IF2P_METMJ
ID IF2P_METMJ Reviewed; 593 AA.
AC A3CSP4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Memar_0461;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN56394.1; -; Genomic_DNA.
DR RefSeq; WP_011843304.1; NC_009051.1.
DR AlphaFoldDB; A3CSP4; -.
DR SMR; A3CSP4; -.
DR STRING; 368407.Memar_0461; -.
DR PRIDE; A3CSP4; -.
DR EnsemblBacteria; ABN56394; ABN56394; Memar_0461.
DR GeneID; 4846305; -.
DR KEGG; mem:Memar_0461; -.
DR eggNOG; arCOG01560; Archaea.
DR HOGENOM; CLU_002656_3_3_2; -.
DR OMA; FRQSKPA; -.
DR OrthoDB; 17053at2157; -.
DR Proteomes; UP000002146; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..593
FT /note="Probable translation initiation factor IF-2"
FT /id="PRO_1000057658"
FT DOMAIN 7..221
FT /note="tr-type G"
FT REGION 16..23
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 41..45
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 77..80
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 131..134
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 199..201
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 77..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 593 AA; 65159 MW; 3E555D64DC1926B8 CRC64;
MAKESTIRTP IVCVMGHVDH GKTSLLDRIR GSSVVSTEEG EITQHIGATL VPIDAVTRMG
GALSKVSVNV PGLLFIDTPG HHAFTTLRAR GGALADMAIV VVDINEGFRP QTIEALQILR
NYKTPFVIAA NKVDRIHGWR VQENQPFLKT FAQQNERVQG MVETKVYELV GKLSDLGFNS
ERFDRVSDFA RNICIVPTSA LTGEGLPDIL MVLIGLAQRY MTESLKVSAD GPGAGTVLEV
KEERGLGMTL DLILYDGTLK VGDEIVVAGN DQIIETKVRS LLKPRPMSEI LIEERFERVK
SVTAAAGIKV AAPKLDGVIA GSPLRAVRSG NRDEVIEQVR REVQDIEVNL SDVGVIIRAD
TIGALEALSK ELEGHQIQVM RATVGPVTRH DVIEAGTIKD PLYSAIIAFN TPVLPDAVDA
LADTAMSHVS IFEGGVIYQL IDDYVEWRDE KKQELERQKF EKLIMPAKIR ILPNCVFRQS
NPAVVGVRIL GGKLQSGVDL ALPNGKKIGR IKQIQAKNET VQEAEAGKEV AISIEGPTVG
RQINVDDDLY VDIPERHVKV IEREVIDHLS PSLRETLEEF TTLKRREDPF WGK