ID   IF2_MYCA1               Reviewed;         914 AA.
AC   A0QIY2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MAV_3693;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000479; ABK66165.1; -; Genomic_DNA.
DR   RefSeq; WP_011725621.1; NC_008595.1.
DR   AlphaFoldDB; A0QIY2; -.
DR   SMR; A0QIY2; -.
DR   PRIDE; A0QIY2; -.
DR   EnsemblBacteria; ABK66165; ABK66165; MAV_3693.
DR   KEGG; mav:MAV_3693; -.
DR   HOGENOM; CLU_006301_9_2_11; -.
DR   OMA; QVRPEMI; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001574; 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   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..914
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008278"
FT   DOMAIN          421..581
FT                   /note="tr-type G"
FT   REGION          52..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..239
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         430..437
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         469..473
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         523..526
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   914 AA;  95466 MW;  2FD60908F5E5A89A CRC64;
     MAGKARVHEL AKELGVTSKE VLARLNEQGE FVKSASSTVE APVARRLRES FGGGKAAEGA
     AKAPAKAAAK GDAKTAAKGD VKAPDKALDA ALDNAIKAGG NGEAAAPPAQ PGGTATTPAA
     QATPEAPARP GPAAARPSAP APGQPKPPAP GQPPRPGATP GPRPGPAPKP AARTPRVGNN
     PFSSAQPVDR PIPRPVPRPG APRPGAPRPG ASPGNMPPRP GGVGGPGRPA RPGAPRPGGG
     RPGGPGGRDG GGGNYRGGGV GAPPGGGGGF RGRPGGGGGG RPGQRGGAAG AFGRPGGAPR
     RGRKSKRQKR QEYDSMQAPV VGGVRLPHGN GETIRLARGA SLSDFAEKID ANPASLVQAL
     FNLGEMVTAT QSVGDETLEL LGSEMNYNVQ VVSPEDEDRE LLESFDLTYG EDEGTEEDLQ
     TRPPVVTVMG HVDHGKTRLL DTIRKANVRE AEQVTVEHDG VERPITFIDT PGHEAFTAMR
     ARGAKATDIA ILVVAADDGV MPQTVEAINH AQAADVPIVV AVNKIDVEGA DPQKIRGQLT
     EYGLVPEEFG GDTMFVDISA KQGTNIDQLL EAVLLTADAA LDLRANPDME AQGVAIEAHL
     DRGRGPVATV LIQRGTLRVG DSIVAGDAYG RVRRMVDEHG DDVEEALPSR PVQVIGFTSV
     PGAGDNLLVV DEDRIARQIA DKRSARKRNA LAARSRKRIS LEDLDSALKE TSQLNLILKG
     DNAGTVEALE EALMGIQIDD EVALRVIDRG VGGITETNVN LASASDAVII GFNVRAEGKA
     TELANREGVE IRYYSVIYQA IDEIEKALRG MLKPIYEENQ LGRAEIRAIF RSSKVGIIAG
     CMITSGVVRR NAKARLLRDN VVVSENLTIN SLRREKDDVT EVREGFECGM TLGYSDIKEG
     DVIESYELVQ KERT