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EF1A3_SCHPO
ID   EF1A3_SCHPO             Reviewed;         460 AA.
AC   P0CT55; 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 37.
DE   RecName: Full=Elongation factor 1-alpha-B/C;
DE            Short=EF-1-alpha-B/C;
GN   Name=tef103; Synonyms=ef1a-c, tef1c, tef1d;
GN   ORFNames=SPBC24E9.15c, SPBC839.15c;
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 [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   [3]
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 326-460.
RC   STRAIN=972 / ATCC 24843;
RA   Jang Y.-J., Yoo H.-S.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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; D82572; BAA11570.1; -; mRNA.
DR   EMBL; CU329671; CAB46708.1; -; Genomic_DNA.
DR   EMBL; U97366; AAB63858.1; -; mRNA.
DR   PIR; B41453; B41453.
DR   PIR; T38230; T38230.
DR   PIR; T42089; T42089.
DR   RefSeq; NP_594440.1; NM_001019869.2.
DR   RefSeq; NP_595255.1; NM_001021161.2.
DR   AlphaFoldDB; P0CT55; -.
DR   SMR; P0CT55; -.
DR   STRING; 284812.P0CT55; -.
DR   iPTMnet; P0CT55; -.
DR   EnsemblFungi; SPAC23A1.10.1; SPAC23A1.10.1:pep; SPAC23A1.10.
DR   EnsemblFungi; SPBC839.15c.1; SPBC839.15c.1:pep; SPBC839.15c.
DR   GeneID; 2539917; -.
DR   GeneID; 2541984; -.
DR   KEGG; spo:SPAC23A1.10; -.
DR   KEGG; spo:SPBC839.15c; -.
DR   PomBase; SPBC839.15c; tef103.
DR   VEuPathDB; FungiDB:SPAC23A1.10; -.
DR   VEuPathDB; FungiDB:SPBC839.15c; -.
DR   OMA; AIRDMGM; -.
DR   PhylomeDB; P0CT55; -.
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:P0CT55; -.
DR   Proteomes; UP000002485; Chromosome II.
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-B/C"
FT                   /id="PRO_0000433409"
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        412
FT                   /note="A -> S (in Ref. 4; AAB63858)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        416
FT                   /note="Y -> YV (in Ref. 4; AAB63858)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  49675 MW;  2D8429568A5F98D4 CRC64;
     MGKEKGHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEATELG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETPKYNVTVI DAPGHRDFIK NMITGTSQAD CAILIIGGGT
     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
 
 
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