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 03-AUG-2022, entry version 115.
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; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
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 PRIDE; Q6YR66; -.
DR EnsemblBacteria; BAD04235; BAD04235; PAM_150.
DR KEGG; poy:PAM_150; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_14; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; OYEL262768:G1G26-182-MON; -.
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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
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
