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IF2_MYCCT
ID   IF2_MYCCT               Reviewed;         620 AA.
AC   Q2SSE6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MCAP_0333;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000123; ABC01401.1; -; Genomic_DNA.
DR   RefSeq; WP_011387218.1; NC_007633.1.
DR   AlphaFoldDB; Q2SSE6; -.
DR   SMR; Q2SSE6; -.
DR   EnsemblBacteria; ABC01401; ABC01401; MCAP_0333.
DR   GeneID; 23778711; -.
DR   KEGG; mcp:MCAP_0333; -.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   PhylomeDB; Q2SSE6; -.
DR   Proteomes; UP000001928; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..620
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008280"
FT   DOMAIN          119..288
FT                   /note="tr-type G"
FT   REGION          128..135
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          153..157
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          175..178
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          229..232
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          265..267
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         175..179
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         229..232
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   620 AA;  68659 MW;  9DEB5CBD7EE9275C CRC64;
     MKKPVKNIKK QKAQNQTKNI KKQLKEEVNT GLIDGIFVYT EPLSILEFAT KINKPVTVIL
     KHYFNQGLLL NQNTLLTEEQ MGELCLEFGF DFKKETSVTK ENILETLLDT VDDEKHLKER
     PPIVTIMGHV DHGKTTLLDS IKNSNVVASE AGGITQAIGA YQITTKNNKK ITFIDTPGHE
     AFTEMRSRGA NVTDIVVLIV AADDGVMPQT EEAIDHAKLA NVPIIVFINK IDKPGSDPNR
     VKTELMKYGL VAEEFGGDIP FIEGSAIKKI NLDKLEDTII LISELENLKA NPDRFASGVV
     LEAHLDKAKG PVASVLVQQG SLEIKDIMVV GTTFGSIKHI EDEFKHKVLK AEPSKPVVVY
     GLNQVPKAGD KFVVINDEKM AREISEAQLK KQQEEERRTK QAFTLDAIKQ HIDEGELKNI
     TLIIKADTQG SVEALKNSLS KINISGVKIN IIRASVGAIS LSDISLASTV RDGLVIVYGF
     NVRPDAIVRK KAEEDRIEIR LHNIIYKLIE ELEDAAKGIL DPEIKEVVLG QAQVRALFRH
     SAIGTIGGFY VVDGAITRNA KIRVIRNGVV VYDGEINSLQ HQKQDAKEVK AGFEGALTIK
     NFNDIKEGDI FEAYKLEQVK
 
 
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