IF2P_METST
ID IF2P_METST Reviewed; 613 AA.
AC Q2NGM6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=Msp_0629;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57027.1; -; Genomic_DNA.
DR RefSeq; WP_011406227.1; NC_007681.1.
DR AlphaFoldDB; Q2NGM6; -.
DR SMR; Q2NGM6; -.
DR STRING; 339860.Msp_0629; -.
DR EnsemblBacteria; ABC57027; ABC57027; Msp_0629.
DR GeneID; 41325205; -.
DR KEGG; mst:Msp_0629; -.
DR eggNOG; arCOG01560; Archaea.
DR HOGENOM; CLU_002656_3_3_2; -.
DR OMA; FRQSKPA; -.
DR OrthoDB; 17053at2157; -.
DR Proteomes; UP000001931; 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;
KW Reference proteome.
FT CHAIN 1..613
FT /note="Probable translation initiation factor IF-2"
FT /id="PRO_0000335530"
FT DOMAIN 3..220
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 198..200
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 613 AA; 68340 MW; 2F8B2ECAC877B9F6 CRC64;
MKTRSPIVSV LGHVDHGKTT LLDHIRGSTI ASKEAGGITQ HIGATEIPMD VISSICGGFL
EKMNIQEQLP GLFFIDTPGH EAFTTLRKRG GSLADLAILI MDVTEGFKPQ TYEALNILKS
SKTPFVVAAN KIDKIPGWNS TKGECFSKAV QNQHKNVVFD LDQKIYEIVG TLHEEGFESE
RFDRVSNFAS QITIVPISAY TGEGLPELLT MLLGLAYQYL NEQLQIEEDA PASGTVLEVK
EEKGLGLTID TILYDGVLNK DDRIMMLTKE NKVISTKIRS LLKPKPLEEI RESKTMFEDT
NQIVAAAGVK IVAPHVDDVV SGSPLKVAND DNIRVEDELL SEVDNIRIQT NDIGILVKAD
TLGSLEALVN ILDSKDIPIK SAEIGDISRR DIINASIMYE EDEKYGVIIA FNVNILPSAE
DELNDQNIMV FQDRVIYQLT EDYLNWVNSA KERQKKAKLA SIIRPSKIRI MPKLVFRHSK
PAIAGVEIMS GIIEKGVTLI NDKGHVVGRV ESMEDNGENL PKVSRGSQVA MAIGDAVFEK
DFEEGDVLYV DMSERNFFAI NNELKDKLLD DEILTMEELQ EIKQETEDSN WGVINTDWSE
LDTLDEDEYE DFY