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 13-SEP-2023, entry version 90. 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; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; 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., Chillingworth T., RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R., RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S., RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P., RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K., RA 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-codon CC backward translocation of tRNAs on improperly translocated ribosomes. CC Binds to mitochondrial ribosomes in a GTP-dependent manner. CC {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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03137}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP- CC Rule:MF_03137}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_03137}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03137}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. LepA subfamily. CC {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 AlphaFoldDB; A4I9M7; -. DR SMR; A4I9M7; -. DR STRING; 5671.XP_001468446.1; -. DR GeneID; 5072522; -. DR KEGG; lif:LINJ_34_0590; -. DR VEuPathDB; TriTrypDB:LINF_340011300; -. DR eggNOG; KOG0462; Eukaryota. DR InParanoid; A4I9M7; -. DR OMA; LIFDSWF; -. DR OrthoDB; 5473535at2759; -. 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; 3.30.70.240; -; 1. DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1. DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 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; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43512:SF7; TRANSLATION FACTOR GUF1, MITOCHONDRIAL; 1. DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF06421; LepA_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2. 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 GTP-binding; Hydrolase; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Transit peptide. FT TRANSIT 1..66 FT /note="Mitochondrion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137" FT CHAIN 67..834 FT /note="Translation factor GUF1 homolog, mitochondrial" FT /id="PRO_0000402858" FT DOMAIN 129..314 FT /note="tr-type G" FT REGION 363..385 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 476..507 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 367..384 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 138..145 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137" FT BINDING 205..209 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137" FT BINDING 259..262 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="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 //