IF2_RHOE4
ID IF2_RHOE4 Reviewed; 981 AA.
AC C0ZYA5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RER_26320;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
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-2005) 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; AP008957; BAH33340.1; -; Genomic_DNA.
DR RefSeq; WP_020907439.1; NC_012490.1.
DR AlphaFoldDB; C0ZYA5; -.
DR SMR; C0ZYA5; -.
DR STRING; 234621.RER_26320; -.
DR PRIDE; C0ZYA5; -.
DR EnsemblBacteria; BAH33340; BAH33340; RER_26320.
DR KEGG; rer:RER_26320; -.
DR eggNOG; COG0481; Bacteria.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000002204; 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..981
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202783"
FT DOMAIN 477..649
FT /note="tr-type G"
FT REGION 31..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..493
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 511..515
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 536..539
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 590..593
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 626..628
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 82..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486..493
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 536..540
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 590..593
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 981 AA; 100446 MW; BA5ACAECE311901B CRC64;
MAGKARVHEL AKELGVTSKE LLATLKEQGE FVKSASSTVE APVARRLRES FPSAGGAETK
SETGAAAPAA RPAAKPGAPS PSAAKPGGPR PGPKPAAPAP AAPAAPAPAA PAAPAAAAPA
APSAPVPTPT FNAPKPAQPA RPAPAAPAAS APAAPAAPAA PSTGAKPGGP RPGPKAPRVG
NNPYSSAPAE RPAPRPAPGA PRPGAGQGGS RPAPGQGGPR PAPGQGGPRP APGQGGPRPA
PGQGGPRPPA GQGGPRPSPG SMPPRPNPGA MPARSARPAP GGGGRPGRPG GAPGGRPGGG
GGGYRGGGAP GAGAGAGAPG GAAPAGGFRG RPGGGGRPGQ RGAAAGAFGR PGGAVRRGRK
SKRAKRAEYE SMQAPAVGGV RLPRGNGETI RLARGASLSD FADKIDANPA ALVQALFNLG
EMVTATQSVN DETLELLGGE MNYVVQVVSP EDEDRELLDS FDLTYGEDAG GEEDLESRPP
VVTVMGHVDH GKTRLLDVIR KANVREGEAG GITQHIGAYQ VLTELEGNER LVTFIDTPGH
EAFTAMRARG AKATDLAILV VAADDGVMPQ TVEAINHAQA ADVPIVVAVN KIDKEGANPD
KIRQQLTEYG LVAEEYGGDT MFVDISAKQG LNIDALLEAV LLTADASLDL RANPDMDAQG
VAIEAHLDRG RGPVATVLIQ RGTLRVGDSI VAGDAYGRVR RMVDEHGQDV HEALPSRPVQ
VIGFTSVPGA GDNLLVVDED RIARQIADRR NARKRNALAA KSRKRISLDD LDAALKEHSQ
LNLILKGDNS GTVEALEEAL LGIPIDDEVQ LRVIDRGVGG ITETNVNLAA ASNAIIIGFN
VRAEGKATEL ANREGVDIRY YSVIYQAIDE VEKALKGLLK PVYEEVELGK AEIRAMFRSS
KIGNIAGCLV TSGSIRRNAK ARLIRDSKVI AETVTISSLK REKEDATEVR EGYECGLTVT
YSDIKIGDVL ECYELREKPR D