ID   EF1A_NEOYE              Reviewed;         449 AA.
AC   Q8LPC4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=TU-1;
RA   Fukuda S., Ootsuka S., Kitade Y., Watanabe T., Saga N.;
RT   "Isolation, characterization and expression of a cDNA encoding an
RT   elongation factor-1 alpha from Porphyra yezoensis (Bangiales,
RT   Rhodophyta).";
RL   Phycol. Res. 50:11-15(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TU-1;
RA   Fukuda S., Kitade Y., Miyamoto H., Nagashima S., Takahashi S., Ohba T.,
RA   Asada K., Kato I., Saga N.;
RT   "Isolation and characterization of an elongation factor-1 alpha gene in
RT   Porphyra yezoensis (Rhodophyta).";
RL   J. Appl. Phycol. 15:81-86(2003).
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; AB048204; BAB96818.1; -; mRNA.
DR   EMBL; AB098024; BAC77640.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8LPC4; -.
DR   SMR; Q8LPC4; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..449
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000277249"
FT   DOMAIN          5..234
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"
FT   MOD_RES         55
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         79
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         187
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         265
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         310
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         400
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
SQ   SEQUENCE   449 AA;  49358 MW;  91546AB7A1F9A228 CRC64;
     MGKEKQHVSI VVIGHVDSGK STTTGHLIYK CGGIEKRAIE KFEKEAAEMG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETEKYSFTII DAPGHRDFIK NMITGTSQAD LAILVIASPP
     GEFEAGISQN GQTREHALLA YTLGVKQMIV ACNKMDDKNV NWSQDRYEEV SKEMDLYLKK
     VGYNPAKVPK VPTSGWTGEN LFERTDKTHA LGKWYKGPCL LEALDNCDPP KRPVDKPLRL
     PLQDVYKIGG IGTVPVGRVE TGLIKPGMVV TFAPSGLSTE VKSVEMHHEA LPQAGPGDNV
     GFNVKNVSVK DLKRGYVCGD SKNDPPKGCA SFNAQVIILN HPGEIHAGYA PVLDCHTAHI
     ACKFSELILK MDRRSGKKLE DTPKMIKSGD AAMVKMVASK PMCVEAFTQY PPLGRFAVRD
     MRQTVAVGVI KSVEKKEVEG KMTKSAAKK