ID   IF2P_METMP              Reviewed;         598 AA.
AC   Q6M0I6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=MMP0284;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF29840.1; -; Genomic_DNA.
DR   RefSeq; WP_011170228.1; NC_005791.1.
DR   AlphaFoldDB; Q6M0I6; -.
DR   SMR; Q6M0I6; -.
DR   STRING; 267377.MMP0284; -.
DR   EnsemblBacteria; CAF29840; CAF29840; MMP0284.
DR   GeneID; 36101864; -.
DR   KEGG; mmp:MMP0284; -.
DR   PATRIC; fig|267377.15.peg.287; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
DR   BioCyc; MMAR267377:MMP_RS01530-MON; -.
DR   Proteomes; UP000000590; 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; 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; 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..598
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_0000137304"
FT   DOMAIN          3..225
FT                   /note="tr-type G"
FT   REGION          12..19
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          37..41
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          76..79
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          130..133
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          200..202
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   598 AA;  66154 MW;  E2C21FC4D105C32C CRC64;
     MALRCPIVSV LGHVDHGKTS LLDKIRRTRV TQREAGGITQ HIGASEIPIN TIKKVSKDLL
     GLFKADLSIP GILVIDTPGH EAFTSLRKRG GALADIAILV VDINEGFKPQ TIEAINILKQ
     CKTPFVVAAN KVDRIPGWNS SEGPFILNFN EKNQHPNAMT EFEIRLYENV IKHLNELGFD
     ADLFSRVKDT TKTINVVPVS AMTGEGVPDL LVIISGLAQR FLEQKLALNV EGYAKGTVLE
     LKEEKGLGKT IDAIIYDGIA KTGDFLVVGN PDGVLVSKIK ALLKPKELDE MRDPKDKFKP
     SKQISAATGV KISAPDLDSV IAGSPLRIVP KNQVEAAKEE VLEEVEEFTI LTDDEGIIIK
     ADTMGSLEAL ANELRKVNAK IKKAEVGDIS KKDVIEASSY ASTNPLNGLI ISFNTKVLAD
     AKAEIEKSDV KLLEGKIIYK LVEEHEEWTK EMEELMKSDE INRLTKPAMI KILPNCIFRQ
     KEPAVCGVEV LYGTLKIGSP IMSEDGKKLG YVKEMRDNQQ ENIKEAKVGM QVPVSIDGNI
     VLGRNAKEND ILYVEVPEPE ARKLHHEFKD ELRGDEKEAL SRYMELKQKI ENNIFWGM