GUF1_LEIBR
ID GUF1_LEIBR Reviewed; 831 AA.
AC A4HAG7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, 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=LbrM20_V2.0500, LbrM_20_0500;
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904;
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; FR798994; CAM38396.1; -; Genomic_DNA.
DR RefSeq; XP_001564337.1; XM_001564287.1.
DR AlphaFoldDB; A4HAG7; -.
DR SMR; A4HAG7; -.
DR STRING; 5660.A4HAG7; -.
DR GeneID; 5414881; -.
DR KEGG; lbz:LBRM_20_0500; -.
DR VEuPathDB; TriTrypDB:LbrM.20.0500; -.
DR VEuPathDB; TriTrypDB:LBRM2903_200011700; -.
DR InParanoid; A4HAG7; -.
DR OMA; MVQIAIQ; -.
DR Proteomes; UP000007258; Chromosome_20_34.1.
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..68
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT CHAIN 69..831
FT /note="Translation factor GUF1 homolog, mitochondrial"
FT /id="PRO_0000402857"
FT DOMAIN 130..315
FT /note="tr-type G"
FT BINDING 139..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 206..210
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 260..263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 831 AA; 90908 MW; D9290DCB7CBFFB34 CRC64;
MKRHGVCNTS GVALTRYSER LRFRTTHYGN GNMATSHQSC CGRRLDFYTG PGKGWCFTSL
LPVLRRYCSA SSSSTTAVAP VQAHGEDLYV SHYAIPEDAH RLVGTPQLLP RSPAEEVAFK
KSLIKSFPQA CIRNVSVVAH VDHGKTTLAD AMLRFSNLLP ADGATGTFTD RLQVEKERGI
TIKAQTCSVL LTLRETGTQY LVNLIDTPGH VDFQYEVSRS LRASEGAALL VDVRQGVEAQ
TMAQFYAALE QNLTILPVLT KMDSVMNDAE VEKTLLQLED STGLLSREAV LTSAKSKQGI
EQLFQHIIDK VPPPRGRAGF SDMKQLPIMH ADSAERKQME KELVPLRALL FDCWTAESSG
MTDGAASAPA SAATSFSSVS SGTVTASGGQ PVAREGIYGL IRVMDGTVTP GTMVTFCHSG
KKHEVREVGI IHPTLHPTAA LTAGMVGFVF FPGLTKRDVF IGDTLCTLPT RKHTVRVGVS
NIPAAELGTE PTATAELASS DSFAVEPIPG FKTVHPVVFA GFYPDEGVYI TQLRDAVDLL
CVNDPSVTME QLQCPTLGPG LQLGFLGFLH MQVFKERLLM EFGQTVLVTP PQVQYMYVEQ
HCDPGDPAQR KPVSVSNWRW PHEGVGAYLE PFVTATVLTP TQYFSEINSA ALSSFRGEMQ
EMRVIDDART LVRYRMPLAD LARGFFSTVK SSSHGYATLE YDDLTYMAAD LVKMDIVINK
ARISALSTIC LRHEANTHAR RIICSLKENL LRSSVDLPLQ ALVGSKIITR ETVKAYRKDV
TAKIHAGDIS RKQKKWNDQK KGKERMARRS VGTVTLDQSV LAAAMGATTA R
