IF2_RHOJR
ID IF2_RHOJR Reviewed; 980 AA.
AC Q0S219;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, 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};
GN OrderedLocusNames=RHA1_ro06644;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG98417.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0S219; -.
DR SMR; Q0S219; -.
DR STRING; 101510.RHA1_ro06644; -.
DR EnsemblBacteria; ABG98417; ABG98417; RHA1_ro06644.
DR KEGG; rha:RHA1_ro06644; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000008710; 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; 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; 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; Reference proteome.
FT CHAIN 1..980
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008320"
FT DOMAIN 476..647
FT /note="tr-type G"
FT REGION 28..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..492
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 510..514
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 535..538
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 589..592
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 625..627
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 77..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 535..539
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 589..592
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 980 AA; 100669 MW; 6574979D18A929D4 CRC64;
MAGKARVHEL AKELGVTSKE LLATLKEQGE FVKSASSTVE APVARRLRES FPSAKSADSA
ARPAAKPGAP APSTPATAAK PGGPRPGPKP AAPAPAPVAP AAAAPAATPE AQAPAPAAPA
ARAVTPAAPA TNAPKPGRPT PAAPAPAAPA PAAPAAPAAP AASAPAAPST GAKPGGPRPG
PKPPRVGNNP YSSAPAERPA PRPAPGAPRP GAPRPAPGQG GPRPAPGQGG PRPAPGQGGP
RPAPGQGGPR PAPGQGGPRP SPGSMPPRPN PGAMPARSAR PAPGGRPGRP GGAPGGRPGG
GGGGYRGGGA PGAGAGAPGG GAPAGGFRGR PGGGGRPGQR GAAAGAFGRP GGAPRRGRKS
KRQKRQEYDS MQAPAVGGVR LPRGNGETIR LARGASLSDF AEKIDANPAA LVQALFNLGE
MVTATQSVND ETLELLGGEM NYVVQVVSPE DEDRELLDSF DLTYGEDEGG EEDLESRPPV
VTVMGHVDHG KTRLLDTIRK ANVREGEAGG ITQHIGAYQV LTELDGNERL VTFIDTPGHE
AFTAMRARGA KATDLAILVV AADDGVMPQT VEAINHAQAA DVPIVVAVNK IDKEGANPDK
IRQQLTEYGL VAEEYGGDTM FVDISAKLGT NIDALLEAVL LTADAALDLR ANPDMDAQGV
AIEAHLDRGR GPVATVLIQR GTLRVGDSIV AGDAYGRVRR MVDEHGDDVL EALPSRPVQV
VGFTSVPGAG DNLLVVDEDR IARQIADRRN ARKRNALAAK SRKRISLEDL DSALKETSQL
NLILKGDNSG TVEALEEALH GIEIDDEVQL RVIDRGVGGV TETNVNLAAA SNAIIIGFNV
RAEGKATELA NREGVDIRYY SVIYQAIDEV EKALKGMLKP IYEEVELGKA EIRAMFRSSK
VGNIAGCLVT SGTIRRNAKA RLLRDNTVVA ETVTISSLKR EKEDVVEVRE GYECGLTVTY
SDIKVGDVIE AYELREKPRD
