GUF1_PLAVS
ID GUF1_PLAVS Reviewed; 910 AA.
AC A5K6I6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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};
GN ORFNames=PVX_099025;
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I;
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q.,
RA Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
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 -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {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 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAKM01000007; EDL44927.1; -; Genomic_DNA.
DR RefSeq; XP_001614654.1; XM_001614604.1.
DR AlphaFoldDB; A5K6I6; -.
DR SMR; A5K6I6; -.
DR STRING; 126793.A5K6I6; -.
DR PRIDE; A5K6I6; -.
DR EnsemblProtists; EDL44927; EDL44927; PVX_099025.
DR GeneID; 5473945; -.
DR KEGG; pvx:PVX_099025; -.
DR VEuPathDB; PlasmoDB:PVX_099025; -.
DR InParanoid; A5K6I6; -.
DR OMA; MVQIAIQ; -.
DR PhylomeDB; A5K6I6; -.
DR Proteomes; UP000008333; Chromosome 7.
DR Proteomes; UP000008333; Unassembled WGS sequence.
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; IPR041095; EFG_II.
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; 3.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 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; 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.
FT CHAIN 1..910
FT /note="Translation factor GUF1 homolog, mitochondrial"
FT /id="PRO_0000402854"
FT DOMAIN 189..366
FT /note="tr-type G"
FT REGION 126..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 259..263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 313..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 910 AA; 101952 MW; B97FD926D6872807 CRC64;
MIHAWAIKRA LCIFILINCV LKLERSLKVT WKSKRGFHTP VDGANGCERE WKRRGVFFSI
RRGSNRKAAR LRKAFRGVGT GGRPLFRGGK FIPLFLLRDC QRSGLNENQY KLTGRRCSSR
LEVAPRRGNG LPFERRSGGA IGATGQLEDG GPDGGSPPGV QANTSRRSHS SGCSSSGSDG
GGAPEHPQQN VRNFCILAHI DSGKSTLADR FLELTKTIKK KKMQDQFLDM MSLEREKGIT
IKLKAVRMNY QNYIFNLIDT PGHFDFYHEV KRSLSVCEGA ILLIDGSKGI QSQTLNIFLE
LQKHNLKIIP VINKIDLNVC RLDEIETDLL SKFHFMKKDI LHISAKYAQG VESLFQRIVS
DIPCPAIKSN AFFRAIVFDS FYDQYKGVIL IIKVLNGVLT KKTEVFFIQS EKTSIIQEVG
YLTPDMKPTE SIRQGDIAYV SCNMRKCDDV QISETIVSRD IVKMNAHRKL VVDLDRLGGE
RTGEAHTNVT RCGVESLRGA APPVEMHTER EIHLEQMAAS KVDVSYPVVF CNIYSVSDKQ
ANELEAALNK LKLNDASFSF KPDVCETLGK GFKCGFNGLL HLNIIQERIK REYGVETIVT
APSVNYLVRV KERGIDKQLR ERLVDARFDI AHVNVAAGGS GDGRADGSAD GSADGSADGS
GDSSAHGSSD RRGAGCARGS DDIIGNNPPE GLYYMTSNVN DIPQKNYVQG IYEPYVRTSI
VTPEEYQKHI MAECFQRRGI FIKKENINSH VIFHFDMPLS EILINFLDQI KSCTKGYGSM
SYESYITYRE SDLHKINIYV NNRSIDSLSF LAHKLNYQEK GKRIVLKLKE MIKPHQFLVV
IQAGVGTRIF ASERINPIRK NVTAKCYGGD ITRRRKLLEK QSAGKKKMFS IGKVKLPPNM
FTKLFDLKAQ
