ID F1B1B1_9NEOP Unreviewed; 411 AA.
AC F1B1B1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Mycalesis anaxias.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Satyrini; Mycalesina; Mycalesis.
OX NCBI_TaxID=856273 {ECO:0000313|EMBL:ADX98478.1};
RN [1] {ECO:0000313|EMBL:ADX98478.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20537168; DOI=10.1186/1471-2148-10-172;
RA Kodandaramaiah U., Lees D.C., Muller C.J., Torres E., Karanth K.P.,
RA Wahlberg N.;
RT "Phylogenetics and biogeography of a spectacular Old World radiation of
RT butterflies: the subtribe Mycalesina (Lepidoptera: Nymphalidae:
RT Satyrini).";
RL BMC Evol. Biol. 10:172-172(2010).
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; HM240673; ADX98478.1; -; Genomic_DNA.
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:SF236; ELONGATION FACTOR 1-ALPHA 1; 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:ADX98478.1};
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:ADX98478.1}.
FT DOMAIN 1..226
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADX98478.1"
FT NON_TER 411
FT /evidence="ECO:0000313|EMBL:ADX98478.1"
SQ SEQUENCE 411 AA; 44871 MW; FBEAFF1EC593A085 CRC64;
DSGKSTTTGX XIYKCGGIDK RTIEKFEKEA QEMGKGSFKY AWVLDKLKAE RERGITIDIA
LWKFETAKYY VTIIDAPGHR DFIKNMITGT SQADCAVLIV AAGTGEFEAG ISKNGQTREH
ALLAFTLGVF QLIVGVNKMD STEPPYSEPR FEEIKKEVSS YIKKIGYNPA AVAFVPISGW
HGDNMLEAST KMPWFKGWQV ERKEGKADGK CLIEALDAIL PPARPTDKAL RLPLQDVYKI
GGIGTVPVGR VETGVLKPGT IVVFAPANIT TEVKSVEMHH EALQEAVPGD NVGFNVKNVS
VKELRRGYVA GDSKNNPPKG AADFTAQVIV LNHPGQISNG YTPVLDCHTA HIACKFAEIK
EKVDRRTGKS TEDNPKSIKS GDAAIVNLVP SKPLCVESFQ EFPPLGRFAV R
//
