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Protein

Elongation factor 1-alpha-B/C

Gene

tef1b

more
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi91 – 955GTPBy similarity
Nucleotide bindingi153 – 1564GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. translation elongation factor activity Source: PomBase

GO - Biological processi

  1. cytoplasmic translational elongation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_311207. Peptide chain elongation.
REACT_337862. Eukaryotic Translation Elongation.
REACT_353614. HSF1 activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-alpha-B/C
Short name:
EF-1-alpha-B/C
Gene namesi
Name:tef1b
Synonyms:ef1a-b
ORF Names:SPAC23A1.10
AND
Name:tef1c
Synonyms:ef1a-c, tef1d
ORF Names:SPBC24E9.15c, SPBC839.15c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componentsi: Chromosome I, Chromosome II

Organism-specific databases

PomBaseiSPAC23A1.10.
SPBC839.15c.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. eukaryotic translation elongation factor 1 complex Source: PomBase
  4. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Elongation factor 1-alpha-B/CPRO_0000090969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphothreonine1 Publication
Modified residuei24 – 241Phosphothreonine1 Publication
Modified residuei158 – 1581Phosphothreonine1 Publication
Modified residuei289 – 2891Phosphoserine1 Publication
Modified residuei296 – 2961Phosphoserine1 Publication
Modified residuei314 – 3141Phosphoserine1 Publication
Modified residuei388 – 3881Phosphoserine1 Publication
Modified residuei394 – 3941Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10119.
PRIDEiQ10119.

Interactioni

Protein-protein interaction databases

BioGridi276461. 5 interactions.
278469. 6 interactions.
IntActiQ10119. 1 interaction.
MINTiMINT-4697049.
STRINGi4896.SPBC839.15c-1.

Structurei

3D structure databases

ProteinModelPortaliQ10119.
SMRiQ10119. Positions 2-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 240236tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 218G1By similarity
Regioni70 – 745G2By similarity
Regioni91 – 944G3By similarity
Regioni153 – 1564G4By similarity
Regioni192 – 1943G5By similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000229291.
InParanoidiQ10119.
KOiK03231.
OMAiHMISESA.
OrthoDBiEOG715QCW.
PhylomeDBiQ10119.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A.
InterProiIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKEKGHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEATELG
60 70 80 90 100
KGSFKYAWVL DKLKAERERG ITIDIALWKF ETPKYNVTVI DAPGHRDFIK
110 120 130 140 150
NMITGTSQAD CAILIIGGGT GEFEAGISKD GQTREHALLA YTLGVKQLIV
160 170 180 190 200
AVNKMDTTGW SQARFEEIVK ETSNFIKKVG FNPKTVPFVP VSGFQGDNMI
210 220 230 240 250
EPTTNMPWYQ GWQKETKAGV VKGKTLLEAI DSIEPPARPT DKPLRLPLQD
260 270 280 290 300
VYKIGGIGTV PVGRVETGVI KPGMIVTFAP AGVTTEVKSV EMHHESLDAG
310 320 330 340 350
LPGDNVGFNV KNVSVKDIRR GNVCGDSKND PPMGCASFTA QVIILNHPGQ
360 370 380 390 400
ISAGYSPVLD CHTAHIACKF AELIEKIDRR SGKKIEESPK FVKSGDACIA
410 420 430 440 450
KMVPSKPMCV EAFTDYAPLG RFAVRDMRQT VAVGVIKAVE KVAPGAAKVT
460
KAAVKAGAKK
Length:460
Mass (Da):49,675
Last modified:November 1, 1996 - v1
Checksum:i2D8429568A5F98D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211S → F in BAA11571 (PubMed:9099890).Curated
Sequence conflicti139 – 1391L → R in BAA11571 (PubMed:9099890).Curated
Sequence conflicti139 – 1391L → V in BAA19867 (PubMed:9501991).Curated
Sequence conflicti388 – 3881S → A in AAP86554 (PubMed:12748053).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82572 mRNA. Translation: BAA11570.1.
D82573 mRNA. Translation: BAA11571.1.
D89112 mRNA. Translation: BAA19867.1.
CU329670 Genomic DNA. Translation: CAA16984.1.
CU329671 Genomic DNA. Translation: CAB46708.1.
AF402093 Genomic DNA. Translation: AAP86554.1.
PIRiB41453.
T38230.
T42089.
RefSeqiNP_594440.1. NM_001019869.2.
NP_595255.1. NM_001021161.2.

