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EFTU_CYAPA
ID   EFTU_CYAPA              Reviewed;         409 AA.
AC   P17245;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Elongation factor Tu, cyanelle;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RX   PubMed=2129337; DOI=10.1007/bf00017831;
RA   Kraus M., Goetz M., Loeffelhardt W.;
RT   "The cyanelle str operon from Cyanophora paradoxa: sequence analysis and
RT   phylogenetic implications.";
RL   Plant Mol. Biol. 15:561-573(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-409.
RX   PubMed=1901820; DOI=10.1016/0378-1119(91)90170-g;
RA   Bryant D.A., Schluchter W.M., Stirewalt V.L.;
RT   "Ferredoxin and ribosomal protein S10 are encoded on the cyanelle genome of
RT   Cyanophora paradoxa.";
RL   Gene 98:169-175(1991).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, cyanelle.
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; X52497; CAA36740.1; -; Genomic_DNA.
DR   EMBL; U30821; AAA81238.1; -; Genomic_DNA.
DR   EMBL; M35206; AAA31701.1; -; Genomic_DNA.
DR   PIR; T06895; EFKTT.
DR   RefSeq; NP_043207.1; NC_001675.1.
DR   AlphaFoldDB; P17245; -.
DR   SMR; P17245; -.
DR   GeneID; 801571; -.
DR   GO; GO:0009842; C:cyanelle; 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   3: Inferred from homology;
KW   Cyanelle; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           1..409
FT                   /note="Elongation factor Tu, cyanelle"
FT                   /id="PRO_0000091455"
FT   DOMAIN          10..214
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        391
FT                   /note="A -> R (in Ref. 1; CAA36740)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  44538 MW;  5DCE5B37E0FE9759 CRC64;
     MARQKFDGNK PHVNIGTIGH VDHGKTTLTA AITTALASQG KGKARKYDEI DAAPEEKARG
     ITINTAHVEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLAKQVGVPN MVVFLNKEDQ IDDADLLELV ELEVRELLSK YDFPGDQIPF VSGSALLALE
     SLSSNPKLMR GEDKWVDKIL ALMDAVDEYI PTPERPIDKS FLMAIEDVFS ITGRGTVATG
     RIERGAIKVG ETVELVGLKD TKSTTVTGLE MFQKTLEEGM AGDNIGILLR GVQKTDIERG
     MVLAKPGSIT PHTQFESEVY VLTKDEGGRH TPFFSGYRPQ FYVRTTDVTG SIDAFTADDG
     SNAEMVMPGD RIKMTVSLVH PIAIEQGMRF AIREGGRTIG AGVVSKILK
 
 
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