ID G5EDF5_CAEEL Unreviewed; 439 AA. AC G5EDF5; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAR-2024, entry version 106. DE SubName: Full=Elongation factor Tu, mitochondrial {ECO:0000313|EMBL:CCD65152.1}; DE SubName: Full=Mitochondrial elongation factor Tu homologue {ECO:0000313|EMBL:BAA31345.1}; GN Name=tufm-2 {ECO:0000313|EMBL:CCD65152.1, GN ECO:0000313|WormBase:C43E11.4}; GN ORFNames=C43E11.4 {ECO:0000313|WormBase:C43E11.4}, CELE_C43E11.4 GN {ECO:0000313|EMBL:CCD65152.1}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD65152.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CCD65152.1, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD65152.1, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] {ECO:0000313|EMBL:BAA31345.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12145639; DOI=10.1038/nsb826; RA Ohtsuki T., Sato A., Watanabe Y., Watanabe K.; RT "A unique serine-specific elongation factor Tu found in nematode RT mitochondria."; RL Nat. Struct. Biol. 9:669-673(2002). RN [3] {ECO:0000313|EMBL:CCD65152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD65152.1}; RA Sulson J.E., Waterston R.; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:BAA31345.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16953577; DOI=10.1021/bi060536i; RA Sato A., Watanabe Y., Suzuki T., Komiyama M., Watanabe K., Ohtsuki T.; RT "Identification of the residues involved in the unique serine specificity RT of Caenorhabditis elegans mitochondrial EF-Tu2."; RL Biochemistry 45:10920-10927(2006). RN [5] {ECO:0000313|EMBL:CCD65152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD65152.1}; RG WormBase Consortium; RA WormBase; RL Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB010028; BAA31345.1; -; mRNA. DR EMBL; BX284601; CCD65152.1; -; Genomic_DNA. DR PIR; T37273; T37273. DR RefSeq; NP_491338.2; NM_058937.4. DR SMR; G5EDF5; -. DR IntAct; G5EDF5; 1. DR MINT; G5EDF5; -. DR STRING; 6239.C43E11.4.1; -. DR PaxDb; 6239-C43E11-4; -. DR EnsemblMetazoa; C43E11.4.1; C43E11.4.1; WBGene00007001. DR GeneID; 172024; -. DR KEGG; cel:CELE_C43E11.4; -. DR AGR; WB:WBGene00007001; -. DR WormBase; C43E11.4; CE32610; WBGene00007001; tufm-2. DR eggNOG; KOG0460; Eukaryota. DR GeneTree; ENSGT00940000174062; -. DR HOGENOM; CLU_007265_0_0_1; -. DR OMA; PFDRIDR; -. DR OrthoDB; 167272at2759; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00007001; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central. DR CDD; cd01884; EF_Tu; 1. DR CDD; cd03697; EFTU_II; 1. DR CDD; cd03706; mtEFTU_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; IPR041709; EF-Tu_GTP-bd. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR033720; EFTU_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. 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; IPR004160; Transl_elong_EFTu/EF1A_C. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43721:SF33; ELONGATION FACTOR TU, MITOCHONDRIAL; 1. DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 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 1: Evidence at protein level; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, KW ECO:0000313|EMBL:CCD65152.1}; GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}; KW Proteomics identification {ECO:0007829|EPD:G5EDF5, KW ECO:0007829|PeptideAtlas:G5EDF5}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}. FT DOMAIN 43..236 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" SQ SEQUENCE 439 AA; 47831 MW; 5EE533C1A3636D5A CRC64; MNPAALSAFT RSLLFNRCST SSFCNSITRN AVAFFATAAA TPKINVNVGT IGHIDHGKTT LTSAITRVQA KKGFAKHIKF DEIDKGKEEK KRGITINVAH IGYESPLRRY SHTDCPGHSD FIKNMICGTS QMDVAVLVIA ATDGVMEQTK EHLILAKQVG VKNMAIFINK ADLVEEDDLD LVEMEARELL SLHGFNGDAT PVIRGSALSA LEGQDISCIE RLIDALDSLP EPDRNEKDTF VMPIASKTAI TGRGTVIVGT LERGVLKKGD KVEIKGDGQT LQTTASDIQV FGKSVKEVRA GDHCGVLCRG VKGDTVKRGM WAGHPGAVTI TNRVKVELYL LSEAENGRKI GIRTGFTDKM YCSTWDQVGR FDMSNELLMP GEHTSATVLL MKDMPLRKGM PFTLREGSSK TTIARGIISD LEDHVAVEKH NLKKSAEKM //