GUF1_ARATH
ID GUF1_ARATH Reviewed; 663 AA.
AC Q9FLE4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 OrderedLocusNames=At5g39900; ORFNames=MYH19.60;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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; AB010077; BAB10215.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94489.1; -; Genomic_DNA.
DR EMBL; BT020385; AAV91331.1; -; mRNA.
DR EMBL; BT020455; AAW30033.1; -; mRNA.
DR RefSeq; NP_198806.2; NM_123353.4.
DR AlphaFoldDB; Q9FLE4; -.
DR SMR; Q9FLE4; -.
DR STRING; 3702.AT5G39900.1; -.
DR PaxDb; Q9FLE4; -.
DR PRIDE; Q9FLE4; -.
DR ProteomicsDB; 247264; -.
DR EnsemblPlants; AT5G39900.1; AT5G39900.1; AT5G39900.
DR GeneID; 833987; -.
DR Gramene; AT5G39900.1; AT5G39900.1; AT5G39900.
DR KEGG; ath:AT5G39900; -.
DR Araport; AT5G39900; -.
DR TAIR; locus:2178042; AT5G39900.
DR eggNOG; KOG0462; Eukaryota.
DR HOGENOM; CLU_009995_3_3_1; -.
DR InParanoid; Q9FLE4; -.
DR OMA; HADVFHQ; -.
DR OrthoDB; 165663at2759; -.
DR PhylomeDB; Q9FLE4; -.
DR PRO; PR:Q9FLE4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLE4; baseline and differential.
DR Genevisible; Q9FLE4; AT.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IBA:GO_Central.
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 HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031157; G_TR_CS.
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; TIGR01393; lepA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..663
FT /note="Translation factor GUF1 homolog, mitochondrial"
FT /id="PRO_0000402843"
FT DOMAIN 64..250
FT /note="tr-type G"
FT BINDING 73..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 143..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 197..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 663 AA; 73595 MW; 1E40147FA4A85D60 CRC64;
MGSMYRASKT LKSSRQALSI LFNSLNSNRQ NPTCIGLYQA YGFSSDSRQS SKEPTIDLTK
FPSEKIRNFS IIAHIDHGKS TLADRLMELT GTIKKGHGQP QYLDKLQVER ERGITVKAQT
ATMFYENKVE DQEASGYLLN LIDTPGHVDF SYEVSRSLSA CQGALLVVDA AQGVQAQTVA
NFYLAFEANL TIVPVINKID QPTADPERVK AQLKSMFDLD TEDVLLVSAK TGLGLEHVLP
AVIERIPPPP GISESPLRML LFDSFFNEYK GVICYVSVVD GMLSKGDKVS FAASGQSYEV
LDVGIMHPEL TSTGMLLTGQ VGYIVTGMRT TKEARIGDTI YRTKTTVEPL PGFKPVRHMV
FSGVYPADGS DFEALGHAME KLTCNDASVS VAKETSTALG MGFRCGFLGL LHMDVFHQRL
EQEYGTQVIS TIPTVPYTFE YSDGSKLQVQ NPAALPSNPK YRVTASWEPT VIATIILPSE
YVGAVINLCS DRRGQQLEYT FIDAQRVFLK YQLPLREIVV DFYDELKSIT SGYASFDYED
AEYQASDLVK LDILLNGQAV DALATIVHKQ KAYRVGKELV EKLKNYIERQ MFEVMIQAAI
GSKIIARDTI SAMRKNVLAK CYGGDITRKK KLLEKQKEGK KRMKRVGSVD IPHEAFQQIL
KVS
