ID C8YJP1_9CRUS Unreviewed; 346 AA.
AC C8YJP1;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Elongation factor-1 alpha {ECO:0000313|EMBL:ACV73090.1};
DE Flags: Fragment;
GN Name=EF-1 alpha {ECO:0000313|EMBL:ACV73090.1};
OS Limnadopsis parvispinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Spinicaudata; Limnadiidae; Limnadopsis.
OX NCBI_TaxID=299815 {ECO:0000313|EMBL:ACV73090.1};
RN [1] {ECO:0000313|EMBL:ACV73090.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W116 {ECO:0000313|EMBL:ACV73090.1};
RX PubMed=19702888; DOI=10.1111/j.1420-9101.2009.01813.x;
RA Weeks S.C., Chapman E.G., Rogers D.C., Senyo D.M., Hoeh W.R.;
RT "Evolutionary transitions among dioecy, androdioecy and hermaphroditism in
RT limnadiid clam shrimp (Branchiopoda: Spinicaudata).";
RL J. Evol. Biol. 22:1781-1799(2009).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|ARBA:ARBA00003982}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR EMBL; FJ499054; ACV73090.1; -; Genomic_DNA.
DR AlphaFoldDB; C8YJP1; -.
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 InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:ACV73090.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000313|EMBL:ACV73090.1}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV73090.1"
FT NON_TER 346
FT /evidence="ECO:0000313|EMBL:ACV73090.1"
SQ SEQUENCE 346 AA; 37659 MW; CAB58EB9B9E28852 CRC64;
RGITIDIALW KFETAKYYVT IIDAPGHRDF IKNMITGTSQ ADCAVLIVAA GVGEFEAGIS
KNGQTREHAL LAYTLGVKQL IVGVNKMDST EPPYSEARFE EIKKEVSSYI KKIGYNPVAV
PFVPISGWHG DNMLEASTNL PWYKGWAIER KEGKADGKTL IDALDAILPP SRPTEKPLRL
PLQDVYKIGG IGTVPVGRVE TGVIKPGTVV TFAPCNLTTE VKSVEMHHEA LEEAVPGDNV
GFNVKNVSVK ELRRGYVAGD SKNNPPKGAA DFYAQVIVLN HPGQISNGYT PVLDCHTAHI
ACKFAEIKEK CDRRTGKTTE ENPKFIKSGD AAMITLVPSK PLCVES
//