ID   EF1A_HYDVU              Reviewed;         468 AA.
AC   P51554;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
OS   Hydra vulgaris (Hydra) (Hydra attenuata).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schroeder J.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; Z68181; CAA92323.1; -; mRNA.
DR   RefSeq; NP_001296663.1; NM_001309734.1.
DR   AlphaFoldDB; P51554; -.
DR   SMR; P51554; -.
DR   PRIDE; P51554; -.
DR   GeneID; 100206683; -.
DR   KEGG; hmg:100206683; -.
DR   Proteomes; UP000694840; Unplaced.
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   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   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..468
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090926"
FT   DOMAIN          6..244
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          15..22
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          71..75
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          92..95
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          154..157
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          195..197
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..96
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         303
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         376
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  51110 MW;  99B7D08263F62E61 CRC64;
     MSNKVKPHIN IVVIGHVDSG KSTSTGHMIY KCGGIDKRQI EKFEKEAQEM GKGSFKYAWV
     LDKLKAERER GITIDIALWK FETTKYVVTI IDAPGHRDFI KNMITGTSQA DCAVLIVASS
     TGEFEAGISK NGQTREHALL AFTLGVKQMI VAVNKIDNTE PPYSEARFNE IKKEISAYVK
     KVGYDPKTVP VLPVSGWHGD NMIEPSPNMS WYKGWEVEYK DTGKHTGKTL LEALDNIPLP
     ARPSSKPLRL PLQDVYKIGG IGTVPVGRVE TGILKPGMVV TFCPANLSTE VKSVEMHHES
     LPEALPGDNV GFNVKNVSIK DIRRGMVASD SKNDPAIEAA SFKAQVIILN HPGEIHAGYQ
     PVLDCHTAHI ACKFAELLEK IDRRSGKVIE TEPKMVKSGD AAIINLIPSK GMCVESFSQY
     PPLGRFAVRD MRQTVAVGVI KEVDKTVAVA GKVTKSAQKA GVAAGKKK