ID   IF2P_METM6              Reviewed;         598 AA.
AC   A9A813;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Probable translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=MmarC6_0669;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
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}.
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DR   EMBL; CP000867; ABX01486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A813; -.
DR   SMR; A9A813; -.
DR   STRING; 444158.MmarC6_0669; -.
DR   KEGG; mmx:MmarC6_0669; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OrthoDB; 30957at2157; -.
DR   PhylomeDB; A9A813; -.
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; cd03703; aeIF5B_II; 1.
DR   CDD; cd16266; IF2_aeIF5B_IV; 1.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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   NCBIfam; TIGR00491; aIF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..598
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_1000093802"
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;  66289 MW;  A848923E8956D0D7 CRC64;
     MALRCPIVSV LGHVDHGKTS LLDKIRSTRV TQREAGGITQ HIGASEIPIN TIKKVSKDLL
     GLFKADLTIP GLLVIDTPGH EAFTSLRKRG GALADIAILV VDMNEGFKPQ TIEAINILKQ
     CKTPFIVAAN KLDRVPGWNS KEGPFILNFN EKNQHPNAMT EFEIRLYENV IKHLNELGFD
     ADLFSRVKDT TKTINVVPVS AMTGEGIPDL LVIISGLAQK FLEQKLALNV EGYAKGTVLE
     LKEEKGLGKT IDAIIYDGIA KTGDFLVVGN PQGVLVSKIK ALLKPKELDE MRDPKDKFKP
     SKQISAATGV KISAPDLDNV IAGSPLRIVP KDQIENAKAE VLQEVEEFTI LTDDEGIIIK
     ADTMGSLEAL ANELRKVKAK IKKAEVGDIS KKDVIEASSY ASTNPLNGLI ISFNTKVLSD
     AKAEIEKSDV KLLEGRIIYK LVEEYEEWVK EMEELMKSDE INRLTKPAMI KILPNCIFRQ
     KEPAVCGVEV LYGTLKIGSP LMSEDGKKLG YVKEIRDNQQ ENIKEAKVGM QVPVSIDGNI
     VLGRNAKEND ILYVEVPEPE ARKLHHEFRD ELRGDEKEAL SRYMELKQKI ENNIFWGM
//