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EFGM_ORYSJ
ID   EFGM_ORYSJ              Reviewed;         757 AA.
AC   Q9FE64; Q10I39; Q94I51; Q94LE1;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE            Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE   AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE            Short=mEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE   AltName: Full=Elongation factor G1 {ECO:0000255|HAMAP-Rule:MF_03061};
GN   OrderedLocusNames=Os03g0565500, LOC_Os03g36780; ORFNames=OSJNBa0026A15.1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=11328648; DOI=10.3109/10425170009033990;
RA   Kato A., Fujita S., Komeda Y.;
RT   "Identification and characterization of the gene encoding the mitochondrial
RT   elongation factor G in rice.";
RL   DNA Seq. 11:395-404(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent
CC       ribosomal translocation step during translation elongation. During this
CC       step, the ribosome changes from the pre-translocational (PRE) to the
CC       post-translocational (POST) state as the newly formed A-site-bound
CC       peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC       sites, respectively. Catalyzes the coordinated movement of the two tRNA
CC       molecules, the mRNA and conformational changes in the ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_03061}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC       {ECO:0000255|HAMAP-Rule:MF_03061}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
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_03061}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK53868.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB040051; BAB13514.1; -; mRNA.
DR   EMBL; AB040052; BAB13515.1; -; Genomic_DNA.
DR   EMBL; AC016781; AAK53868.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC084404; AAK50578.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF97151.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12415.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS84953.1; -; Genomic_DNA.
DR   RefSeq; XP_015631992.1; XM_015776506.1.
DR   AlphaFoldDB; Q9FE64; -.
DR   SMR; Q9FE64; -.
DR   STRING; 4530.OS03T0565500-01; -.
DR   PaxDb; Q9FE64; -.
DR   PRIDE; Q9FE64; -.
DR   EnsemblPlants; Os03t0565500-01; Os03t0565500-01; Os03g0565500.
DR   GeneID; 4333268; -.
DR   Gramene; Os03t0565500-01; Os03t0565500-01; Os03g0565500.
DR   KEGG; osa:4333268; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_0_1; -.
DR   InParanoid; Q9FE64; -.
DR   OMA; FRVHRDE; -.
DR   OrthoDB; 637899at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; Q9FE64; OS.
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; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd04097; mtEFG1_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR045044; EFG1-like.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   PANTHER; PTHR43636; PTHR43636; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00484; EF-G; 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   Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..757
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000007447"
FT   DOMAIN          66..344
FT                   /note="tr-type G"
FT   BINDING         75..82
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         142..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         196..199
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CONFLICT        45
FT                   /note="S -> F (in Ref. 1; BAB13514/BAB13515)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156..158
FT                   /note="ALR -> RLG (in Ref. 1; BAB13514/BAB13515)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257..259
FT                   /note="ASD -> RIC (in Ref. 1; BAB13514/BAB13515)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347
FT                   /note="S -> T (in Ref. 1; BAB13514/BAB13515)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   757 AA;  83925 MW;  C3E7C7068ACD7B93 CRC64;
     MAMARRSASR LLSSFRPFSL LLQPLDDAPS LSAAAAAASA RRGMSSASAL RARDEKEVAR
     WRESMDRMRN IGISAHIDSG KTTLTERVLY YTGRIHEIHE VRGRDGVGAK MDSMDLEREK
     GITIQSAATY CTWNGYQVNI IDTPGHVDFT IEVERALRVL DGAILVLCSV GGVQSQSITV
     DRQMRRYEIP RVAFINKLDR MGADPWKVLN QARSKLRHHN AAVQVPIGLE EEFEGLVDLV
     ELKAYKFEGG SGQNVVASDV PSNMQDLVME KRRELIEVVS EVDDQLAEAF LNDEPIQANQ
     LKAAIRRATV ARKFIPVYMG SAFKNKGVQP LLDGVLDYLP CPMEVESYAL DQNKSEEKVL
     LAGTPAEPLV ALAFKLEEGR FGQLTYLRIY DGVIRKGDFI YNVNTGKKIK VPRLVRMHSN
     EMEDIQEAHA GQIVAVFGVD CASGDTFTDG SVKYTMTSMN VPEPVMSLAV SPISKDSGGQ
     FSKALNRFQK EDPTFRVGLD PESGETIISG MGELHLDIYV ERIRREYKVD AKVGKPRVNF
     RETITQRAEF DYLHKKQSGG QGQYGRVCGY IEPLPSESDG KFEFDNMIIG QAIPSNFIPA
     IEKGFKEACN SGSLIGHPVE NIRIVLTDGA SHAVDSSELA FKLASIYAFR QCYAAARPVI
     LEPVMKVELK VPTEFQGTVT GDMNKRKGII VGNDQEGDDT VVVCHVPLNN MFGYSTALRS
     MTQGKGEFSM EYLEHNTVSQ DVQMQLVNTY KASRGTE
 
 
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