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 13-SEP-2023, entry version 91.
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 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 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:SF170; ELONGATION FACTOR 1-ALPHA 2; 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 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
//
