EF1A1_SCHPO
ID EF1A1_SCHPO Reviewed; 460 AA.
AC P0CT53; O14372; O14441; O59818; P50522; P78764; Q10117; Q10119; Q10158;
AC Q7M4U9; Q7Z8V5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Elongation factor 1-alpha-A;
DE Short=EF-1-alpha-A;
GN Name=tef101; Synonyms=ef1a-a, tef1a, tef1e; ORFNames=SPCC794.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9099890; DOI=10.1016/s0378-1119(96)00764-0;
RA Mita K., Morimyo M., Ito K., Sugaya K., Ebihara K., Hongo E., Higashi T.,
RA Hirayama Y., Nakamura Y.;
RT "Comprehensive cloning of Schizosaccharomyces pombe genes encoding
RT translation elongation factors.";
RL Gene 187:259-266(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10593605; DOI=10.1139/o99-055;
RA Rasmussen C., Wiebe C.;
RT "Cloning of a Schizosaccharomyces pombe homologue of elongation factor 1
RT alpha by two-hybrid selection of calmodulin-binding proteins.";
RL Biochem. Cell Biol. 77:421-430(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-64.
RC STRAIN=972 / ATCC 24843;
RA Jang Y.-J., Yoo H.-S.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 64-94.
RX PubMed=3214489; DOI=10.1093/oxfordjournals.jbchem.a122301;
RA Miyazaki M., Uritani M., Fujimura K., Yamakatsu H., Kageyama T.,
RA Takahashi K.;
RT "Peptide elongation factor 1 from yeasts: purification and biochemical
RT characterization of peptide elongation factors 1alpha and 1beta(gamma) from
RT Saccharomyces carlsbergensis and Schizosaccharomyces pombe.";
RL J. Biochem. 103:508-521(1988).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; D82571; BAA11569.1; -; mRNA.
DR EMBL; U42189; AAA85129.1; -; mRNA.
DR EMBL; D89112; BAA19867.1; -; mRNA.
DR EMBL; CU329672; CAA19136.1; -; Genomic_DNA.
DR EMBL; U97367; AAB63859.1; -; mRNA.
DR EMBL; U97373; AAB63865.1; -; mRNA.
DR PIR; B41453; B41453.
DR PIR; T41617; T41617.
DR PIR; T42089; T42089.
DR PIR; T43267; T43267.
DR PIR; T43704; T43704.
DR RefSeq; NP_587757.1; NM_001022750.2.
DR AlphaFoldDB; P0CT53; -.
DR SMR; P0CT53; -.
DR IntAct; P0CT53; 6.
DR MINT; P0CT53; -.
DR STRING; 4896.SPCC794.09c.1; -.
DR iPTMnet; P0CT53; -.
DR PaxDb; P0CT53; -.
DR EnsemblFungi; SPCC794.09c.1; SPCC794.09c.1:pep; SPCC794.09c.
DR GeneID; 2539035; -.
DR KEGG; spo:SPCC794.09c; -.
DR PomBase; SPCC794.09c; tef101.
DR VEuPathDB; FungiDB:SPCC794.09c; -.
DR eggNOG; KOG0052; Eukaryota.
DR OMA; VACTFES; -.
DR PhylomeDB; P0CT53; -.
DR Reactome; R-SPO-156842; Eukaryotic Translation Elongation.
DR Reactome; R-SPO-3371511; HSF1 activation.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8876725; Protein methylation.
DR PRO; PR:P0CT53; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; ISO:PomBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; ISO:PomBase.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IDA:PomBase.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Methylation; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT CHAIN 2..460
FT /note="Elongation factor 1-alpha-A"
FT /id="PRO_0000090968"
FT DOMAIN 5..240
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 192..194
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 3
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 3
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 30
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 316
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 316
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 390
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT CONFLICT 47
FT /note="T -> F (in Ref. 5; AAB63859/AAB63865)"
FT /evidence="ECO:0000250"
FT CONFLICT 57
FT /note="A -> S (in Ref. 5; AAB63859/AAB63865)"
FT /evidence="ECO:0000250"
FT CONFLICT 113
FT /note="V -> I (in Ref. 3; BAA19867)"
FT /evidence="ECO:0000250"
FT CONFLICT 139
FT /note="L -> R (in Ref. 1; BAA11569)"
FT /evidence="ECO:0000250"
FT CONFLICT 139
FT /note="L -> V (in Ref. 3; BAA19867)"
FT /evidence="ECO:0000250"
FT CONFLICT 140
FT /note="A -> G (in Ref. 2; AAA85129)"
FT /evidence="ECO:0000250"
FT CONFLICT 422
FT /note="F -> FG (in Ref. 2; AAA85129)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 460 AA; 49660 MW; 82EA58185D514294 CRC64;
MGKEKGHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEATELG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPKYNVTVI DAPGHRDFIK NMITGTSQAD CAVLIIGGGT
GEFEAGISKD GQTREHALLA YTLGVKQLIV AVNKMDTTGW SQARFEEIVK ETSNFIKKVG
FNPKTVPFVP VSGFQGDNMI EPTTNMPWYQ GWQKETKAGV VKGKTLLEAI DSIEPPARPT
DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KPGMIVTFAP AGVTTEVKSV EMHHESLDAG
LPGDNVGFNV KNVSVKDIRR GNVCGDSKND PPMGCASFTA QVIILNHPGQ ISAGYSPVLD
CHTAHIACKF AELIEKIDRR SGKKIEESPK FVKSGDACIA KMVPSKPMCV EAFTDYAPLG
RFAVRDMRQT VAVGVIKAVE KVAPGAAKVT KAAVKAGAKK
