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