IF2_DEHMC
ID IF2_DEHMC Reviewed; 593 AA.
AC Q3ZXU3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=cbdbA947;
OS Dehalococcoides mccartyi (strain CBDB1).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=255470;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBDB1;
RX PubMed=16116419; DOI=10.1038/nbt1131;
RA Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT "Genome sequence of the chlorinated compound-respiring bacterium
RT Dehalococcoides species strain CBDB1.";
RL Nat. Biotechnol. 23:1269-1273(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; AJ965256; CAI83073.1; -; Genomic_DNA.
DR RefSeq; WP_011309424.1; NC_007356.1.
DR AlphaFoldDB; Q3ZXU3; -.
DR SMR; Q3ZXU3; -.
DR KEGG; deh:cbdbA947; -.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
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.
FT CHAIN 1..593
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228190"
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; 64080 MW; EC0325DC858036F8 CRC64;
MVEKTSKPSA KTEVAPPVKI IELGAAVSVK ELADSLETNP VEVIKALMRK GIMANINQVI
DFDIAKGVIE AAGFEAKLKI LKKSAAKKAS PAKEKLSNFP LRPPVVTIMG HVDHGKTRLL
DAIRSTNVME KEVGGITQHI GAYQVEIKGH KITFLDTPGH EAFTAMRARG AQATDITILV
VAADDGVMPQ TLEALDHAKA AGVPIILAIN KMDKPEANPD RVKQQLAEVG LVVEEWGGDT
LAIPTSAREN KGINELLEAV LLIAELEDLR ADPNQPASGV VIEAEMDKTK GPMATVLVQS
GTLKLGDTVV AGNTWGRVKA MFNDVGKRIK KAEPSTPVAL LGMESVPQVG DKIIAVATEK
QARDMVNENS QSTRKTNAVS LTNVYDQVSQ GNIKELNIIL KTDVQGSLEP IKDSLEKLST
DKIKININRS GAGNVTESDV MLAMASGGLI IGFSTGIETN AQRLADAEDI DIRHYDIIYK
LIEDVDKALQ GLLEPTIKEV IDGRAEVRAV FESTKKLSIA GCMVLEGKLV KNSQVRLLRG
GEVIVDAPSN SLRRFKEDVK EVVAGYECGV GLKDFNEFQK SDILEFYHKE KSR