IF2_RHOPA
ID IF2_RHOPA Reviewed; 883 AA.
AC Q6NCN5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RPA0436;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572594; CAE25880.1; -; Genomic_DNA.
DR RefSeq; WP_011156004.1; NC_005296.1.
DR AlphaFoldDB; Q6NCN5; -.
DR SMR; Q6NCN5; -.
DR STRING; 258594.RPA0436; -.
DR PRIDE; Q6NCN5; -.
DR EnsemblBacteria; CAE25880; CAE25880; RPA0436.
DR GeneID; 66891451; -.
DR KEGG; rpa:RPA0436; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q6NCN5; -.
DR BioCyc; RPAL258594:TX73_RS02260-MON; -.
DR Proteomes; UP000001426; Chromosome.
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; Reference proteome.
FT CHAIN 1..883
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228236"
FT DOMAIN 379..548
FT /note="tr-type G"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..395
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 413..417
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 436..439
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 490..493
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 526..528
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 388..395
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 436..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 490..493
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 883 AA; 95505 MW; DA994D360EC01B7A CRC64;
MVDTKTPGDK TLTMPTKTLT LKPRVEQGVV RQSFSHGRSK QVVVEKRGKR RLGGDEPAAP
AAPEVAKKPA PAPAAPPRQQ QSRPAPQQSR SGMVLRTLTE DERTARATAL ADARVREIEE
RKQAEIEAQR RAEQEKIEKA EREAAEARRK AEEERHRQED EAKRKAETEA KKRFGDAEPA
KKPAETSTTT TTAAPARPAT TTTRTPTPAG RPPAVAAEAG DDDEAPRMIR RPGGPARPAP
PPKQPAAKPG ASKQRGRLTV VTALNADDVR ERSIASFRRR TQRLKGHASN EPKEKLVREV
VIPEVIAIQE LANRMSERAV DVIRLLMKQG AMHKITDVID ADTAQLIAEE LGHTVKRVAA
SDVEEGLFDV VDDSTDTEPR SPVVTVMGHV DHGKTSLLDA LRHANVVSGE AGGITQHIGA
YQVTSPESGK KITFIDTPGH AAFTAMRARG AKVTDIVVLV VAADDGVMPQ TIEAINHAKA
AGVPIIVAIN KIDKPDAKPD RVRTDLLQHN VQVESMGGDV VDVEVSAKNK INLDKLLEMI
ALQAEILELK TNTQRPAEGT VIEAKLDRGR GPVATVLVQR GTLRVGDIIV AGAEMGRVRA
LISDQGETVQ EAGPSVPVEV LGFNGPPEAG DRLAVVENEA RARQITDYRA HQKREKSAAS
VSGMRGSLEQ MMTQLKTSGR KEFPLIVKAD VQGSLEAILG SLEKLGTDEV AARILHAGVG
GISESDVTLA EGFNAVILGF SVRANKEAAA AAKRNGIEIR YYNIIYDLVD DIKKAMSGLL
APTLRETMLG NAQILEIFNI SKVGKVAGCR VTDGTVERGA NVRLIRDNVV VHEGKLSTLK
RFKDEVKEVV AGQECGMAFE NYTDMRAGDI IECYRVETIQ RSL
