IF2_DEHM1
ID IF2_DEHM1 Reviewed; 593 AA.
AC Q3Z7U3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=DET0983;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
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; CP000027; AAW39798.1; -; Genomic_DNA.
DR RefSeq; WP_010936685.1; NC_002936.3.
DR AlphaFoldDB; Q3Z7U3; -.
DR SMR; Q3Z7U3; -.
DR STRING; 243164.DET0983; -.
DR PRIDE; Q3Z7U3; -.
DR EnsemblBacteria; AAW39798; AAW39798; DET0983.
DR KEGG; det:DET0983; -.
DR PATRIC; fig|243164.10.peg.932; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008289; 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..593
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228189"
FT DOMAIN 101..270
FT /note="tr-type G"
FT REGION 110..117
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 135..139
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 156..159
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 210..213
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 246..248
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 110..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 156..160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 210..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 593 AA; 64059 MW; 9FA5F2270F81955D CRC64;
MVEKTSKSSA KTEVAPPAKV IELGAAVSVK ELADSLDTNP VEVIKALMRK GIMANINQVI
EFEVAKGIVE AAGFEARLKV LKKSAAKKVS PAKEKLSNFP LRPPVVTIMG HVDHGKTRLL
DAIRSTNVME KEAGGITQHI GAYQVEIKGQ KITFLDTPGH EAFTAMRARG AQATDITILV
VAADDGVMPQ TLEALDHAKA AGVPIILAIN KMDKPEANPD RVKQQLAEAG LVVEEWGGDT
LAIPTSAREK KGINELLEAV LLIAELEDLR ADPNQPASGV VIEAEMDKNR GPMATVLVQS
GTLKLGDTVV AGTTWGRVKA MFNDVGKRIK KAEPSTPVAL LGMESVPQVG DKIIAVATEK
QARDMVNENS QVTRKTNAVS LTNVYDQVSK GNIKELNIIL KTDVQGSLEP IKDSLEKLST
DKIKININRS GVGNITESDV MLAMASGGLI IGFSTGIETN AQRLADAEDI DIRHYDIIYK
LVEDVEKAVQ GLLEPTIKEV IDGRAEVRAV FESTKKLSIA GCMVLEGKVL KNSQVRLLRG
GEVIVDAPSN SLRRFKDDVK EVVAGYECGV GLKDFNDFQK SDILEFYHKE KSR
