GUF1_PLAKH
ID GUF1_PLAKH Reviewed; 894 AA.
AC B3L3C9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=PKH_070910;
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H;
RX PubMed=18843368; DOI=10.1038/nature07306;
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R.D., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M.A., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clark T.G., Galinski M.R., Hall N., Harper D., Harris D.,
RA Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S., Marti M.,
RA Moule S., Meyer I.M., Ormond D., Peters N., Sanders M., Sanders S.,
RA Sargeant T.J., Simmonds M., Smith F., Squares R., Thurston S., Tivey A.R.,
RA Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F.,
RA Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I.,
RA Barrell B.G., Berriman M.;
RT "The genome of the simian and human malaria parasite Plasmodium knowlesi.";
RL Nature 455:799-803(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; AM910989; CAQ39162.1; -; Genomic_DNA.
DR RefSeq; XP_002258390.1; XM_002258354.1.
DR AlphaFoldDB; B3L3C9; -.
DR SMR; B3L3C9; -.
DR STRING; 5850.PKH_070910; -.
DR PRIDE; B3L3C9; -.
DR EnsemblProtists; CAQ39162; CAQ39162; PKH_070910.
DR GeneID; 7320118; -.
DR KEGG; pkn:PKNH_0709700; -.
DR VEuPathDB; PlasmoDB:PKNH_0709700; -.
DR HOGENOM; CLU_009995_2_0_1; -.
DR InParanoid; B3L3C9; -.
DR OMA; MVQIAIQ; -.
DR PhylomeDB; B3L3C9; -.
DR Proteomes; UP000031513; Chromosome 7.
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; 2.
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..894
FT /note="Translation factor GUF1 homolog, mitochondrial"
FT /id="PRO_0000402853"
FT DOMAIN 199..376
FT /note="tr-type G"
FT REGION 157..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 269..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 323..326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 894 AA; 102197 MW; 70CE1A29138CF95B CRC64;
MIDAWAIKRA LCIFILINCV LKLGRSRKIT WKPKKGVYIP LDDANGCKGE WKRKGVFFNI
QSGKKGKRLK GRKGLRRGLV TRGTPQFRRD KFIPLFLLQD CEHRSLNGKQ YNLRGRRCSS
PLDVNPRGWD ILPPEQPNEE TIGERIGERI GEAEQLEDEG LDGGPPPGME AKKSSSSSSS
NNVHSNCSDA GKAPVCSQEN IRNFCILAHI DSGKSTLADR FLELTKTIKK KKMQDQFLDM
MSLEREKGIT IKLKAVRMNY KNYIFNLIDT PGHFDFYHEV KRSLSVCEGA ILLIDGTKGI
QSQTLNIFME LQKHNLKIIP VINKIDLNIC RLEKIENDLL NKFHFMKKDI LHISAKYSHG
VESLFQRIVS EIPSPAIKSN SFFRAIVFDS FYDQYKGVIL IIKVLNGVLT KKTEVFFIQS
EKTYIIQEVG YLTPEMKPTE SIRQGDIAYV SSNIRKCDEV QMSETIISRD IVHLNAQRRL
VVDSDLLRRN PSGEEHINVK RCNIDSSLGG VAPRMERIER EVNLEEIAAS KVDVSYPVVF
CNIYSVNDKQ ANELQAALNK LKLNDASFSF KPDVCETLGK GFKCGFNGLL HLNIIQERIK
REYDVETIVT APSVNYLIRV KEKCIDKQLK ERLIDASFDI ANINVEGGDH DDCNDNGGSN
SDDRSDRSGK NPPDGLYYMT SNVNDIPQKN YIHGIYEPYV RTSIMTPEEY QKYIMAECFQ
RRGIFIKKES MDSHIIFYFD MPLSEILINF LDQIKSCTKG YGSMSYENFI TYRESDLHKI
NIYVNNRSID SLSFLAHKLN YQEKGKRIVL KLKEMIKPHQ FLVVIQAGIG TRIFASERIN
PLRKNVTAKC YGGDITRRRK LLEKQSAGKK KMFSIGKVKL PPNMFTKLFD LKAQ
