ID C9DDZ6_9METZ Unreviewed; 411 AA.
AC C9DDZ6;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF1a {ECO:0000313|EMBL:ACV87929.1};
OS Darwinella muelleri.
OC Eukaryota; Metazoa; Porifera; Demospongiae; Keratosa; Dendroceratida;
OC Darwinellidae; Darwinella.
OX NCBI_TaxID=662694 {ECO:0000313|EMBL:ACV87929.1};
RN [1] {ECO:0000313|EMBL:ACV87929.1}
RP NUCLEOTIDE SEQUENCE.
RA Sperling E.A., Pisani D., Peterson K.J.;
RT "Poriferan paraphyly and its implications for Precambrian palaeobiology.";
RL (In) Vickers-Rich, P. and Komarower, P. (eds.);
RL THE RISE AND FALL OF THE EDIACARAN BIOTA, pp.355-368, Geological Society,
RL London (2007).
RN [2] {ECO:0000313|EMBL:ACV87929.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19597161; DOI=10.1093/molbev/msp148;
RA Sperling E.A., Peterson K.J., Pisani D.;
RT "Phylogenetic-signal dissection of nuclear housekeeping genes supports the
RT paraphyly of sponges and the monophyly of Eumetazoa.";
RL Mol. Biol. Evol. 26:2261-2274(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|RuleBase:RU000325}.
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; GQ330927; ACV87929.1; -; mRNA.
DR AlphaFoldDB; C9DDZ6; -.
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:SF308; ELONGATION FACTOR 1-ALPHA; 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 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ACV87929.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ACV87929.1}.
FT DOMAIN 1..226
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV87929.1"
FT NON_TER 411
FT /evidence="ECO:0000313|EMBL:ACV87929.1"
SQ SEQUENCE 411 AA; 45053 MW; A3113D500A774F64 CRC64;
DSGKSTTTGH LIYKCGGIDK RAIEKFEKEA QEMGKGSFKY AWVLDKLKAE RERGITIDIA
LWKFETKKYY ITVIDAPGHR DFIKNMITGT SQADCAVLIV AAGVGEFEAG ISKNGQTREH
ALLAYTLGVK QLIVGINKMD STEPPYSEAR YNEIVKEVSG YIKKIGYNPK AVAFVPISGW
HGDNMLEKSD KMSWFKAWSI ERKEGTANGT TLFEALDSIL PPKRPTDKPL RLPLQDVYKI
GGIGTVPVGR VETGVLKPGM VVTIAPANIT TEVKSVEMHH ESLTEALPGD NVGFNVKNVS
VKEIRRGMVA GDSKSDPPKK AANFTAQVII LNHPGQISNG YAPVLDCHTA HIACKFAEIK
EKCDRRSGKK LEDNPKFVKS GDSAIIQLVP SKPMCVGAFS EYPPLGRFAV R
//
