IF2_RHOP5
ID IF2_RHOP5 Reviewed; 893 AA.
AC Q07V78;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RPE_0196;
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000463; ABJ04156.1; -; Genomic_DNA.
DR RefSeq; WP_011661650.1; NC_008435.1.
DR AlphaFoldDB; Q07V78; -.
DR SMR; Q07V78; -.
DR STRING; 316055.RPE_0196; -.
DR EnsemblBacteria; ABJ04156; ABJ04156; RPE_0196.
DR KEGG; rpe:RPE_0196; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
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.
FT CHAIN 1..893
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008315"
FT DOMAIN 389..560
FT /note="tr-type G"
FT REGION 1..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..405
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 423..427
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 446..449
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 500..503
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 536..538
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 8..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 446..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 500..503
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 893 AA; 95638 MW; D64DF6AA41DB2D94 CRC64;
MVDTKNPGDK TLSVSPSKTL TLKPRVEQGT VRQSFSHGRT KQVVVEKRGK RRIGGEGGPA
DAPTAAAAAP APAPAPVPSA APRPAAPPPP SRPQQSRSQS PSRSGSGVVL RTLTEDERSA
RATALADARV RDEEERRAAE AEVARRNSAE GIAQAEREAA EARRKAEEER HRHEEEAKRK
AELEAKRRFG EEEAKRPAAA ATPAKSATPA ARPTGAPAVR APGVAAEAGD DDEGPRQVRR
GPGGAARPVI PPKQPAAKPA PSKQRGRLTL VTALTADDVR ERSIASFRRR TQRLKGHASN
EPKEKLVREV IVPEAITIQE LANRMSERAV DVIRMLMKQG AMHKINDVID ADTAQLIAEE
LGHTVKRVAA SDVEEGLFDV VDNSTDTEPR SPVVTVMGHV DHGKTSLLDA LRHANVVSGE
AGGITQHIGA YQVTSPESGK KITFIDTPGH AAFTAMRARG AKVTDIVILV VAADDGVMPQ
TVEAINHAKA AGVPIIVAIN KIDKPDAKPE RVRTELLQYN VQVESLGGDT VDVEVSAKNK
TNLDKLLEMI ALQAELLDLK TNEQRPAEGT VIEAKLDRGR GPVATVLVQR GTLKVGDIIV
AGAEMGRVRA LISDQGDTVE SAGPSVPVEV LGFNGPPEAG DRLAVVENEA RARQVTSYRA
HQKREKAASL TGGMRGSLEQ MMSQLKTVGR KEFPLIIKAD VQGSLEAILG SLEKLGTEEV
AARILHAGVG GISESDVTLA EGFNAVILGF SVRANKEAAA AAKRNGIEIR YYNIIYDLVD
DIKKAMSGLL APTLRETMLG NALILEIFNI SKVGKVAGCR VTDGTVERGA NVRLIRDNVV
VHEGKLSTLK RFKDEVKEVQ SGQECGMAFE NYTDMRAGDV IECYRVETIQ RSL
