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IF2P_METBU
ID   IF2P_METBU              Reviewed;         591 AA.
AC   Q12Z93;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Mbur_0223;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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; CP000300; ABE51233.1; -; Genomic_DNA.
DR   RefSeq; WP_011498395.1; NC_007955.1.
DR   AlphaFoldDB; Q12Z93; -.
DR   SMR; Q12Z93; -.
DR   STRING; 259564.Mbur_0223; -.
DR   PRIDE; Q12Z93; -.
DR   EnsemblBacteria; ABE51233; ABE51233; Mbur_0223.
DR   GeneID; 3997659; -.
DR   KEGG; mbu:Mbur_0223; -.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
DR   Proteomes; UP000001979; 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; 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; 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;
KW   Reference proteome.
FT   CHAIN           1..591
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_1000008271"
FT   DOMAIN          7..223
FT                   /note="tr-type G"
FT   REGION          16..23
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          41..45
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         16..23
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   591 AA;  64256 MW;  2CA81097FBEBD2E1 CRC64;
     MVVKDNLRTP IVCVMGHVDH GKTSLLDMIR GSAVVSGEAG AITQHIGATE VPISAIVEKC
     GNPGLLDKFM VPGLLFIDTP GHHAFTTLRS RGGALADLAV VIVDINEGFK PQTIESLNIL
     QQHKTPFVVV ANKIDKIHGW NPQKGAPFMT SYNKQSEHVR GSLDTKFYEV VGELYNHGFS
     SDRYDRVNDF QHNIGVIPIS AITGEGIPDL LMVLLGLAQR FLESNLHYNA EGPGVGTVLE
     VKEERGLGTT LDLILYDGVL KKGDTIVVGC LGEPIQTKVR AVLKPRALSE INVEDKFKQV
     SKVTAAVGVK ISAPHLDGAL SGGSVRVATA ETLDAVVEEV RNEIEDVQID TDQSGITIKA
     DTIGSLEALV NELKKEDIPI RKANVGDISN RDIMEAFAIE DPFHSVIVGF NVNILPDAKE
     KVRSTGVKVF MNDVIYRLID DYRDWVKEQR AISEKAVSET IVKPAMFTIM PDCVFRQSKP
     AVVGVRVIGG TIKTKVDVAT GDGTVVGIVK GLQSRGENVS VATIGMEVAM SIEGPTVGRQ
     INEGDILHAN IPERHVKILE QELYDSLSAD ELEALDSFLD IKRRDNPFWA K
 
 
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