ID   EF1AS_PORPU             Reviewed;         515 AA.
AC   P50257;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Elongation factor 1-alpha S;
DE            Short=EF-1-alpha S;
DE   AltName: Full=Sporophyte-specific EF-1-alpha;
GN   Name=TEF-S;
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 only in the sporophyte, a shell-boring,
CC       filamentous phase.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U08841; AAA61790.1; -; mRNA.
DR   AlphaFoldDB; P50257; -.
DR   SMR; P50257; -.
DR   PRIDE; P50257; -.
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; 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; 2.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..515
FT                   /note="Elongation factor 1-alpha S"
FT                   /id="PRO_0000090944"
FT   DOMAIN          5..258
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          70..74
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          91..94
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          151..154
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          187..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..224
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          396..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         151..154
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         289
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         334
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         441
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
SQ   SEQUENCE   515 AA;  56648 MW;  EBA03F4029F62350 CRC64;
     MGKEKTHINL VVIGHVDAGK STTTGHLIYK LGGIDARTIA KFEADAKEMG KSSFKYAWVL
     DKLKAERERG ITIDIALWKF STAKFEYTVI DAPGHRDFIK NMITGTSQAD VALLVIDGNN
     FEAGIAEGGS TKEHALLAYT LGVKQLAVGI NKMDDVKDKD GGPWAQGRYN EVVDYLGPEL
     MKIGFKKKDK GDKKKGDKKE KKDKKDKGEK KYVCSATFVP ISGWTGDNML EKSTNMPWYT
     GPTLFEVLDA MKPPKRPTED PLRLPLQDVY KIGGIGTVPV GRVETGILKA GMQVTFEPAG
     KAAVEVKSVE MHHTSVPQAI PGDNVGFNVK LTVKDIKRGD VCGDTKNDPP IPTECFLANV
     IIQDHKNIRN GYTPVLDCHT AHIACKFASI LSKKDKRGKQ THDVSDDTEW ATKDDAEPRN
     NRMNIAAKTG ESVNVWLQPT KAMVVEAYSM YSPLGRFAVR DMKKTVAVGV IQCVQPRNMA
     KGATEELPIR GESDAVSKYI KFRPLPLKAG KKAKK