ID   IF2P_CALMQ              Reviewed;         594 AA.
AC   A8MBV9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Cmaq_0457;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000852; ABW01302.1; -; Genomic_DNA.
DR   RefSeq; WP_012185522.1; NC_009954.1.
DR   AlphaFoldDB; A8MBV9; -.
DR   SMR; A8MBV9; -.
DR   STRING; 397948.Cmaq_0457; -.
DR   EnsemblBacteria; ABW01302; ABW01302; Cmaq_0457.
DR   GeneID; 5709932; -.
DR   KEGG; cma:Cmaq_0457; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
DR   Proteomes; UP000001137; 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..594
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_0000335521"
FT   DOMAIN          5..224
FT                   /note="tr-type G"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          39..43
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          80..83
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          134..137
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          202..204
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         80..84
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   594 AA;  66068 MW;  DCF51060FBF71582 CRC64;
     MSENYRAPIV VVVGHVDVGK TLLLDKIRNT MVAYREPGMI TQHIGLSYLP WPIIEKYAAP
     VIERYRLKGK VWVKGFLMVD TPGHAAFSNL RRRGGSVADL AILVIDLTRG FEEQTYESLI
     LLKSRNIPFV VAANKVDRIY GWKPIPNASI LDSYNAQDEE TQGRLEEALA NIIMDFNKQG
     FEAERFDRIT DFSRQVPIVP TSAVTGEGIP DLLVLMAGLT QRLVKDRLRL VGGPGKGVVM
     EVKEEKGLGT TMDVVLYDGV MRKGDTIVAM GLNGPVVTRI RMMVMPKPLD EMRDPEDKYM
     HINEVEAAAG VKVIADGLDD VVPGSSVYVV QGDPKPYIDE VVKDAASVKI ETDQIGVVAK
     ADTLGTLEAM VLYLRSQGIP VRKADIGPVT RRDIIDASVV RRKNPLYGVV LAFNVKVPKE
     VEEEAKVQLV TIFQNNILYR LVEEFTKWFN EEKSRLIESE LSKYVRPGKI AIIPGYVFRR
     SDPAIVGVEV LGGLIKPGYR LVKANGKEVG VIMQIQDKGK PIQVAKKGMS VAISIEGNVI
     VGRHIKEGDV LYVNVPLEHA VKLIMQYKDH LSSDEVEVLE EFMKLRSTWK AQAQ