IF2P_META3
ID IF2P_META3 Reviewed; 598 AA.
AC A6UVG0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Maeo_0901;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
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; CP000743; ABR56482.1; -; Genomic_DNA.
DR RefSeq; WP_011973614.1; NC_009635.1.
DR AlphaFoldDB; A6UVG0; -.
DR SMR; A6UVG0; -.
DR STRING; 419665.Maeo_0901; -.
DR PRIDE; A6UVG0; -.
DR EnsemblBacteria; ABR56482; ABR56482; Maeo_0901.
DR GeneID; 5327717; -.
DR KEGG; mae:Maeo_0901; -.
DR eggNOG; arCOG01560; Archaea.
DR HOGENOM; CLU_002656_3_3_2; -.
DR OMA; FRQSKPA; -.
DR OrthoDB; 17053at2157; -.
DR Proteomes; UP000001106; 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;
KW Reference proteome.
FT CHAIN 1..598
FT /note="Probable translation initiation factor IF-2"
FT /id="PRO_1000008270"
FT DOMAIN 3..223
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; 66116 MW; 9627CE748D20CE19 CRC64;
MALRCPIVSV LGHVDHGKTS LLDKIRKTRV TQREAGGITQ HIGASEIPID IIKKISKDLI
KMLGANLTIP GILVIDTPGH AAFTSLRKRG GALADIAVLI VDINEGFMPQ TIEALNILKQ
NKTPFVVAAN KIDRLPGWSS VDGAFITNFN EQKQHPNALT EFEIKLYENV IAPLAERGFE
ADLFSRVKDV SKTINIVPIS AMTGEGIPDL LVMISGLAQR FMEQNLKLNV EGYAKGTVLE
VKEERGLGKT MDAIIYDGVA KRGDYIVIGN PDGIVVSRIK ALLKPKALDE MRDPRDKFKT
MNEISAATGL KISAPDLDNI IAGSPLRIVP KNMVEQAKAE IVEEIEETAI QLDEEGIIIK
ADTLGSLEAL ATELRKVGAK IKKAEVGDVS KKDVIEASSY AQTNPLNGAI ILFNSKLLAD
AKSEVEKYEI KTFEGDIIYK LVEDYEEWTK EMKELLKSDE FNRLTKPAIL RIIPGCIFNK
TKPAICGVEV VYGTLRVGCS VVDEQGKRLG TVKEIKDKKQ ENIKEAKVGM EVPISIDGTV
ILGRHIGEDD IMYVELPEPE VRILSHNYMG ELRGDEREAF ERYVELKRKL ENNPFWGI