ID B5AHS6_9HYME Unreviewed; 370 AA.
AC B5AHS6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Ashmeadiella aff. gillettei CJP-2008.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Megachilidae; Megachilinae; Ashmeadiella.
OX NCBI_TaxID=549033 {ECO:0000313|EMBL:ACF71187.1};
RN [1] {ECO:0000313|EMBL:ACF71187.1}
RP NUCLEOTIDE SEQUENCE.
RA Praz C.J., Muller A., Danforth B.N., Griswold T.L., Widmer A., Dorn S.;
RT "Phylogeny and biogeography of bees of the tribe Osmiini (Hymenoptera:
RT Megachilidae).";
RL Mol. Phylogenet. Evol. 49:185-197(2008).
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; EU851536; ACF71187.1; -; Genomic_DNA.
DR AlphaFoldDB; B5AHS6; -.
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; IPR009001; Transl_elong_EF1A/Init_IF2_C.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
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:ACF71187.1};
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:ACF71187.1}.
FT DOMAIN 1..185
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACF71187.1"
FT NON_TER 370
FT /evidence="ECO:0000313|EMBL:ACF71187.1"
SQ SEQUENCE 370 AA; 40360 MW; 858AB486C62BCD36 CRC64;
WVLDKLKAER ERGITIDIAL WKFETSKYYV TIIDAPGHRD FIKNMITGTS QADCAVLIVA
AGTGEFEAGI SKNGQTREHA LLAFTLGVKQ LIVGVNKMDS TEPPYSETRF EEIKKEVSSY
IKKIGYNPAA VAFVPISGWH GDNMLEVSSK MPWFKGWSVE RKEGKVEGKC LIEALDAILP
PTRPTDKALR LPLQDVYKIG GIGTVPVGRV ETGVLKPGMV VTFAPAGLTT EVKSVEMHHE
ALQEAVPGDN VGFNVKSVSV KELRRGYVAG DSKNNPPKGA ADFTAQVIVL NHPGQISNGY
TPVLDCHTAH IACKFAEIKE KCDRRTGKTT EQNPKAIKSG DAAIVTLVPS KPMCVEAFQE
FPPLGRFAVR
//
