EF1A2_DICDI
ID EF1A2_DICDI Reviewed; 453 AA.
AC P0CT32; P18624; Q55E03;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
DE AltName: Full=50 kDa actin-binding protein;
DE AltName: Full=ABP-50;
GN Name=eef1a2; Synonyms=efaa2, efaAII; ORFNames=DDB_G0269136;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-450, PARTIAL PROTEIN SEQUENCE, AND
RP INTERACTION WITH ACTIN.
RC STRAIN=AX3;
RX PubMed=2215665; DOI=10.1038/347494a0;
RA Yang F., Demma M., Warren V., Dharmawardhane S., Condeelis J.;
RT "Identification of an actin-binding protein from Dictyostelium as
RT elongation factor 1a.";
RL Nature 347:494-496(1990).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis. It is also
CC an abundant actin filament bundling protein.
CC -!- SUBUNIT: Binds to actin.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X55972; CAA39442.1; -; mRNA.
DR EMBL; AAFI02000005; EAL71918.1; -; Genomic_DNA.
DR PIR; S11665; S11665.
DR RefSeq; XP_645839.1; XM_640747.1.
DR RefSeq; XP_645978.1; XM_640886.1.
DR AlphaFoldDB; P0CT32; -.
DR SMR; P0CT32; -.
DR PRIDE; P0CT32; -.
DR EnsemblProtists; EAL71918; EAL71918; DDB_G0269136.
DR GeneID; 8616783; -.
DR GeneID; 8616922; -.
DR KEGG; ddi:DDB_G0269134; -.
DR KEGG; ddi:DDB_G0269136; -.
DR dictyBase; DDB_G0269136; efaAII.
DR HOGENOM; CLU_007265_3_5_1; -.
DR OMA; AIRDMGM; -.
DR PhylomeDB; P0CT32; -.
DR Reactome; R-DDI-156842; Eukaryotic Translation Elongation.
DR Reactome; R-DDI-3371511; HSF1 activation.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-8876725; Protein methylation.
DR PRO; PR:P0CT32; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0030027; C:lamellipodium; IDA:dictyBase.
DR GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0003785; F:actin monomer binding; IDA:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0010446; P:response to alkaline pH; IDA:dictyBase.
DR GO; GO:0006412; P:translation; IDA:dictyBase.
DR GO; GO:0006414; P:translational elongation; IDA:dictyBase.
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; IPR005225; Small_GTP-bd_dom.
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 TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Direct protein sequencing; Elongation factor;
KW GTP-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..453
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000424064"
FT DOMAIN 5..230
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 194..196
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"
SQ SEQUENCE 453 AA; 49662 MW; 5D608E4B722CE003 CRC64;
MGKEKTHINI VVIGHVDAGK STTTGHLIYK CGGIDKRVIE KYEKEASEMG KQSFKYAWVM
DKLKAERERG ITIDIALWKF ETSKYYFTII DAPGHRDFIK NMITGTSQAD CAVLVIASPT
GEFEAGIAKN GQTREHALLA YTLGVKQMIV AINKMDEKST NYSQARYDEI VKEVSSFIKK
IGYNPEKVAF VPISGWNGDN MLERSDKMEW YKGPTLLEAL DAIVEPKRPH DKPLRIPLQD
VYKIGGIGTV PVGRVETGII KPGMVVTFAP AGLSTEVKSV EMHHEQLPEA RPGDNVGFNV
KNVSVKEIKR GMVAGDSKND PPQETEKFVA QVIVLNHPGQ IHAGYSPVLD CHTAHIACKF
TEIVDKVDRR TGAVVAKEGT AAVVLKNGDA AMVELTPSRP MCVESFTEYP PLGRFAVRDM
RQTVAVGVIK STVKKAPGKA GDKKGAAAPS KKK
