ID   IF2P_THEON              Reviewed;         597 AA.
AC   B6YWH3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=TON_0948;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
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; CP000855; ACJ16436.1; -; Genomic_DNA.
DR   RefSeq; WP_012571908.1; NC_011529.1.
DR   AlphaFoldDB; B6YWH3; -.
DR   SMR; B6YWH3; -.
DR   STRING; 523850.TON_0948; -.
DR   EnsemblBacteria; ACJ16436; ACJ16436; TON_0948.
DR   GeneID; 7017251; -.
DR   KEGG; ton:TON_0948; -.
DR   PATRIC; fig|523850.10.peg.956; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
DR   Proteomes; UP000002727; 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..597
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_1000093837"
FT   DOMAIN          4..221
FT                   /note="tr-type G"
FT   REGION          13..20
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          38..42
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          77..80
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          131..134
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          199..201
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         77..81
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         131..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   597 AA;  66124 MW;  26663C247FFBAECE CRC64;
     MKRIRQPIIA VLGHVDHGKT TLLDRIRRTN VAGKEAGGIT QHIGATEVPI ETVKNLAGPL
     IKLWKGEIKL PGLLFIDTPG HEAFTSLRAR GGSLADLAVL VVDINEGFQP QTIESIEILR
     KNRTPFIVAA NKIDRIKGWK IEKDEPFLVN IKKQDQRAQQ ELETKLWELI GKFYEMGFQA
     NRFDRVQNFT RELAIVPISA KYGIGVPELL VLIAGLSQKY LEEKLKIEVE GPARGTILEV
     REEIGLGTTI DVIIYDGTLH KDDTIVVGGK DKAIVTKIRA LLKPKPLDEI RDPRFRFDQV
     DEVTAAAGVK IAAPGLEEAL AGSPVIAARS EEEVEKAKQE ILSQIQSVVI STGKVGVIVK
     ADTLGSLEAL SKELQEKNIP IRKADVGNIS KTDVMEALSV KDEDPKYGVV LGFNVKVNED
     AEEVAKARGV PIFTGNIIYK LIEDYEAWVK GEEEKKKREL LSKVTFPGVI RLYPDERYVF
     RRSHPAIVGI EVVEGRIRPG VTLIKQNGQK VGVIKSIKNR NDFVQEAKKG EAVAIAIEGA
     IVGRHIHPGE TLYVDLSKND VIILAKQLKN ELDETDIKAL KMTAKVKAQQ DPFWKAV