ID IF2_DEIRA Reviewed; 597 AA.
AC Q9RTG5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=DR_1799;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; AE000513; AAF11355.1; -; Genomic_DNA.
DR PIR; C75351; C75351.
DR RefSeq; NP_295522.1; NC_001263.1.
DR RefSeq; WP_010888434.1; NZ_JMLF01000007.1.
DR AlphaFoldDB; Q9RTG5; -.
DR SMR; Q9RTG5; -.
DR STRING; 243230.DR_1799; -.
DR PaxDb; 243230-DR_1799; -.
DR EnsemblBacteria; AAF11355; AAF11355; DR_1799.
DR GeneID; 69518039; -.
DR KEGG; dra:DR_1799; -.
DR PATRIC; fig|243230.17.peg.2012; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_2_0; -.
DR InParanoid; Q9RTG5; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 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_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
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; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..597
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137199"
FT DOMAIN 98..271
FT /note="tr-type G"
FT REGION 57..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..114
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 132..136
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 207..210
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 243..245
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 153..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 207..210
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 597 AA; 64024 MW; AEC1E13FE5B438D4 CRC64;
MSKVRIYTLA KDLGVDNHKM LEILDGLGVS YKSVSSTIDE ENVEIIKQIL ADEAAEGGDA
APAAASAPAA ATAEPEEADE TPAAAAQADA EPASDLPHRA PVVTIMGHVD HGKTSLLDYI
RKTRVAAKEA GGITQHVGAF EAKTSKGKIV FIDTPGHEAF TTIRARGANV ADIAIIVIAA
DDSLMPQTRE AIAHAQAAKV PMLIAINKVD LPQADPEKVK TDLTQLNLVP EEYGGDVIVV
PVSAKTGEGV EDLLEYISLT AELEDLRADP KGQFSGVIIE GRVDKQAGVL ATVMVQEGTL
HVGDFLVVGE NYGKIKAMTD SNGGRIKEAG PSTPVQILGF SEVPSSGETV VSAKNEHAAR
EIVAQRASDR RDEEDARERR KAQRSLADLL GPLGEVHTVN LILRADTQGS LEAIQGILAR
KETEDVKLNV MLAGIGAPTE GDVLLASTAE AQILCFNVTP SAAVTKVAET KEIPIKAYRI
IYEMIDEVDR LIKGNLDPVF EEQYLGRAEV RMVIHHPKSG NIAGSYVTDG MFKRNAKAKV
TRGKEVVYEG TVVGLKRFKD DVREVQQGYE CGINIDWNDV QEGDIIEASE MVEVEPR
//
