IF2_RHOOB
ID IF2_RHOOB Reviewed; 974 AA.
AC C1B313;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ROP_66830;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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; AP011115; BAH54930.1; -; Genomic_DNA.
DR AlphaFoldDB; C1B313; -.
DR SMR; C1B313; -.
DR STRING; 632772.ROP_66830; -.
DR EnsemblBacteria; BAH54930; BAH54930; ROP_66830.
DR KEGG; rop:ROP_66830; -.
DR PATRIC; fig|632772.20.peg.6969; -.
DR HOGENOM; CLU_006301_9_4_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000002212; 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; 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; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..974
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118771"
FT DOMAIN 470..641
FT /note="tr-type G"
FT REGION 31..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..486
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 504..508
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 529..532
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 583..586
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 619..621
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 77..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479..486
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 529..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 583..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 974 AA; 100063 MW; 82E392A60C241398 CRC64;
MAGKARVHEL AKELGVTSKE LLATLKEQGE FVKSASSTVE APVARRLRES FPSAKSADSA
ARPAAKPGAP APSTPATSAK PGGPRPGPKP AAPAPAAPAA AAPAATPAAQ APAPAAPAAS
TATPAAPASN APKPGRPTPA APAPAAPAAP AAPAAASTPA APSTGAKPGG PRPGPKPPRV
GNNPYSSAPA ERPAPRPAPG APRPGAPRPA PGQGGPRPAP GQGGPRPAPG QGGPRPAPGQ
GGPRPAPGQG GPRPSPGSMP PRPNPGAMPA RSARPAPGGR PGRPGGAPGG RPGGGGGGYR
GGGAPGAGAG APGGGAPAGG FRGRPGGGGR PGQRGAAAGA FGRPGGAPRR GRKSKRQKRQ
EYDSMQAPAV GGVRLPRGNG ETIRLARGAS LSDFAEKIDA NPAALVQALF NLGEMVTATQ
SVNDETLELL GGEMNYVVQV VSPEDEDREL LDSFDLTYGE DEGGEEDLES RPPVVTVMGH
VDHGKTRLLD TIRKANVREG EAGGITQHIG AYQVLTELDG NERLVTFIDT PGHEAFTAMR
ARGAKATDLA ILVVAADDGV MPQTVEAINH AQAADVPIVV AVNKIDKEGA NPDKIRQQLT
EYGLVAEEYG GDTMFVDISA KQGTNIDALL EAVLLTADAA LDLRANPDMD AQGVAIEAHL
DRGRGPVATV LIQRGTLRVG DSIVAGDAYG RVRRMVDEHG DDVLEAMPSR PVQVVGFTSV
PGAGDNLLVV DEDRIARQIA DRRNARKRNA LAAKSRKRIS LEDLDSALKE TSQLNLILKG
DNSGTVEALE EALHGIEIDD EVQLRVIDRG VGGVTETNVN LAAASNAIII GFNVRAEGKA
TELANREGVD IRYYSVIYQA IDEVEKALKG MLKPIYEEVE LGKAEIRAMF RSSKVGNIAG
CLVTSGTIRR NAKARLLRDN TVVAETVTIS SLKREKEDAV EVREGYECGL TLTYSDIKVG
DVIEAYELRE KPRD
