ID   EF1AC_PORPU             Reviewed;         449 AA.
AC   P50256;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Elongation factor 1-alpha C;
DE            Short=EF-1-alpha C;
GN   Name=TEF-C;
OS   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Avonport;
RX   PubMed=8704161; DOI=10.1007/bf00020608;
RA   Liu Q.Y., Baldauf S.L., Reith M.E.;
RT   "Elongation factor 1 alpha genes of the red alga Porphyra purpurea include
RT   a novel, developmentally specialized variant.";
RL   Plant Mol. Biol. 31:77-85(1996).
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   -!- DEVELOPMENTAL STAGE: Expressed in both sporophyte and gametophyte
CC       phases of the life cycle.
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; U08844; AAA61793.1; -; mRNA.
DR   AlphaFoldDB; P50256; -.
DR   SMR; P50256; -.
DR   PRIDE; P50256; -.
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 C"
FT                   /id="PRO_0000090943"
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;  49174 MW;  21C76036B1ABE4DE CRC64;
     MGKEKQHVSI VVIGHVDSGK STTTGHLIYK CGGIDKRAIE KFEKEAAEMG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETDKYNFTII DAPGHRDFIK NMITGTSQAD LAILVIASPP
     GEFEAGISQN GQTREHALLA YTLGVKQMIV ACNKMDDKNV NWSKERYEEV SKEMDLYLKK
     VGYNPPKVPK VPTSGWTGEN LFERTGGDHA LGKWYKGPCL LEALDACDPP KRPVDKPLRL
     PLQDVYKIGG IGTVPVGRVE TGVIKPGMVV TFAPSGLSTE VKSVEMHHEA LTQAGPGDNV
     GFNVKNVSVK DLKRGYVCGD SKNDPPKGCA SFNAQVIILN HPGEIHAGYA PVLDCHTAHI
     ACKFSELILK MDRRSGKKLE DSPKMIKSGD AAMVKMVASK PMCVEAFTSY PPLGRFAVRD
     MRQTVAVGVI KSVEKKEVEG KMTKSAAKK