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IF2_THET2
ID   IF2_THET2               Reviewed;         571 AA.
AC   Q72KE8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=TT_C0347;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR   EMBL; AE017221; AAS80695.1; -; Genomic_DNA.
DR   RefSeq; WP_011172797.1; NC_005835.1.
DR   AlphaFoldDB; Q72KE8; -.
DR   SMR; Q72KE8; -.
DR   STRING; 262724.TT_C0347; -.
DR   PRIDE; Q72KE8; -.
DR   EnsemblBacteria; AAS80695; AAS80695; TT_C0347.
DR   GeneID; 3168456; -.
DR   KEGG; tth:TT_C0347; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43381; PTHR43381; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF50447; SSF50447; 2.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00487; IF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..571
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228255"
FT   DOMAIN          71..239
FT                   /note="tr-type G"
FT   REGION          80..87
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          105..109
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          126..129
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          180..183
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          216..218
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..87
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         126..130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         180..183
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   571 AA;  63178 MW;  7FA1269583DB969F CRC64;
     MAKVRIYQLA KELGMETQEL LELLDQMGVA YKSHASTLEE KDAEAVRELV KEQRGLQEKL
     AEEERRKSLP RRPPVVVIMG HVDHGKTTLL DYLRKSRIAE KEAGGITQHV GAFEVKTPQG
     TVVFIDTPGH EAFTTIRQRG AKVADIAVIV IAADDGIMPQ TEEAIAHAKA AGAKLIFAIN
     KIDLPQADPE KVKRQLMERG FVPEEYGGDA IVIPISAKTG QGVQDLLEMI LLLAELEDYR
     ADPNAEPRGV ILESKLDKQA GIIANMLVQE GTFRVGDYVV AGEAYGRIRA MMDADGNQRK
     EAGPGSAVQV LGFQELPHAG DVVEWVPDLE AAKEIAEERK EERKAREEEE KARRPRTMAE
     LLRAMQEEGR KELNLILRAD TQGSLEAIQH ILARESTEDV KINILLAQVG APTESDVLLA
     QTANAAILAF GVNPPGSVKK KAEEKGVLLK TFRIIYDLVD EVRNMVKGQR EPQYKEEVLG
     QAEVRAIFRL PTGKQVAGCM VTQGRIPRNA EVRVLRDGQV IWQGRIASLK RFKEDVREVA
     QGYECGIGLD GFDDFREGDV IEAFQMVEVP A
 
 
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