ID IF2P_METB6 Reviewed; 591 AA.
AC A7IAP7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=Mboo_2294;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS56808.1; -; Genomic_DNA.
DR RefSeq; WP_012107868.1; NC_009712.1.
DR AlphaFoldDB; A7IAP7; -.
DR SMR; A7IAP7; -.
DR STRING; 456442.Mboo_2294; -.
DR GeneID; 5410885; -.
DR KEGG; mbn:Mboo_2294; -.
DR eggNOG; arCOG01560; Archaea.
DR HOGENOM; CLU_002656_3_3_2; -.
DR OrthoDB; 30957at2157; -.
DR Proteomes; UP000002408; 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 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;
KW Reference proteome.
FT CHAIN 1..591
FT /note="Probable translation initiation factor IF-2"
FT /id="PRO_0000335528"
FT DOMAIN 6..220
FT /note="tr-type G"
FT REGION 15..22
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 40..44
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 198..200
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 15..22
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 591 AA; 65151 MW; DCBB059FF8272DF5 CRC64;
MSDPKIRTPI VCVMGHVDHG KTSLLDRIRG SSVVASEAGA ITQHIGATIV PIEAIRKMSG
SMEKIPINIP GLLFIDTPGH HAFTTLRARG GALADMAILV VDISQGFQPQ TIEALQILRN
CKTPFVIAAT KVDRIHGWRI NKDESFLSSF GKQNERVKTD IETKTYEIVG KLSDLGFSAD
RYDRVSDFQR NLAIVPVSAH TGEGIADLLM IMIGLAQRYM GEELKLSAEG PGEGTVLEVK
EERGLGTTLD VILYNGTLSV GDEIAMASQD DVVTTKVRSL LKPRPMKEIL IEDRFERVKS
VVAASGIKVS APGLEKVIAG SPLFVTRGNM DELAARIRKE MQEIHVNLAE EGIVIKADTI
GALEALCKEL ESKEIKVMRA QVGPVSRHDL IDTETIKNPT FRVLLSFNTP ILPDAADMIK
DPLYTQVKVF SGQVIYQLID QYVAWRDEQK RIAEKAQFEH VMMPAKIRLL PDCVFRQSNP
AVVGVRVLGG KLRADVDLVK TDGKKIGHLK TMQLRQESIK EADAGLEVAI SIEGATVGRQ
LNVGDDLLVD LPERHVKVLE REMLKNLNIS TQEVLAEFVA IRRKAEPFWG K
//
