ID   IF2P_METVS              Reviewed;         598 AA.
AC   A6URS1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Mevan_1296;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-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; CP000742; ABR55193.1; -; Genomic_DNA.
DR   RefSeq; WP_012066108.1; NC_009634.1.
DR   AlphaFoldDB; A6URS1; -.
DR   SMR; A6URS1; -.
DR   STRING; 406327.Mevan_1296; -.
DR   EnsemblBacteria; ABR55193; ABR55193; Mevan_1296.
DR   GeneID; 5324779; -.
DR   KEGG; mvn:Mevan_1296; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
DR   Proteomes; UP000001107; 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.
FT   CHAIN           1..598
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_1000008276"
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;  66229 MW;  754AA203CFBD2397 CRC64;
     MALRCPIVSV LGHVDHGKTS LLDKIRSTRV TQREAGGITQ HIGASEIPIN TIKKVSKDLL
     GLFNANLSIP GLLVIDTPGH EAFTSLRKRG GALADIAILV VDINEGFKPQ TIEAINILKQ
     CKTPFVVAAN KLDRIPGWSS SNGPFILNFN EKVQHPNAMT EFEIRLYENV IKHLNELGFD
     ADLFSRVKDT TRTINVVPVS AITGEGVPDL LIIIAGLAQK FLEQKLALNV EGYAKGTVLE
     VKEEKGLGRT IDAIIYDGIA RTGDYIVIGN PDGIVTSKVK ALLKPKELDE MRDPKDKFKP
     SREISAATGV KISAPELEMV VSGSPLRIVP KEHINKAMDE ITEEIEEFTI KTDEEGIIIK
     ADTMGSLEAI ANELRKAKAN IKKAEVGDVS KKDIIEASSY SSSDPLNGLI ISFNTKTLPD
     AKLELEKTDV KLLEGKIIYK LVEDYGAWLK EMEELLKSDE LNKLTKPAMI KILPNCIFRQ
     KGPAVCGVEI LYGTLKIGSH IMSDDGKKLG YVKEIRNNQQ ENIKEAKVGM QVPVSIDGNM
     ILGRNAKEND ILYVEVSEPE VRKLYHIYKD ELRGDEKEAL LRYMELKQKL EKSIFWGM