ID IF2P_METM7 Reviewed; 598 AA.
AC A6VIS4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, 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}; OrderedLocusNames=MmarC7_1287;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
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., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
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; CP000745; ABR66350.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VIS4; -.
DR SMR; A6VIS4; -.
DR STRING; 426368.MmarC7_1287; -.
DR KEGG; mmz:MmarC7_1287; -.
DR eggNOG; arCOG01560; Archaea.
DR HOGENOM; CLU_002656_3_3_2; -.
DR OrthoDB; 30957at2157; -.
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_1000008274"
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; 66259 MW; C1B4B90E14DD9AE8 CRC64;
MALRCPIVSV LGHVDHGKTS LLDKIRRTRV TQREAGGITQ HIGASEIPIN TIKKVSKDLL
GLFKADLSIP GILVIDTPGH EAFTSLRKRG GALADIAILV VDINEGFKPQ TIEAINILKQ
CKTPFVVAAN KVDRIPGWNS SEGPFILNFN EKNQHPNAMT EFEIRLYENV IKHLNELGFD
ADLFSRVKDT TKTINVVPVS AMTGEGIPDL LVIISGLAQK FLEQKLALNV EGYAKGTVLE
LKEEKGLGKT IDAIIYDGIA KTGDFLVVGN PDGVLVTKIK ALLKPKELDE MRDPKDKFKP
SKQISAATGV KISAPDLDNV IAGSPLRIVP KDQVDAAKEE VLQEVEEFTI LTDDEGIIIK
ADTMGSLEAL ANELRKVKAK IKKAEVGDIS KKEVIEASSY ASTNPLNGLI ISFNTKVLAD
AKVEIEKSDV KLLEGKIIYK LVEEYEDWIK EMEELLKSDE INRLTKPAMI KILPNCIFRQ
KEPAVCGVEV LYGTLKIGSP IMSEDGKKLG YVKEMRDNQQ ENIKEAKVGM QVPVSIDGNI
VLSRNAKEND ILYVEVPEPE ARKLHHEFKD ELRGDEKEAL SRYMELKQKI ENNIFWGM
//
