GUFP_ARATH
ID GUFP_ARATH Reviewed; 681 AA.
AC Q9FNM5; Q8RWP3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Translation factor GUF1 homolog, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03138};
DE EC=3.6.5.-;
DE AltName: Full=Elongation factor 4 homolog {ECO:0000255|HAMAP-Rule:MF_03138};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_03138};
DE AltName: Full=GTPase GUF1 homolog {ECO:0000255|HAMAP-Rule:MF_03138};
DE AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03138};
DE Flags: Precursor;
GN OrderedLocusNames=At5g08650; ORFNames=T2K12.1;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: Promotes chloroplast protein synthesis. May act as a fidelity
CC factor of the translation reaction, by catalyzing a one-codon backward
CC translocation of tRNAs on improperly translocated ribosomes.
CC {ECO:0000255|HAMAP-Rule:MF_03138}.
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_03138};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03138}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10014.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB006697; BAB10014.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91334.1; -; Genomic_DNA.
DR EMBL; AY092958; AAM12957.1; -; mRNA.
DR EMBL; AY128719; AAM91119.1; -; mRNA.
DR RefSeq; NP_196482.2; NM_120952.6.
DR AlphaFoldDB; Q9FNM5; -.
DR SMR; Q9FNM5; -.
DR BioGRID; 16044; 5.
DR IntAct; Q9FNM5; 5.
DR STRING; 3702.AT5G08650.1; -.
DR iPTMnet; Q9FNM5; -.
DR PaxDb; Q9FNM5; -.
DR PRIDE; Q9FNM5; -.
DR ProteomicsDB; 247238; -.
DR EnsemblPlants; AT5G08650.1; AT5G08650.1; AT5G08650.
DR GeneID; 830766; -.
DR Gramene; AT5G08650.1; AT5G08650.1; AT5G08650.
DR KEGG; ath:AT5G08650; -.
DR Araport; AT5G08650; -.
DR TAIR; locus:2159572; AT5G08650.
DR eggNOG; KOG0462; Eukaryota.
DR HOGENOM; CLU_009995_3_3_1; -.
DR InParanoid; Q9FNM5; -.
DR OrthoDB; 165663at2759; -.
DR PhylomeDB; Q9FNM5; -.
DR PRO; PR:Q9FNM5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNM5; baseline and differential.
DR Genevisible; Q9FNM5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
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_03138; GUFP; 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; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027518; GUFP.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
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 1: Evidence at protein level;
KW Chloroplast; GTP-binding; Hydrolase; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138, ECO:0000305"
FT CHAIN 52..681
FT /note="Translation factor GUF1 homolog, chloroplastic"
FT /id="PRO_0000402913"
FT DOMAIN 84..265
FT /note="tr-type G"
FT BINDING 93..100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT BINDING 158..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT BINDING 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT CONFLICT 275
FT /note="L -> I (in Ref. 3; AAM12957/AAM91119)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="I -> T (in Ref. 3; AAM12957/AAM91119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 681 AA; 75437 MW; BC3E9D4DDB09B178 CRC64;
MAMASAMDLS SPPTFFLSGT STSSPSLRRL SSISVSGFRR HSNRKLQILC QATAGTEPQS
GLSVSGSKLA ARSGQDRLLK VPISNIRNFS IIAHIDHGKS TLADKLLQVT GTVQNRDMKE
QFLDNMDLER ERGITIKLQA ARMRYVYEDT PFCLNLIDTP GHVDFSYEVS RSLAACEGAL
LVVDASQGVE AQTLANVYLA LENNLEIIPV LNKIDLPGAE PEKVLREIEE VIGLDCSKAI
FCSAKEGIGI TEILDAIVQR IPAPLDTAGK PLRALIFDSY YDPYRGVIVY FRVIDGKVKK
GDRIFFMASG KDYFADEVGV LSPNQIQVDE LYAGEVGYIA ASVRSVADAR VGDTITHYSR
KAESSLPGYE EATPMVFCGL FPVDADQFPD LRDALEKLQL NDAALKFEPE TSSAMGFGFR
CGFLGLLHME IVQERLEREY NLNLITTAPS VVYRVNSVNG DTTLCSNPSR LPDPGQRKSV
EEPYVKIELL TPKDYIGALM ELAQERRGEF KEMKYIAENR ASILYELPLA EMVGDFFDQL
KSRTKGYASM EYSVIGYRES DLIKLDILIN AEMVEPLSTI VHRDKAYSVG RALTQKLKEL
IPRQMFKVPI QACIGSKVIA SEALSAIRKD VLAKCYGGDI SRKKKLLKKQ AAGKKRMKAI
GRVDVPQEAF MAVLKLEREV L
