ID   IF2_FRAAA               Reviewed;        1021 AA.
AC   Q0RDS4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, 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=FRAAL5760;
OS   Frankia alni (strain ACN14a).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CT573213; CAJ64392.1; -; Genomic_DNA.
DR   RefSeq; WP_011606833.1; NC_008278.1.
DR   AlphaFoldDB; Q0RDS4; -.
DR   SMR; Q0RDS4; -.
DR   STRING; 326424.FRAAL5760; -.
DR   KEGG; fal:FRAAL5760; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_9_4_11; -.
DR   OMA; QVRPEMI; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000657; 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; 1.
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..1021
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335471"
FT   DOMAIN          514..686
FT                   /note="tr-type G"
FT   REGION          50..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..530
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          548..552
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          573..576
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          627..630
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          663..665
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        70..128
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..212
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..279
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         523..530
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         573..577
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         627..630
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1021 AA;  103535 MW;  3AFE1B74AF2D099E CRC64;
     MAGKARVHEL AKELGVDSKT VLAKLKDLGE FVKSASSTVE APVVRKLKEA FPAEGGSASG
     GRPGGRPGPG NGARPAPPRP GLAPRPGPRP VPGRPGPAAR PGGPAAPSAP AAPSAPAPGA
     PAASPPASQP RPIAASAAAP PPAATSIPPV SSPAAASGPR PGPRPAGGPA APGRARPGAP
     VPPPGGSAPS APSAGGPRPG PRPGPRPSAP GNNPYTTPSA GPRQSAGQSG SGPASPPRPG
     APRPGPRPGG PRPGAPGAGG PRPSPGSMPP RPGSRPGGSG GMPPRPGGSG GPRPNANMFQ
     PRPAGGAPGR PGGGGAPGRP GGGGGGGGAR PGGFAGRGGA PGRPGGGGGG GGGAGAPGRP
     GGGGGGRPAA GGRGRGGTTA GAFGPGGRGR PGRQRKSKRA KRQEWESGLE APRMGAMVPR
     GNGQAIRLPR GASLADFADK IDANPGALVQ VVFTQLGEMV TATQSCTDET LQLLGVTLGY
     EVQIVSPEDE DKELLESFDL SFGGEYGDDV ELSIRPPVVT VMGHVDHGKT KLLDAIRFTD
     VVAGEAGGIT QHIGAYQVRA TVDGDERPIT FIDTPGHETF TAMRARGAQV TDIVVLVVAA
     DDGVKPQTIE ALNHAQAAGV PVVVAVNKVD KEGADPAKVR GQLTEYGLVA EEYGGDTMFV
     DVSARNKTNI DGLLEAIILT ADASLDLRAP TGTEAQGVAI EGRLDRGRGP VATVLVQRGT
     LRVGDSVVAG EAFGRVRAML DEHGGQVTEA GPARPVQVLG FTSVPDAGDN FLVVPEDRVA
     RQIAERRQAR ERNAELALSR GRPTLETILE RMKEGEKTQL NLILKGDVSG SVEALEDALL
     KIDVGDEVGL RIIDRGVGAI TETNVMLASA SDAVIIGFNV RPQGKATELA DREGVEVRYY
     SVIYQAIEDI ENALKGMLKP VYEEAQLGTA EVREVFRVPR IGNVAGSLVR SGIIRRNTKA
     RLIRDGVVVA DNLTVESLKR FKDDATEVRE GYECGIGLGS FNDIKIDDVI ETFEQREVPR
     V