Genome annotation databases

EnsemblFungiiSPAC23A1.10.1; SPAC23A1.10.1:pep; SPAC23A1.10.
SPBC839.15c.1; SPBC839.15c.1:pep; SPBC839.15c.
GeneIDi2539917.
2541984.
KEGGispo:SPAC23A1.10.
spo:SPBC839.15c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82572 mRNA. Translation: BAA11570.1.
D82573 mRNA. Translation: BAA11571.1.
D89112 mRNA. Translation: BAA19867.1.
CU329670 Genomic DNA. Translation: CAA16984.1.
CU329671 Genomic DNA. Translation: CAB46708.1.
AF402093 Genomic DNA. Translation: AAP86554.1.
PIRiB41453.
T38230.
T42089.
RefSeqiNP_594440.1. NM_001019869.2.
NP_595255.1. NM_001021161.2.

3D structure databases

ProteinModelPortaliQ10119.
SMRiQ10119. Positions 2-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276461. 5 interactions.
278469. 6 interactions.
IntActiQ10119. 1 interaction.
MINTiMINT-4697049.
STRINGi4896.SPBC839.15c-1.

Proteomic databases

MaxQBiQ10119.
PRIDEiQ10119.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC23A1.10.1; SPAC23A1.10.1:pep; SPAC23A1.10.
SPBC839.15c.1; SPBC839.15c.1:pep; SPBC839.15c.
GeneIDi2539917.
2541984.
KEGGispo:SPAC23A1.10.
spo:SPBC839.15c.

Organism-specific databases

PomBaseiSPAC23A1.10.
SPBC839.15c.

Phylogenomic databases

HOGENOMiHOG000229291.
InParanoidiQ10119.
KOiK03231.
OMAiHMISESA.
OrthoDBiEOG715QCW.
PhylomeDBiQ10119.

Enzyme and pathway databases

ReactomeiREACT_311207. Peptide chain elongation.
REACT_337862. Eukaryotic Translation Elongation.
REACT_353614. HSF1 activation.

Miscellaneous databases

NextBioi20801060.
PROiQ10119.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A.
InterProiIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comprehensive cloning of Schizosaccharomyces pombe genes encoding translation elongation factors."
    Mita K., Morimyo M., Ito K., Sugaya K., Ebihara K., Hongo E., Higashi T., Hirayama Y., Nakamura Y.
    Gene 187:259-266(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (TEF1B AND TEF1C).
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: PR745.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF1B AND TEF1C).
    Strain: 972 / ATCC 24843.
  4. "Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses."
    Kurtzman C.P., Robnett C.J.
    FEMS Yeast Res. 3:417-432(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-397.
    Strain: NRRL Y-12796.
  5. "Peptide elongation factor 1 from yeasts: purification and biochemical characterization of peptide elongation factors 1alpha and 1beta(gamma) from Saccharomyces carlsbergensis and Schizosaccharomyces pombe."
    Miyazaki M., Uritani M., Fujimura K., Yamakatsu H., Kageyama T., Takahashi K.
    J. Biochem. 103:508-521(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 64-94.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23; THR-24; THR-158; SER-289; SER-296; SER-314; SER-388 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiEF1A2_SCHPO
AccessioniPrimary (citable) accession number: Q10119
Secondary accession number(s): P78764
, Q10158, Q7M4U9, Q7Z8V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 29, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.