ID   IF2P_HALWD              Reviewed;         620 AA.
AC   Q18FT0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 3.
DT   03-AUG-2022, entry version 102.
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=HQ_3074A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53175.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q18FT0; -.
DR   SMR; Q18FT0; -.
DR   STRING; 362976.HQ_3074A; -.
DR   PRIDE; Q18FT0; -.
DR   EnsemblBacteria; CAJ53175; CAJ53175; HQ_3074A.
DR   KEGG; hwa:HQ_3074A; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   Proteomes; UP000001975; 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..620
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_0000335522"
FT   DOMAIN          33..248
FT                   /note="tr-type G"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          42..49
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          67..71
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          104..107
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          158..161
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          162..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..228
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        7..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42..49
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         104..108
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         158..161
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   620 AA;  66852 MW;  8BBF6152D8A3211A CRC64;
     MSDTDADADT DAVSTTETSM NADANANADG DTLRTPIVAV LGHVDHGKTT LLDTVRGSAV
     SEDEAGAITQ HIGATAVPLE TVSEMAGELV DPADFDLPGL LFIDTPGHHS FTTLRSRGGA
     LADIAVVVVD VNDGFQPQTI EALDILQRTG TPFVVAANKV DTTPGWTPTD GSPIQPTYES
     QPSAARDRLD ERLYELIGDL SDEGFSGDLY WRVQNFTKNV GVVPLSAITS EGVPDLLAVL
     MGLSQRYMRE QMAIDITGPG AGTILEVKDE RGFGATVDVV LYDGSVRPDD IIVVGGTDGP
     IVTDVRALLQ PRPNAEIRTE NRFDRVEIAQ AAAGVKIAAP DLDNAMAGAP LRVVRNRDRA
     NVVSEVEAEL ADIAVETAEE GVVVKADTLG SLEAMANALK EADVPILRAE VGDVAPRDIA
     IASTANEERN QTVLGFSVDV LSNASDELEE SNVRLFTDDV IYQLVDEYKS YVDEQERAQQ
     ETVLDKIVRP CRFRILEDHV FRQSSPAVVG VEVLSGTLKN NQYIIKWNGN EPARIGELSG
     IQEQGEDVSS ARAGTRVSIA IDGPTVGRQI EEGDELWVEL PEKHAKILEQ ELIDEIPADE
     LEALTSYLDS HRKRDPFWGK