ID GUF1_LEIIN Reviewed; 834 AA. AC A4I9M7; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 1. DT 08-MAY-2019, entry version 73. DE RecName: Full=Translation factor GUF1 homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03137}; DE EC=3.6.5.-; DE AltName: Full=Elongation factor 4 homolog {ECO:0000255|HAMAP-Rule:MF_03137}; DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_03137}; DE AltName: Full=GTPase GUF1 homolog {ECO:0000255|HAMAP-Rule:MF_03137}; DE AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03137}; DE Flags: Precursor; GN ORFNames=LinJ34.0590, LinJ_34_0590; OS Leishmania infantum. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=5671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JPCM5; RX PubMed=17572675; DOI=10.1038/ng2053; RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., RA Fraser A., Rajandream M.-A., Carver T., Norbertczak H., RA Chillingworth T., Hance Z., Jagels K., Moule S., Ormond D., Rutter S., RA Sqaures R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., RA Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., RA Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., RA Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M.; RT "Comparative genomic analysis of three Leishmania species that cause RT diverse human disease."; RL Nat. Genet. 39:839-847(2007). CC -!- FUNCTION: Promotes mitochondrial protein synthesis. May act as a CC fidelity factor of the translation reaction, by catalyzing a one- CC codon backward translocation of tRNAs on improperly translocated CC ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent CC manner. {ECO:0000255|HAMAP-Rule:MF_03137}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03137}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000255|HAMAP-Rule:MF_03137}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_03137}; Matrix side {ECO:0000255|HAMAP- CC Rule:MF_03137}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. LepA CC subfamily. {ECO:0000305}. 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; FR796466; CAM71530.1; -; Genomic_DNA. DR RefSeq; XP_001468446.1; XM_001468409.1. DR STRING; 5671.XP_001468446.1; -. DR EnsemblProtists; CAM71530; CAM71530; LINJ_34_0590. DR GeneDB; LinJ.34.0590:pep; -. DR GeneID; 5072522; -. DR KEGG; lif:LINJ_34_0590; -. DR eggNOG; KOG0462; Eukaryota. DR eggNOG; COG0481; LUCA. DR HOGENOM; HOG000020624; -. DR InParanoid; A4I9M7; -. DR KO; K03596; -. DR OMA; ALIFDSW; -. DR Proteomes; UP000008153; Chromosome 34. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule. DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR CDD; cd03709; lepA_C; 1. DR Gene3D; 3.30.70.2570; -; 1. DR HAMAP; MF_00071; LepA; 1. DR InterPro; IPR006297; EF-4. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR038363; LepA_C_sf. DR InterPro; IPR013842; LepA_CTD. DR InterPro; IPR035654; LepA_IV. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF06421; LepA_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 2. 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 Complete proteome; GTP-binding; Hydrolase; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Nucleotide-binding; KW Protein biosynthesis; Reference proteome; Transit peptide. FT TRANSIT 1 66 Mitochondrion. {ECO:0000255|HAMAP- FT Rule:MF_03137}. FT CHAIN 67 834 Translation factor GUF1 homolog, FT mitochondrial. FT /FTId=PRO_0000402858. FT DOMAIN 129 314 tr-type G. FT NP_BIND 138 145 GTP. {ECO:0000255|HAMAP-Rule:MF_03137}. FT NP_BIND 205 209 GTP. {ECO:0000255|HAMAP-Rule:MF_03137}. FT NP_BIND 259 262 GTP. {ECO:0000255|HAMAP-Rule:MF_03137}. SQ SEQUENCE 834 AA; 90543 MW; 8BF38BA98D60179F CRC64; MKLCGVRSSG VSLTRSSDFP RFRAAHHGGA HTATRHQSLC GRRLDSYMGA GKRWCFRPLL AEPRRYSNAS SAFTTDGATA PAHGEGLYVS HYAMPEDARR LVGTPQLLPR NPAEEVAFKK NLIRSFPQAC IRNVSVVAHV DHGKTTLSDA MLRFSNLLPA DGATGTFTDR LKVEKERGIT IKAQTCSVLL TLRETGTQYL VNLIDTPGHV DFQYEVSRSL CASEGAALLV DVRQGVEAQT MAQFYAALEQ NLTILPVLTK MDSVMSDAEV EKTLLQLEDS TGLLSREVIL TSAKSKRGIE QLFQHIIDKV PPPCGREGFS DMKQLPAMHP GSADRKKVEK ELVPLRALLF DCWTSESSGM ADGAASAPVS TASSVSSGTA PASGGQSVAK DGIYGLIRVM DGTVTPGTTV TFFHSGKKHE VREVGIIHPT LHPTAALTAG MVGFVFFPGL LKKDVFIGDT LCTLPTRKHT MRVVATGSPA TASRTKPATA AETASSDDAS GSGSSSVVEP IPGFKTVQPV VFAGFYPDEG VYITQLREAV DLLCVNDPSV TVEQLQCPAL GPGLQLGFLG FLHMQVFKER LLMEFGQAVL VTPPQVQYMY VEQHGDPDDP AQRKPVSVSN WRWPHEGVGA YLEPFVTATV LTPSEYLNEI NSAALSAFRG EMQEMRVIDG ARTLVRYRMP LADLARGFFS TVKSSSHGYA TLEYDDLTYM TADLVKMDIV INKAHISALS TICLRHEANT HARRIIGSLK EKLLRSSVDL PLQALVGSKI IARETVKAYR KDVTAKIHAG DISRKQKKWN DQKKGKERMA RRSVGTVTLD QSVLAAALGA TTAR //