ID A1BMA2_9HYME Unreviewed; 364 AA.
AC A1BMA2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF-1 alpha {ECO:0000313|EMBL:ABB58712.1};
OS Cladomyrma maryatiae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Cladomyrma.
OX NCBI_TaxID=354279 {ECO:0000313|EMBL:ABB58712.1};
RN [1] {ECO:0000313|EMBL:ABB58712.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JL9 {ECO:0000313|EMBL:ABB58712.1};
RA LaPolla J.L., Bischoff J.F., Schultz T.R., Kjer K.M.;
RT "Phylogenetic position of the ant genus Acropyga Roger (Hymenoptera:
RT Formicidae) and the evolution of trophophoresy.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU000325}.
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,
CC ECO:0000256|RuleBase:RU000325}.
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DR EMBL; DQ226021; ABB58712.1; -; Genomic_DNA.
DR AlphaFoldDB; A1BMA2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; 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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ABB58712.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ABB58712.1}.
FT DOMAIN 1..191
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABB58712.1"
FT NON_TER 364
FT /evidence="ECO:0000313|EMBL:ABB58712.1"
SQ SEQUENCE 364 AA; 39838 MW; 7AA1D770A27E0481 CRC64;
GSFKYAWVLD KLKAERERGI TIDIALWKFE TAKYYVTIID APGHRDFIKN MITGTSQADC
AVLIVAAGIG EFEAGISKNG QTREHALLAF TLGVKQLIVG VNKMDMTDPP YSETRFEEIK
KEVSSYIKKI GYNTASVAFV PISGWHGDNM LEPSPKTPWY KGWKVERKDG NADGKTLIEA
LDAILPPSRP TDKALRLPLQ DVYKIGGIGT VPVGRVETGI LKPGMLVTFP PAALTTEVKS
VEMHHEALTE ALPGDNVGFN VKNISVKELR RGYVAGDSKN QPPRGAADFT AQVIVLNHPG
QISNGYTPVL DCHTAHIACK FAEIKEKCDR RTGKTTEENP KSIKSGDAAI VMLQPTKPMC
VEAF
//
