IF2_MYCVP
ID IF2_MYCVP Reviewed; 930 AA.
AC A1T7H8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mvan_2314;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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; CP000511; ABM13128.1; -; Genomic_DNA.
DR AlphaFoldDB; A1T7H8; -.
DR SMR; A1T7H8; -.
DR STRING; 350058.Mvan_2314; -.
DR EnsemblBacteria; ABM13128; ABM13128; Mvan_2314.
DR KEGG; mva:Mvan_2314; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_006301_9_2_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000009159; 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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..930
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008286"
FT DOMAIN 426..598
FT /note="tr-type G"
FT REGION 29..316
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 79..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..240
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; 96072 MW; 9303DEFDD94516FC CRC64;
MAGKARVHEL AKELGVTSKE VLARLSEQGE FVKSASSTVE APVARRLRES YGGSKSDKTK
AAPSGNGAAG ATVKPSAPQS RPGPKPGPPV AQQPAAPAAP PAAPPAPPTP AAAPPSPAPA
APAAATPAEP AAPSARPGPT PGPRPGPSAP KPGAPKPAAR TPRVGNNPFS SQQPVERPAP
RPQGPGGPRP GPGAGGPRPG GGPRPGASPG SMPPRPQGAR PGGGPRPGGG PRPGGGPRPT
PGGAGRPGGG GGGGGNYRGG GAGGGAPAAG GGGFRGRPGG GGGGGRPGQR GGAAGAFGRP
GGAPKRGRKS KRAKRAEYEN MQAPVVGGVR LPHGNGETIR LARGASLSDF AEKINANPAS
LVQALFNLGE MVTATQSVGD ETLELLGGEM NYVVQVVSPE DEDRELLESF DLTYGEDEGG
EEDLEIRPPV VTVMGHVDHG KTRLLDTIRN ATVREGEAGG ITQHIGAYQV TVDLDGTERP
ITFIDTPGHE AFTAMRARGA KATDIAILVV AADDGVMPQT VEAINHAQAA DVPIVVAVNK
IDKEGADPAK IRGQLTEYGL VPEEYGGDAM FVDISAKQGT NIEALLEAVI LTADASLDLR
ANPDMEAQGV AIEAHLDRGR GPVATVLIQR GTLRVGDSVV AGDAYGRVRR MVDEHGEDVE
EALPSRPVQV IGFTSVPGAG DNFLVVDEDR IARQIADRRS ARKRNALAAR TRKRISLEDL
DSALKETSQL NLILKGDNSG TVEALEEALL GIQVDDEVEL RVIDRGVGGV TETNVNLASA
SDAIIIGFNV RAEGKATELA NREGVEIRYY SIIYQAIDEI ESALKGMLKP VYEEKELGRA
EIRAIFRSSK VGNIAGCLVQ SGIMRRNAKA RLLRDNVVVA ENLTISSLKR EKDDVTEVRD
GYECGLTLTY SDIKEGDVIE TYELVEKART
