IF2_DECAR
ID IF2_DECAR Reviewed; 904 AA.
AC Q47D94;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Daro_2452;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ47187.1; -; Genomic_DNA.
DR RefSeq; WP_011288186.1; NC_007298.1.
DR AlphaFoldDB; Q47D94; -.
DR SMR; Q47D94; -.
DR STRING; 159087.Daro_2452; -.
DR EnsemblBacteria; AAZ47187; AAZ47187; Daro_2452.
DR KEGG; dar:Daro_2452; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
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; IPR009061; DNA-bd_dom_put_sf.
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; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 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..904
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228188"
FT DOMAIN 404..571
FT /note="tr-type G"
FT REGION 239..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..420
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 438..442
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 459..462
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 513..516
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 549..551
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 250..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413..420
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 459..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 513..516
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 904 AA; 98103 MW; 57FECE8A98F213F7 CRC64;
MSATTVSQFA VELKMPVVAL LEQLGKAGVG KSDANDMLND QDKTRLLDYL RRAHGDESQT
KITLTRKQTS EIKATDSHGR ARTVQVEVRK KRVLVKRDIG EHAPEVELEA SNALQEEVSA
PEVIPEPVVE VVPEPVIEVV PEPVVEIVPE PVVEAPVEVP VEEVVLEKAA PVAPTRASII
GEKELQARAE ESRRYNQLRE IQERELREKQ AREAQLVQMR QQAELAAAAA KAAELAKNQA
ATQAKTSEGA EKGTLHKKPE TPGKKGDKGG RAADDGKKKG GIKTRGSDGA GGWKDNRHGH
KKSHKVDDGQ GSFQAPTEPV VREVHIPETI SVSDLAHKMA IKATEIIKVM MKMGSMVTIN
QVLDQETAMI VVEEMGHQAL AAKLDDPDAF LEEHAEHKDV PLEHRAPVVT VMGHVDHGKT
SLLDYIRRAK VASGEAGGIT QHIGAYHVET DRGMVTFLDT PGHEAFTAMR ARGAKATDIV
ILVVAADDGV MPQTKEAIHH AKAAGVPLVV AVNKIDKPDA NPERVKQELV AEGVIPEEYG
GDSPFVPVSA KKGTGIDELL EQVLLQAEIL ELTAQKDAPA KGLIIEARLD KGRGAVATML
VQSGTLKRGD IVLAGQVFGR VRAMLDENGK PINEAGPSIP VEILGLSDVP AAGEEAIVLG
DEKKAREIAL FRQGKFRDVK LAKQQAAKLE NMFQQMEEGE VKTLPLIVKA DVQGSQEALV
QTLSKLSNEE VRVQIIHGAV GAISESDVNL AQASGAVIIG FNIRADAGSR KLAESFGVDI
RYYNVIYDAV DEVKAALSGM LSPEKREQIT GMVEIRQVFL VSKVGAIAGC YVLEGFVKRN
SRVRLLRNNV VQWDGELDSL KRFKDDVKEV RSNFECGLSL RGNNDIQVGD QLEVYEIQEV
ARSL
