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Database: UniProt
Entry: A0A087Y596_POEFO
LinkDB: A0A087Y596_POEFO
Original site: A0A087Y596_POEFO 
ID   A0A087Y596_POEFO        Unreviewed;       462 AA.
AC   A0A087Y596;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN   Name=EEF1A1 {ECO:0000313|Ensembl:ENSPFOP00000013199.1};
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:ENSPFOP00000013199.1, 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:ENSPFOP00000013199.1}
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; AYCK01011845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007567352.1; XM_007567290.2.
DR   RefSeq; XP_007567353.1; XM_007567291.2.
DR   AlphaFoldDB; A0A087Y596; -.
DR   STRING; 48698.ENSPFOP00000013199; -.
DR   Ensembl; ENSPFOT00000013217.1; ENSPFOP00000013199.1; ENSPFOG00000013175.1.
DR   GeneID; 103148491; -.
DR   KEGG; pfor:103148491; -.
DR   eggNOG; KOG0052; Eukaryota.
DR   GeneTree; ENSGT00950000183029; -.
DR   OMA; WHIERNE; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:SF222; ELONGATION FACTOR 1-ALPHA 1-RELATED; 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          5..242
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   462 AA;  50437 MW;  9EF907E4FF89EF66 CRC64;
     MGKEKLHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
     DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
     GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP NYSQKRYEEI VKEVSTYIKK
     IGYNPDTVAF VPISGWNGDN MLEPSPNMTW FKGWKINRKD GSASGTTLLE ALDAIQPPTR
     PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILKPGMVVTF APVNVTTEVK SVEMHHEALS
     EALPGDNVGF NVKNVSVKDI RRGNVAGDSR NDPPQEAAGF TSQVIILNHP GQISAGYAPV
     LDCHTAHIAC KFAELKEKID RRSGKKLEDN PKFLKSGDAA IVDMIPGKPM CVESFSEYPP
     LGRFAVRDMR QTVAVGVIKG VEKKAPTSGK ITKSAQKAQK AK
//
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