ID A0A096LXY5_POEFO Unreviewed; 466 AA.
AC A0A096LXY5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000024026.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000024026.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|RuleBase:RU000325}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC ECO:0000256|RuleBase:RU000325}.
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DR EMBL; AYCK01008111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096LXY5; -.
DR Ensembl; ENSPFOT00000022614.1; ENSPFOP00000024026.1; ENSPFOG00000003924.2.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00940000164334; -.
DR OMA; KSENMEW; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF271; ELONGATION FACTOR 1-ALPHA; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT DOMAIN 10..247
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 466 AA; 51009 MW; CF5CA00978D85CF7 CRC64;
TETKTMGKEK THINIVVIGH VDSGKSTSTG HLIYKCGGID KRTIEKFEKE AAEMGKGSFK
YAWVLDKLKA ERERGITIDI ALWKFETGKY YVTIIDAPGH RDFIKNMITG TSQADCAVLI
VAAGVGEFEA GISKNGQTRE HALLAFTLGV KQLIVGVNKM DSTEPPYSQA RFEEIQKEVS
TYIKKIGYNP AAVAFVPISG WHGDNMLEAS TKMNWFKGWK VERKDGNANG TTLLDALDAI
LPPSRPTDKP LRLPLQDVYK IGGIGTVPVG RVETGVLKPG MVVTFAPPNL TTEVKSVEMH
HESLTEAVPG DNVGFNVKNV SVKEIRRGYV AGDSKNDPPK AADSFNAQVI ILNHPGQINE
GYAPVLDCHT AHIACKFKEL IEKIDRRSGK KLEDNPKFVK SGDAAIVKLI PQKPMVVEPF
SNYPPLGRFA VRDMRQTVAV GVIKAVDTKE VSGKTTKAAE KAQKKK
//
