ID   IF2P_THESM              Reviewed;         597 AA.
AC   C6A1V3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=TSIB_0532;
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739;
RX   PubMed=19447963; DOI=10.1128/aem.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(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; CP001463; ACS89598.1; -; Genomic_DNA.
DR   RefSeq; WP_015848818.1; NC_012883.1.
DR   AlphaFoldDB; C6A1V3; -.
DR   SMR; C6A1V3; -.
DR   STRING; 604354.TSIB_0532; -.
DR   PRIDE; C6A1V3; -.
DR   EnsemblBacteria; ACS89598; ACS89598; TSIB_0532.
DR   GeneID; 8095520; -.
DR   KEGG; tsi:TSIB_0532; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
DR   Proteomes; UP000009079; 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;
KW   Reference proteome.
FT   CHAIN           1..597
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_1000202786"
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;  66657 MW;  DA6561DBF2D08163 CRC64;
     MKKIRQPIIA VLGHVDHGKT SLLDRIRNTH VAEKEAGGIT QHIGATEVPI DVVKQLAGPL
     LSLWKGEIKL PGLLFIDTPG HEAFTSLRAR GGSLADLAIL IIDVNEGFQP QTLESIEILR
     KYKTPFVVAA NKIDRIKGWK VVENEPFLVN IKKQDQRAQQ DLETKLWELI GKFYELGFQV
     NRFDRVKDFR KELAIIPISA KYGIGVPELL VLISGLAQKY LEEKLKIEVE GPARGTILEV
     REEIGFGTTI DVIIYDGTLR KDDTIVVGGK DKAIVTKIRA LLKPKPLDEI RDPRYKFDHV
     NEVSASAGIK IAAPDLEEAL AGSPVIAVRD EEELKRARRE ILEQIKSVII STDKVGVIVK
     ADTIGSLEAL SKELHEKNIP IRKADVGNIS KTDVMEALSV KEEEPFYGVV IGFNVKVNED
     AEEVAKAKNI PLFVNNIIYK LIEDYEAWIK AEEEKKKKEI LANTKFPGVI KLFPDERYVF
     RRSHPAIVGI EVLEGRIKPG YPLIKQNGDK VGVIKSIKSK EDFLQEAKKG DQVAVAIEGA
     IVGRHIHPGE ILYVDISKDD AIRLVKELRD MLDDTDIEAL KNTAKVKAQK DPFWGAL