EFGM_CULQU
ID EFGM_CULQU Reviewed; 744 AA.
AC B0WGM1;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=mEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE Flags: Precursor;
GN ORFNames=CPIJ005834;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent
CC ribosomal translocation step during translation elongation. During this
CC step, the ribosome changes from the pre-translocational (PRE) to the
CC post-translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two tRNA
CC molecules, the mRNA and conformational changes in the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; DS231927; EDS27050.1; -; Genomic_DNA.
DR RefSeq; XP_001847855.1; XM_001847803.1.
DR AlphaFoldDB; B0WGM1; -.
DR SMR; B0WGM1; -.
DR STRING; 7176.CPIJ005834-PA; -.
DR PRIDE; B0WGM1; -.
DR EnsemblMetazoa; XM_001847803.2; XP_001847855.1; LOC6038008.
DR GeneID; 6038008; -.
DR KEGG; cqu:CpipJ_CPIJ005834; -.
DR VEuPathDB; VectorBase:CPIJ005834; -.
DR VEuPathDB; VectorBase:CQUJHB003137; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; B0WGM1; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B0WGM1; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002320; Partially assembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR GO; GO:0070125; P:mitochondrial translational elongation; ISS:UniProtKB.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04097; mtEFG1_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR045044; EFG1-like.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR43636; PTHR43636; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 26..744
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385544"
FT DOMAIN 38..315
FT /note="tr-type G"
FT BINDING 47..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 114..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 168..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 744 AA; 83190 MW; 5B2FB67578E20C0F CRC64;
MTISCLLRIR PALAKSFFEN GQRAFASHAA FAEHAKLERI RNIGISAHID SGKTTLTERI
LFYTGRIKEM HEVKGKDNVG ATMDSMELER QRGITIQSAA TYTVWKDHNI NIIDTPGHVD
FTVEVERALR VLDGAVLVLC SVGGVQSQTL TVNRQMKRYN VPCLAFINKL DRMGANPYRV
LGQMKSKLNH NAAFIQLPIG VESNCKGIVD LVKQKALYFD DQLGLTVRED EIPQDMRTEC
DERRHELIEQ LSNVDDAIGE LFLEEKTPTP QDLMGAIRRS TLKRTFTPVL VGTALKNKGV
QPLLDAVLDY LPNPGEVENL AMIEKKGEEP QKVFLNPARD GKDPFVGLAF KLEAGRFGQL
TYLRCYQGVL KKGDSIFNVR SGKKVRLARL VRLHSNNMED VNEVYAGDIF ALFGVDCASG
DTFVTDPKLE LSMESIFVPD PVVSMAIKPT NTKDRDNFSK AVARFTKEDP TFRFAYDPDV
KETLVSGMGE LHLEIYAQRM EREYNCPVTL GKPKVAFRET LVAPCEFDYL HKKQSGGQGQ
YGRVTGILEP LPPHQNTVIE FTDETIGTNV PKQFVPAIEK GFRQMAEKGL LSGHKLSGLK
FRLLDGAHHI VDSSELAFML AAQGAIKSVF ENGSWQILEP VMMVEVTAPE EFQGTVIGQL
NKRHGIITGT EGTEGWFTIY AEVPLNDMFG YAGELRSSTQ GKGEFSMEYS RYSPCMPDVQ
EQLMREYQAS QGIAVPDKKQ KKKN
