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