IF2_FRASN
ID IF2_FRASN Reviewed; 1046 AA.
AC A8L6F4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=Franean1_1182;
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia;
OC unclassified Frankia.
OX NCBI_TaxID=298653;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EAN1pec;
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; CP000820; ABW10636.1; -; Genomic_DNA.
DR RefSeq; WP_020458812.1; NC_009921.1.
DR AlphaFoldDB; A8L6F4; -.
DR SMR; A8L6F4; -.
DR STRING; 298653.Franean1_1182; -.
DR EnsemblBacteria; ABW10636; ABW10636; Franean1_1182.
DR KEGG; fre:Franean1_1182; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
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 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..1046
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093786"
FT DOMAIN 539..711
FT /note="tr-type G"
FT REGION 49..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..555
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 573..577
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 598..601
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 652..655
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 688..690
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 68..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..210
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 548..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 598..602
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 652..655
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1046 AA; 106407 MW; 0FC5ED7759C025F4 CRC64;
MAGKARVHEL AKELGVDSKT VLAKLKDLGE FVKSASSTVE APVVRKLKEA FPAEGSAPSS
RPGGRPGNGA RPMPPPRPGP AIGRPGPGSG TGPRPGPGGR PVPGRPGPAP LPGASRPSTP
TAAPQSQPAQ TQPPQSQPVA PQPSQAPRPA AAAASAAAPA PAPSAPAPAP SAPAPAPITS
APTAATPPAA PQRPTPGGPR PGPAAPGRPR TGGPGGPGGP GGGPRPGPRP GPRPAAPGNN
PYTSPAAGPR AASGQGGSPS APPRPGAPRP GGPRPGGPRP GGPGGQRPSP GQMPPRPGGS
GGPRPTPGQM PPRPGGSGGP RPNSNMFQPR PAGGAPGRPG GGGGPGRPGG GGGGPRPGGG
GFAPRGGAPG RPGGGGGAPG RPGGGGPGGG GRPAAGGRGR GGTTAGAFGP GGRGRPGRQR
KSKRAKRQEW ESGLEAPRMG AMVPRGNGQA IRLPRGASLA DFADKIDANP GALVQVVFTQ
LGEMVTATQS CTDETLQLLG VTLGYEVQIV SPEDEDKELL ESFDLSFGGD YADDVELSAR
PPVVTVMGHV DHGKTKLLDA IRSTDVVGGE AGGITQHIGA YQVRAVVDGT ERPITFIDTP
GHETFTAMRA RGAQVTDIVV LVVAADDGVK PQTIEALNHA QAANVPIVVA VNKVDKEGAD
PAKVRGQLTE YGLVAEEYGG DTMFVDVSAR NRTGIDELTE AVILTADASL DLRAPTGTEA
QGVAIEGRLD RGRGPVATVL VQRGTLRIGD SVVAGEAFGR VRAMLDENGA QVSEAGPARP
VQVLGFTSVP DAGDNFLVVP EDRVARQIAE RRQARERNAE LALSRGRPTL ETILERMKEG
EKTQLNLILK GDVSGSVEAL EDALLKIDVG DEVGLRIIDR GVGAITETNV MLASASDAVI
IGFNVRPQGK ATELADREGV EVRYYSVIYQ AIEDIENALK GMLKPVYEEA QLGTAEVREV
FRVPRVGNVA GSLVRSGIIR RNTKARLIRD GVVVADNLTV ESLKRFKDDA TEVREGYECG
IGLGSFNDIK VDDVIETFEQ REVPRT
