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Database: UniProt
Entry: IF2_ONYPE
LinkDB: IF2_ONYPE
Original site: IF2_ONYPE 
ID   IF2_ONYPE               Reviewed;         619 AA.
AC   Q6YR66;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PAM_150;
OS   Onion yellows phytoplasma (strain OY-M).
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX   NCBI_TaxID=262768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY-M;
RX   PubMed=14661021; DOI=10.1038/ng1277;
RA   Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA   Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT   "Reductive evolution suggested from the complete genome sequence of a
RT   plant-pathogenic phytoplasma.";
RL   Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04235.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6YR66; -.
DR   SMR; Q6YR66; -.
DR   STRING; 262768.PAM_150; -.
DR   KEGG; poy:PAM_150; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   BioCyc; OYEL262768:G1G26-182-MONOMER; -.
DR   Proteomes; UP000002523; 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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..619
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228220"
FT   DOMAIN          121..289
FT                   /note="tr-type G"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..137
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          155..159
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          176..179
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          230..233
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          266..268
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         176..180
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         230..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   619 AA;  68496 MW;  CBB0D7B1493ECA1B CRC64;
     MTLNKKTNNE NSSKTTPKLS KETDLRNDFA SKNYVFNPQD KVFQIAQVFG ITSAVLIKKL
     LQLGLKADVN QTLEKDIVEL LAKDYNIQVS EPQEKHTPPQ LQPQTPSLTK TKPNQKLNLQ
     KKSPIVTIMG HVDHGKTTLL DAIRKTRVVD QEFGGITQHI GAYQVEYQGN KITFIDTPGH
     EAFDKMRARG AKITDICILV VAVDDCVKPQ TLEALKHAQK AQIPIIVALN KIDKPNNNTQ
     QIMQELSSYD LLPEEWGGTT PYIAISALKR EGLEKILEII LLVSEIQNLQ ANPDQKAQGT
     VIEASLDKSL GLVATFIVSD GNLKVGDIVV AGASYGKIRS MEDENKKKLT KALPSQPVRV
     AGLKEVPQAG DIFYAVANEK QARQIVAEKK SQTKENLAKT LSPLNLEDIL QDLETEKPQE
     LNIILKADTQ GSLEALQGMI AKIKVSDLKV QLLRAAVGTI TETDIAFAKS SDSLLIGFNI
     KPASSTLKSA QRQEVKITIH NVIYRIIEDI EQKLKSMIKP TFEEVVTGKV EVRKIFNISK
     VGNIAGCYVT QGIVNNSDFA KVMRNDEVLF KGKIASLKHL KDNIKSAKQG YECGILLDGF
     NDFEINDIIE TSKLSKVEE
//
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