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IF2P_PYRNV
ID   IF2P_PYRNV              Reviewed;         589 AA.
AC   B1YCQ7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Probable translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Tneu_0631;
OS   Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS   V24Sta) (Thermoproteus neutrophilus).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=444157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Function in general translation initiation by promoting the
CC       binding of the formylmethionine-tRNA to ribosomes. Seems to function
CC       along with eIF-2. {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; CP001014; ACB39570.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1YCQ7; -.
DR   SMR; B1YCQ7; -.
DR   STRING; 444157.Tneu_0631; -.
DR   EnsemblBacteria; ACB39570; ACB39570; Tneu_0631.
DR   KEGG; tne:Tneu_0631; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   Proteomes; UP000001694; Chromosome.
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   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00100_A; IF_2_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR029459; EFTU-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR004544; TF_aIF-2_arc.
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; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF14578; GTP_EFTU_D4; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00491; aIF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..589
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_1000093836"
FT   DOMAIN          3..224
FT                   /note="tr-type G"
FT   REGION          12..19
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          37..41
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          78..81
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          132..135
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          200..202
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         78..82
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         132..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   589 AA;  64748 MW;  2127D6637CD70301 CRC64;
     MAVRSPFVVV MGHVDVGKTL LLDKIRGTSV AYREPGMITQ HIGMSFVPWQ AVEKYAGPLV
     DRLKLRGKIW IPGFLFIDTP GHAAFSNLRK RGGSVADLAI LVVDITSGLE DQGVESLKLI
     QSRGVPFVIA ANKLDRVYGW KSVENRPFLT AVEDQEWHAI ATLEESIGKL VEQLSKLGVE
     ADRYDRVRDF GRQVPIVPTS AVTGEGIADL LLVLAGVSQR FIPRDKLTVR PGPARGVVME
     VKEERGLGVV ADAILYDGVL KKGDTVVTAG IDGPRVAKVR MLVMPKPLEE MRDPEDRYMA
     VEEVKAAAGV RIVADGLEGV VAGAPLMAVR DPGEVQEAVK VVGEEISEIK IETDREGVIV
     RADTFGTLES TVLFLRQQGV PIRKADVGPP THKDVVEAVL SRRKNPAYGV ILAFNVKTPP
     EVEKEAMSSG VKIIRGEILY RIFDEYIKWS QEVKTKTVEQ ILSQMTRPGK IQILPGYVFR
     RSNPAIVGVK VLAGTIKPGV TLVKDGKEVG RVMQIQKSGK PVGEAAAGDE VAVSIQGDVM
     VGRQIKEGDV LYVYVPDEQA RQWLFQYKQY LREDELKALE EFLKAGRRR
 
 
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