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EFTUB_NICSY
ID   EFTUB_NICSY             Reviewed;         485 AA.
AC   Q43364; Q7DNA4;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Elongation factor TuB, chloroplastic;
DE            Short=EF-TuB;
DE   Flags: Precursor;
GN   Name=TUFB;
OS   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8087886; DOI=10.1007/bf00309543;
RA   Sugita M., Murayama Y., Sugiura M.;
RT   "Structure and differential expression of two distinct genes encoding the
RT   chloroplast elongation factor Tu in tobacco.";
RL   Curr. Genet. 25:164-168(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 61-485.
RC   TISSUE=Leaf;
RX   PubMed=8358028; DOI=10.1007/bf00027363;
RA   Murayama Y., Matsubayashi T., Sugita M., Sugiura M.;
RT   "Purification of chloroplast elongation factor Tu and cDNA analysis in
RT   tobacco: the existence of two chloroplast elongation factor Tu species.";
RL   Plant Mol. Biol. 22:767-774(1993).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D11470; BAA02028.1; -; Genomic_DNA.
DR   EMBL; D11376; BAA01975.1; -; mRNA.
DR   PIR; S36184; S36184.
DR   RefSeq; XP_009772722.1; XM_009774420.1.
DR   AlphaFoldDB; Q43364; -.
DR   SMR; Q43364; -.
DR   STRING; 4096.XP_009772722.1; -.
DR   PRIDE; Q43364; -.
DR   GeneID; 104223071; -.
DR   KEGG; nsy:104223071; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   Proteomes; UP000189701; Unplaced.
DR   GO; GO:0009507; C:chloroplast; 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:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
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   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 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   Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..76
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           77..485
FT                   /note="Elongation factor TuB, chloroplastic"
FT                   /id="PRO_0000007456"
FT   DOMAIN          86..290
FT                   /note="tr-type G"
FT   REGION          95..102
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          136..140
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          157..160
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          212..215
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          250..252
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         95..102
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..161
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         212..215
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  52688 MW;  FE88EF5D48B92D29 CRC64;
     MASISAASAT ATASTKLAYP YSPSSSSSSS NTAAVFPSNS SKLILSSSFT PTPSTLFLHS
     PTTTPSTTHP RRFTVRAARG KFERKKPHVN IGTIGHVDHG KTTLTAALTM ALASMGNSAP
     KKYDEIDAAP EERARGITIN TATVEYETEN RHYAHVDCPG HADYVKNMIT GAAQMDGAIL
     VVSGADGPMP QTKEHILLAK QVGVPNMVVF LNKQDQVDDE ELLELVELEV RELLSSYEFP
     GDEIPIISGS ALLALEALMA NPSIKRGENQ WVDKIYQLMD NVDEYIPIPQ RQTELPFLMA
     IEDVFSITGR GTVATGRVER GTVKVGEIVD IVGLKDTRNT TVTGVEMFQK ILDEAMAGDN
     VGLLLRGIQK IDIQRGMVLA KPGTITPHTK FEALVYVLKK EEGGRHSPFF AGYRPQFYMR
     TTDVTGKVTV IMSDKGEESK MVMPGDRVNM VVELIMPVAC EQGMRFAIRE GGKTVGAGVI
     QKILE
 
 
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