IF2_DESHY
ID IF2_DESHY Reviewed; 971 AA.
AC Q24UI6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, 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=DSY2517;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE84306.1; -; Genomic_DNA.
DR RefSeq; WP_011460393.1; NC_007907.1.
DR AlphaFoldDB; Q24UI6; -.
DR SMR; Q24UI6; -.
DR STRING; 138119.DSY2517; -.
DR EnsemblBacteria; BAE84306; BAE84306; DSY2517.
DR KEGG; dsy:DSY2517; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001946; 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; 2.
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..971
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335465"
FT DOMAIN 471..640
FT /note="tr-type G"
FT REGION 39..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..487
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 505..509
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 526..529
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 580..583
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 616..618
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 526..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 580..583
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 971 AA; 106888 MW; 902E5E1768725237 CRC64;
MSIRVHELAK ELNLSSKEVM SRLESIGVDV KNHLSAVEDQ DANRLRTRIQ KPQGKEQAVE
PRKSVPSQES KNLTQGPAEG NRDKSQGLQV ESSRVEGEGR PQGQRPMGDR PQGQRPMGDR
PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR
PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR
PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR PQGQRPMGDR
PQGQRPMGDR PQGQRPMGDR PQGQRPPQRP PATPGTPAVE QPPKRQIGEK KKPQDRNFER
KKEMEKEIRA PRGNRRNVKA APREIRDTAP KHIVIPESLT VQDLAAKMSR KSGEVIKKLM
DMGVMATINQ EIDSETAVII AGEMGVTVEV KIEKPITVIE EIEDDPAELR SRPPVVTVMG
HVDHGKTSLL DAIRTTKVTA SEAGGITQHI GAYQVEINGQ KITFLDTPGH EAFTAMRARG
AQVTDIAILV VAADDGVMPQ TVEAINHAKA ADVPIIVAIN KIDKEESNPD RVKQELTEYG
LVVEEWGGDT IAVPVSAKAR MNIEQLLEMV LLVAEIKELK ANPNRSATGT VIEAELDKGK
GPVATVLVSK GTLNVGDIIL AGSSFGRIRA MVDDKGRRVK KAGPSTPVEV QGLNEVPKAG
QVFNVVDDEK HARQIAEARA NERKAEEVRQ TTKVSLEDLF DRIKEGEVKE LNVIIKADVQ
GSIEALKQSL LRLSTSEVRV NPIHGGVGAI TETDIMLAAA SNAIIIGFNV RPDANTKATA
ELQGVDMRLY RVIYDAIEDV KAAMTGMLDP DFKEVVQGRA EVRQVFKVPK VGTVGGSYVL
NGKITRHSKI RVIRDGIVIH EGELESLRRF KDDAKEVVEG YECGIGVANF NDIKEGDIIE
AFIMEEVKRQ L
