53 {ECO:0000244|PDB:1NHY}.
HELIX 55 57 {ECO:0000244|PDB:1NHY}.
STRAND 59 62 {ECO:0000244|PDB:1NHY}.
HELIX 63 73 {ECO:0000244|PDB:1NHY}.
HELIX 77 83 {ECO:0000244|PDB:1NHY}.
HELIX 90 104 {ECO:0000244|PDB:1NHY}.
TURN 105 108 {ECO:0000244|PDB:1NHY}.
HELIX 109 113 {ECO:0000244|PDB:1NHY}.
HELIX 115 118 {ECO:0000244|PDB:1NHY}.
HELIX 126 147 {ECO:0000244|PDB:1NHY}.
STRAND 151 157 {ECO:0000244|PDB:1NHY}.
HELIX 160 175 {ECO:0000244|PDB:1NHY}.
HELIX 179 184 {ECO:0000244|PDB:1NHY}.
HELIX 186 197 {ECO:0000244|PDB:1NHY}.
TURN 199 201 {ECO:0000244|PDB:1NHY}.
HELIX 202 204 {ECO:0000244|PDB:1NHY}.
SEQUENCE 415 AA; 47088 MW; 17BCE60FFB7B2890 CRC64;
MSQGTLYANF RIRTWVPRGL VKALKLDVKV VTPDAAAEQF ARDFPLKKVP AFVGPKGYKL
TEAMAINYYL VKLSQDDKMK TQLLGADDDL NAQAQIIRWQ SLANSDLCIQ IANTIVPLKG
GAPYNKKSVD SAMDAVDKIV DIFENRLKNY TYLATENISL ADLVAASIFT RYFESLFGTE
WRAQHPAIVR WFNTVRASPF LKDEYKDFKF ADKPLSPPQK KKEKKAPAAA PAASKKKEEA
KPAATETETS SKKPKHPLEL LGKSTFVLDD WKRKYSNEDT RPVALPWFWE HYNPEEYSLW
KVTYKYNDEL TLTFMSNNLV GGFFNRLSAS TKYMFGCLVV YGENNNNGIV GAVMVRGQDY
VPAFDVAPDW ESYDYAKLDP TNDDDKEFIN NMWAWDKPVS VNGEPKEIVD GKVLK


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