GUF1_LEIIN
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 03-AUG-2022, entry version 86.
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}.
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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; MVQIAIQ; -.
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 Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43512; PTHR43512; 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; 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 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
