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EF1A_RHYAM
ID   EF1A_RHYAM              Reviewed;         412 AA.
AC   P27634;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
DE   Flags: Fragment;
OS   Rhynchosciara americana (Fungus gnat).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Sciaroidea; Sciaridae;
OC   Rhynchosciara.
OX   NCBI_TaxID=7186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=1641343; DOI=10.1093/nar/20.14.3780;
RA   Graessmann M., Graessmann A., Caradid E.O., Yokasawa J., Stocker A.J.,
RA   Lara F.J.S.;
RT   "Characterization of the elongation factor 1-alpha gene of Rhynchosciara
RT   americana.";
RL   Nucleic Acids Res. 20:3780-3780(1992).
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; X66131; CAA46922.1; -; mRNA.
DR   PIR; S26293; S26293.
DR   PRIDE; P27634; -.
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.
FT   CHAIN           <1..412
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090915"
FT   DOMAIN          <1..191
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         40..44
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..105
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         250
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         323
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   412 AA;  44740 MW;  0018D304269C4BE6 CRC64;
     GSFKYAWVLD KLKAERERGI TIDIALWKFE TAKYYVTIID APGHRDFIKN MITGTSQADC
     AVLIVAAGTG EFEAGISKNG QTREHALLAF TLGVKQLIVG VNKMDSTEPP FSENRYEEIK
     KEVSSYIKKI GYNPVAVAFV PISGWHGDNM LEPSSNMRWL KGWKVERING NGEGKCGSXA
     LDAILPPPRP TDQALRLPLP DVYKIGGIGT VPVGRLETGI LKPGTVVVFA PANITTEVKS
     VEMHHEALTE AVPGDNVGFN VKNVSVKELR RGYVAGDSKA NPPKGAENFT AQVIVLNHPG
     QISNGYTPVL DCHTAHIACK FAEIKXKVDR RSGKSTEDNP KAIKSGDAAI VILQPSKPLC
     VESFQEFPPL GRFAVRDMRQ TVAVGVIKSV VFKDATGRKV TKAAEKATKG KK
 
 
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