IF2_DICNV
ID IF2_DICNV Reviewed; 879 AA.
AC A5EWY9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=DNO_0029;
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A;
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
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; CP000513; ABQ14161.1; -; Genomic_DNA.
DR RefSeq; WP_011927788.1; NC_009446.1.
DR AlphaFoldDB; A5EWY9; -.
DR SMR; A5EWY9; -.
DR STRING; 246195.DNO_0029; -.
DR PRIDE; A5EWY9; -.
DR EnsemblBacteria; ABQ14161; ABQ14161; DNO_0029.
DR KEGG; dno:DNO_0029; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 153277at2; -.
DR Proteomes; UP000000248; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..879
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335466"
FT DOMAIN 380..549
FT /note="tr-type G"
FT REGION 45..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..396
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 414..418
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 435..438
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 525..527
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 51..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 435..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 489..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 879 AA; 97946 MW; 91A3B5B6368B4A86 CRC64;
MTVAELAKQL RISINRLLDV ISEAGIVIHD VENDVLSPEQ KVAIAGHMKQ RKKQSATEKN
AAKSDNKSDK NSKTGAKKTT NRRKTDARKS QSSEKKISPR ELAQQLAEKK RLEQGNAQRE
NEEREYQEAL AAEEKRQQQE EARKAKREQK EAEAIRAEEE RLQMEAALQA QMQEQERIRQ
EKEAEEAKLN AEKELRKQQE REKRLAQEKA ELERKRQEAI RDVELRESYE EEAETRFHIQ
SKDRNFGSKN DRSGKRAVKN GDDERSGERR NNARNNTRRR NNDNKKGKFE KPVAPISREV
RIPETITVGD LAQKMSVKAS ELIKTMMKLG SMVTINQLLD QETAALIADE MGHRYVLLKE
NELEEQVMAQ ASENKMDVVV RAPVVTIMGH VDHGKTSLLD YIRHTRVVSG EAGGITQHIG
AYRVTTERGV ITFLDTPGHA AFTAMRARGA NVTDIVVLVV AADDGVMPQT KEAIQHAKAA
NVPLIVAVNK MDKPEADPER VKSELSQEGV ISEEWGGEHL FAYVSAKSGM GIDDLLEKIL
IQAEMLELTA PSSGVGKGVV VESRLDRGRG SVATVLVQSG VMKKGNVMLA GMEYGRIRAM
LDEKGKELEE AGPSTPVEIL GLSGTPNAGD DVIIVENERK AREIANFRQG KFKEIRIARQ
QKTKLENLFN NADGEISKVS LMIKADVQGS VEALADSLRE LSTDEVAVNI IATGIGGITE
SDVQLALASS ATIIAFNVRA EANAKKLIEE EGGDLRYYSI IYQAIDDVKA AMQGLLSPEI
REEIIGLAEV RDVFRSSKFG AVAGCIVEDG LLKRHNPIRV LRNNVVIYEG ELESLRRFKD
DVNEVRAGTE CGLGVKNYND VRVGDQIECY ERVEIERKL
