IF2_MYCGI
ID IF2_MYCGI Reviewed; 930 AA.
AC A4TCF8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mflv_4039;
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-2007) 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; CP000656; ABP46509.1; -; Genomic_DNA.
DR AlphaFoldDB; A4TCF8; -.
DR SMR; A4TCF8; -.
DR STRING; 350054.Mflv_4039; -.
DR EnsemblBacteria; ABP46509; ABP46509; Mflv_4039.
DR KEGG; mgi:Mflv_4039; -.
DR eggNOG; COG0481; Bacteria.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_2_11; -.
DR OMA; QVRPEMI; -.
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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..930
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075609"
FT DOMAIN 426..598
FT /note="tr-type G"
FT REGION 31..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..442
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 460..464
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 485..488
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 539..542
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 575..577
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 75..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 435..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 485..489
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 539..542
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 930 AA; 95979 MW; 4115E33C68B6846C CRC64;
MAGKARVHEL AKELGVTSKE VLARLGEQGE FVKSASSTVE APVARRLRES FGGNKPDAVK
PAAGASNGAP AKPSAPGARP GPRPGPPAPA QPKEPPAPAA PAAAAPAPAA PAPPAAPPAP
AASAAPPSAP EAPSARPTPG PRPGPGGPKP GAPKPAPRTP RVGNNPFSSQ QPVERPAPRP
QGPAGPGGPR PGPGAGGPRP GGGPRPGATP GNMPPRPVGG PRPGGGPRPG GGPRPGAGPR
PTPGGAGRPG GGGGGNYRGG GAGGGGGAGG AAAGGFRGRP GGGGGRPGQR GGAAGAFGRP
GGAPKRGRKS KRAKRAEYEN MQAPVVGGVR LPHGNGETIR LARGASLSDF ADKINANPAS
LVQALFNLGE MVTATQSVND ETLELLGGEM NYVVQVVSPE DEDRELLQSF DLSYGEDEGG
EDDLEFRPPV VTVMGHVDHG KTRLLDTIRD ATVREGEAGG ITQHIGAYQV TVDLDGNERP
ITFIDTPGHE AFTAMRARGA KATDIAILVV AADDGVMPQT VEAVNHAQAA DVPIVVAVNK
IDKEGADPAK IRGQLTEYGL VPEEYGGDTM FVDISAKAGT NIEALLEAVV LTADASLDLR
ANPDMEAQGV AIEAHLDRGR GPVATVLIQR GTLRVGDSVV AGDAYGRVRR MVDEHGEDVE
EALPSRPVQV IGFTSVPGAG DNFLVVDEDR IARQIADRRS ARKRNALAAR TRKRISLEDL
DSALKETSQL NLILKGDNSG TVEALEEALL GIQVDDEVQL RVIDRGVGGV TETNVNLASA
SDAIIIGFNV RAEGKATELA NREGVEIRYY SIIYQAIDEI ESALKGMLKP IYEEKELGRA
EIRAIFRSSK VGNIAGCLVQ SGIMRRNAKA RLLRDNVVVA QNLTVSSLKR EKDDATEVRE
GYECGLTLTY NDIKEGDVIE TYELVEKART
