GUF1_PLAF7
ID GUF1_PLAF7 Reviewed; 1085 AA.
AC Q8I335;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Translation factor GUF1 homolog, mitochondrial;
DE EC=3.6.5.-;
DE AltName: Full=Elongation factor 4 homolog;
DE Short=EF-4;
DE AltName: Full=GTPase GUF1 homolog;
DE AltName: Full=Ribosomal back-translocase;
DE Flags: Precursor;
GN ORFNames=PFI0570w;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
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 (By
CC similarity). {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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; AL844508; CAD51800.1; -; Genomic_DNA.
DR RefSeq; XP_001351989.1; XM_001351953.1.
DR AlphaFoldDB; Q8I335; -.
DR SMR; Q8I335; -.
DR BioGRID; 1208671; 1.
DR IntAct; Q8I335; 1.
DR STRING; 5833.PFI0570w; -.
DR EnsemblProtists; CAD51800; CAD51800; PF3D7_0911700.
DR GeneID; 813394; -.
DR KEGG; pfa:PF3D7_0911700; -.
DR VEuPathDB; PlasmoDB:PF3D7_0911700; -.
DR HOGENOM; CLU_009995_0_0_1; -.
DR InParanoid; Q8I335; -.
DR OMA; MVQIAIQ; -.
DR PhylomeDB; Q8I335; -.
DR Proteomes; UP000001450; Chromosome 9.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
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 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; 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..1085
FT /note="Translation factor GUF1 homolog, mitochondrial"
FT /id="PRO_0000402852"
FT DOMAIN 232..409
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 241..248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 302..306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 356..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1085 AA; 126929 MW; 30DC5AFD173766B4 CRC64;
MNYTSVNKIR LWVLIVFLIL YNIKCICENI SDLKKRLCFN NFSNSKKKIK KKWLAKKKKN
YLTIWKNKTY TTKRRNGYGK IEYKREENKK DDYNFMNTSL YLNYISNVKN FLFNKNNNKK
NKIYYHKCKK SNIIEAKIND NDTLLSDEEF RNDVDRNDKE YYNIKKEYSE NVCNQNRIND
LSNCSVSSNN NILNECSSEV KKEMNYPLHN ELYDNLNDNT IGHLKSEKCK EKYIRNFCIL
AHIDSGKSTL ADRFLELTNT IKKKRMQEQF LDMMCLEREK GITIKLKAVR MHYNNYVFNL
IDTPGHFDFY HEVKRSLNVC EGAILLIDGG KGIQSQTLNI FFELKKHDIK IIPVINKIDL
STCLYDKIKD DLINKFNFKE NEILKISAKY GKNVKMLFQR IISDIPPPIN TINSFFRGVV
FDSFFDQYKG VVLIIKVLNG ELRKKTEIFF INSAKSYIIQ EVGYLVPEMK PTDVISQGDI
AYVCSNIRNC DDIQISETIV NKDIIKKNNH NEFVINFKKI NLGRDKNIMQ RLSDEGKQYL
THHNKGEIKG DENGQVKCDE NGQVKCDENG QVKCDENGQV KCDENGQVKC DENGQVKCDE
NGQVKCDENG QVKCDENGQV KCDENGQVKC DENGQVKCDE NGQVKCDENG QVKCDKNKGE
IKSFQYNEVK VDERYERNKE EIIYDHEHKK EGIFNIHKND DLIKENIKEK ENFSCSIQGN
DNAIPILKKT DINIKSIAAN KIEASYPSVY CNIYCVNDKK SNELEMSLNK LKLNDSSFSF
KKYICETLGK GFKCGFNGLL HLNIIQERIK REYNIDTIVT APSVNYLIRV KEKYMDKRLK
EKLLEKNFDI QNMHIEQMDK TSSDDCFFFM TSNVNDIPTK NVVHSIYEPY VKTNIITPEI
YQKYIMNECF KRRGIFIKKE IMNDQIIFLF EMPLSEILIN FLDQIKSSTK GYGSMSYENI
IIYKPSELYK IHIYINKKKI DSLSFLAHKR NYEDKSRKLV SKLKTLINPH QFLIIIQAAL
ESKIFVSEKI KPLKKNVTAK CYGGDITRRR KLIEKQNEGK KKMFEIGKVK LPPNIFTKLF
DIKSE
