IF2_HAEDU
ID IF2_HAEDU Reviewed; 839 AA.
AC Q7VLI2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HD_1461;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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; AE017143; AAP96265.1; -; Genomic_DNA.
DR RefSeq; WP_010945310.1; NC_002940.2.
DR AlphaFoldDB; Q7VLI2; -.
DR SMR; Q7VLI2; -.
DR STRING; 233412.HD_1461; -.
DR EnsemblBacteria; AAP96265; AAP96265; HD_1461.
DR KEGG; hdu:HD_1461; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001022; 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.
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..839
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137206"
FT DOMAIN 338..508
FT /note="tr-type G"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..354
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 372..376
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 394..397
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 448..451
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 484..486
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 347..354
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 394..398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 448..451
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 839 AA; 91847 MW; BDFF37BB8B10461D CRC64;
MSDNEIKNET PKKLSLQRRT KTTIADGKVQ VEVRKSRKID TAVAKAEQAK LKAKQEAEAK
AQEKQAAEKA AQAQTEAKAQ TEQACTTKKT IQPPIIPGKQ KAMPKTEAKK ATPKTEKIVD
AEKEAKRKEE AELRRKQEEL ASPKAEMEAK RAAENARRLA EIAREETVEN GEEFEDNRFT
STYAREADRD HDRRSEGNRT RAKGGVAKAK KGGREDDKNE RNSDRRNAKD IKGKKSKGKK
GASLQQAFTK PVQAVKTDVV IGETITVAEL ANKMAIKATE IIKTMMKMGE MVTINQVIDQ
ETAQLVAEEL GHKVILRKEN ELEESVMEDR DIDAEKVTRA PVVTIMGHVD HGKTLLLDYI
RKAKVAAGEA GGITQHIGAY HVETEDGKMI TFLDTPGHAA FTSMRARGAK ATDIVVLVVA
ADDGVMPQTI EAIQHAKAAG APLVVAVNKI DKPEADPSRV EQELLQYEVV SEKFGGDVQF
VAVSAKKGMG IDELLEAIIL QSEVLELTAV KKGMASGVVI ESYLDKGRGP VATILVQSGT
LNKGDIVLCG FEYGRVRAMR DENGKDINSA GPSIPVEVLG LSGVPSAGDE ATVVRDEKKA
REVALYRQGK YREVKLARQQ KAKLENMFSN MTEGDIAELN VIVKADVQGS VEAICQALGE
LSTEEVKVKV VGSGVGGITE TDATLAAASN AIMVGFNVRA DASARRVIEN ENIDLRYYSI
IYELLNEIKA AMTGMLQPEF KQEIIGLAEV RNIFRHPKFG AIAGCMVTEG IIKRNNPIRV
LRDNVVIFEG ELDSLRRFKD DVAEVRNGME CGIGVKNYND VKVGDQIEVF EVVEIKRSI
