ID   IF2P_METS3              Reviewed;         596 AA.
AC   A5UJM9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Msm_0202;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86407.1; -; Genomic_DNA.
DR   RefSeq; WP_011953751.1; NC_009515.1.
DR   AlphaFoldDB; A5UJM9; -.
DR   SMR; A5UJM9; -.
DR   STRING; 420247.Msm_0202; -.
DR   EnsemblBacteria; ABQ86407; ABQ86407; Msm_0202.
DR   GeneID; 5215790; -.
DR   KEGG; msi:Msm_0202; -.
DR   PATRIC; fig|420247.28.peg.206; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   Proteomes; UP000001992; 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..596
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_0000335526"
FT   DOMAIN          3..220
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          76..79
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          130..133
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          198..200
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         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   596 AA;  66426 MW;  0623E35109CEE41D CRC64;
     MKIRSPIVSV LGHVDHGKTT LLDYIRGSTI AAKEAGGITQ HIGATEIPND TIENICGDFI
     SKLAIKDLIP GLFFIDTPGH AAFTSLRKRG GALADLAVLI LDVNDGFKPQ TYEALNILKM
     YKTPFIVVAN KIDRLFGWEV HEGASFRETF SNQAKSVQQD LDNKIYEIVG ELHKEGFQSE
     RFDRVSNFAS QISIIPISAK TGEGVIEVLA MLLGLAQEYL TEQLEIDENA PAKGTVLEIK
     EETGLGVTLD AIIYDGVLRT NDEIALMLSS EDVLVTKIRS ILRPLPLEEM RDSKKKFRKL
     DEVVAAAGIK VAAPHLDDVV SGSPLRVLSE DTDVEQEILN EIDNITIDTE DEGILVKADT
     IGSLEAVVKL LREMDIPIRA ADIGDVNRRD IINSSIAYDE NELHGAIIAF NVDVHPNSEE
     DLNNSEVKLF SGDVIYQILE EYEEWVKQKQ EDKKKSFYDA IIKPAKFVSL PKLVFRQSKP
     AIIGIESLSG TLKQGQQLIN KDGHVVGSIA SMEDKGETLP DISRGQRVAM AIKDAIVGKD
     FEEGDELYVD IPEKHYKYIE REFKDKLTED EFETLYEFLE IKRKQDSDWG SFGLFE