IF2_THEYD
ID IF2_THEYD Reviewed; 752 AA.
AC B5YHT8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=THEYE_A1884;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001147; ACI21413.1; -; Genomic_DNA.
DR RefSeq; WP_012546130.1; NC_011296.1.
DR RefSeq; YP_002249674.1; NC_011296.1.
DR AlphaFoldDB; B5YHT8; -.
DR SMR; B5YHT8; -.
DR STRING; 289376.THEYE_A1884; -.
DR PRIDE; B5YHT8; -.
DR EnsemblBacteria; ACI21413; ACI21413; THEYE_A1884.
DR KEGG; tye:THEYE_A1884; -.
DR PATRIC; fig|289376.4.peg.1840; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR InParanoid; B5YHT8; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 173747at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..752
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093841"
FT DOMAIN 250..419
FT /note="tr-type G"
FT REGION 148..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..266
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 284..288
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 305..308
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 359..362
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 395..397
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 259..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 305..309
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 359..362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 752 AA; 83755 MW; 1398E5405496A051 CRC64;
MSTKAVRSIE LARELGVKPL EIVKFIEKIR NIQFKKGTTN IKVEPDEIDK IIQHFKKEAK
LEKIKEKEEK PVELKKTEEI KELEEKKPIT PKIIEEEIKE EEELQLPGRF RREISFEKIE
KIKPKPVPTK IPPKKFEPKK WLDIKEQKKV KDKNKKEEPA VTPSTAPRKK SIKIEEGTTV
KEFAELIGQK VPDVIKKFME LGYMPTINQP VDIDAAQLVA ESFGIKVEFS QTQELDIIEE
VEDSPELLQP RPPIVTVMGH VDHGKTSLLD AIRKTKVTEQ EAGGITQHIG AYKVTLQGKD
ITFLDTPGHE AFTALRARGA KVTDIVVLVV AADDGVMPQT IEAINHAKAA NVPIVVAVNK
IDKPEANPQR VRTQLSDYGV IPEEWGGQNI FVDISAKKRI GIENLLEMIA LQAEIMELKA
NPNKPARGTI IESRLDKGRG PVATVIVQNG TLRIGDAFVA GVTYGKVRAI IDDTGKRINE
APPSTPVEVV GFEEVPQAGD SFTVVEDERI ARQIANTRAQ KKRLAEMQKA QRLTLQDLYE
KIKEGEVKEL NLVIKGDVQG SVEALKKAVE DITHPEIKVK VIHTGVGGIT ESDVNLAATA
NAIIIGFNVR PETKAQDLAE QLGVDIKLYS IIYEVIDDVK KALQGMLEPE IKERVIGRAE
VRAVFKISKI GTVAGCYVLN GTISRASDGV RVIRDNIVVY EGKISSLKRF KEDVREVQAG
YECGITIENF NDIKEGDILE NYVLEKVPVK GL
