EF1A_STYLE
ID EF1A_STYLE Reviewed; 446 AA.
AC P25166;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=EFAA;
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840642; DOI=10.1111/j.1365-2958.1991.tb00804.x;
RA Bierbaum P., Doenhoff T., Klein A.;
RT "Macronuclear and micronuclear configurations of a gene encoding the
RT protein synthesis elongation factor EF 1 alpha in Stylonychia lemnae.";
RL Mol. Microbiol. 5:1567-1575(1991).
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; X57926; CAA41001.1; -; Genomic_DNA.
DR PIR; S16308; S16308.
DR AlphaFoldDB; P25166; -.
DR SMR; P25166; -.
DR PRIDE; P25166; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..446
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090929"
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 446 AA; 49596 MW; AF76173638A6FF5A CRC64;
MPKEKNHLNL VVIGHVDSGK STSTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDIALWNF ETAKSVFTII DAPGHRDFIK NMITGTSQAD AAILIIASGQ
GEFEAGISKE GQTREHALLA FTMGVKQMIV AVNKMDDKSV NWDQGRFIEI KKELSDYLKK
IWLQPRQDPF IPISGWHGDN MLEKSPNMPW FTGSTLIDAL DALDQPKRPK DKPLRLPLQD
VYKIGGIGTV PVGRVETGLL KPGMVLTFAP MNITTECKSV EMHHESLTEA EPGDNVGFTV
KNLSVKDLRR GYVASDSKND PAKDTTNFLA QVIVLNHPGQ IQKGYAPVLD CHTAHIACKF
DEIESKVDRR SGKVLEEEPK FIKSGEAALV RMVPQKPMCV EAFNQYPPLG RFAVRDMKQT
VAVGVIKEVV KKEQKGMVTK AAQKKK