IF2_FRAAA
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