GUFP_VITVI
ID GUFP_VITVI Reviewed; 680 AA.
AC A5B4D2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 ORFNames=VITISV_013255;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir;
RX PubMed=18094749; DOI=10.1371/journal.pone.0001326;
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "A high quality draft consensus sequence of the genome of a heterozygous
RT grapevine variety.";
RL PLoS ONE 2:E1326-E1326(2007).
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 {ECO:0000255|HAMAP-
CC Rule:MF_03138}.
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}.
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DR EMBL; AM446164; CAN60938.1; -; Genomic_DNA.
DR STRING; 29760.VIT_07s0031g03050.t01; -.
DR eggNOG; KOG0462; Eukaryota.
DR ExpressionAtlas; A5B4D2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; 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_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 3: Inferred from homology;
KW Chloroplast; GTP-binding; Hydrolase; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT CHAIN 52..680
FT /note="Translation factor GUF1 homolog, chloroplastic"
FT /id="PRO_0000402921"
FT DOMAIN 83..264
FT /note="tr-type G"
FT BINDING 92..99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT BINDING 157..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT BINDING 211..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
SQ SEQUENCE 680 AA; 75697 MW; 12F51D4B2EBBE44F CRC64;
MAAKINSLAA LVSLQASHHH HXSTPFYFSP FSPHLSTTLT SRRRSLRSAV VAQSTAGTQS
KAPSDVDLAA VSGQDRLLKV PISNIRNFCI IAHIDHGKST LADKLLQMTG TVQKREMKEQ
FLDNMDLERE RGITIKLQAA RMRYVFENEP YCLNLIDTPG HVDFSYEVSR SLAACEGALL
VVDASQGVEA QTLANVYLAL ENNLEIIPVL NKIDLPGAEP VRVSQEIEEV VGLDCSDAIH
CSAKEGIGIT EILNAIVKRI PPPCDTAERP LRALIFDSYY DPYRGVIVYF RVIDGTIKKG
DRIYFMASKK DYFADEIGVL SPNQLQADEL YAGEVGYLAA SIRSVADARV GDTITHYGRK
AENSLPGYEE ATPMVFCGLF PVDADKFPDL RDALEKLQLN DAALKFEPET SSAMGFGFRC
GFLGLLHMEI IQERLEREYN LTLITTAPSV VYRVNCINGD TVECSNPSLL PEPGKRTSIE
EPYVKIEMLT PKDYIGPLME LAQDRRGEFK EMKFITENRA SITYELPLAE MVGDFFDQLK
SRSKGYASME YSFLGYKESE LIKLDIQING ERVEPLATIV HKDKAYAVGR ALTQKLKELI
PRQMFKVPIQ ACIGAKVIAS ESLSAIRKDV LSKCYGGDIT RKKKLLKKQA EGKKRMKAIG
KVDVPQEAFM AVLKLEKEVL
