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IF2_HALOH
ID   IF2_HALOH               Reviewed;         686 AA.
AC   B8CW72;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Hore_07840;
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562;
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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; CP001098; ACL69541.1; -; Genomic_DNA.
DR   RefSeq; WP_012635729.1; NC_011899.1.
DR   AlphaFoldDB; B8CW72; -.
DR   SMR; B8CW72; -.
DR   STRING; 373903.Hore_07840; -.
DR   EnsemblBacteria; ACL69541; ACL69541; Hore_07840.
DR   KEGG; hor:Hore_07840; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000719; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   CDD; cd03702; IF2_mtIF2_II; 1.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
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; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF50447; SSF50447; 2.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00487; IF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..686
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000202776"
FT   DOMAIN          186..355
FT                   /note="tr-type G"
FT   REGION          35..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..202
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          220..224
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          241..244
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          295..298
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          331..333
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        45..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         195..202
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         241..245
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         295..298
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   686 AA;  75987 MW;  F1908A3C4637AAF5 CRC64;
     MSKIRVYKLA KELGKSSKEL VNILNDLGVE VSSHMSTVED ETAELVKGML QEEDKPEEKI
     SKKEPDKKDR KKTKGKKQMT RTATQKEGTE HGQKDTDRRE MRVTVNPPLS VKELAEKADI
     PVNRIIKTLI GLGVMATVNH QIDEEIVKKL IDKMNLKIKI SQGEDKEEKP DKVQTDIKDK
     PEDLELRPPI VTVMGHVDHG KTTLLDVIRE TRVAESEAGG ITQHIGAYQA VVQNKKITFI
     DTPGHEAFTA MRARGARLTD IAILVVAADD GVMPQTVEAI NHAKAADIPI IVAINKVDKS
     NAQPDMVKQQ LTEHGLVPED WGGDTICVPI SALKKKNIDE LLEMVLLVAE MEELKANPDR
     PAEGVIVESQ LDKGRGPVAT VLVKNGTLKV GDPILAGYTH GKVRAMINDQ GKRIKEALPS
     TPVEVLGFSD VPAAGDYVQV LEDEKEARAI AEERLQKKQE RDLQHDGRIS LDGLYQQIKE
     GGVKELNLII KGDVHGSIEA LRESLVKLST DEVTVNIIHT GVGAINETDV NLASASNAII
     IGFNVRPDSN ARKLAEREKV EIKTYRVIYK IIEDLKDAMA GMLEPELKEE VTGRAEVRAT
     FKVPNVGTVA GLYVKEGFIN RNNKVRLLRD GVVVYEGDIA SLKRFKNDVR EVKEGYECGL
     GIEGYNDIKE GDQIETYTYR EIKRTL
 
 
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