IF2_PARDP
ID IF2_PARDP Reviewed; 848 AA.
AC A1B587;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, 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=Pden_2594;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) 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; CP000489; ABL70681.1; -; Genomic_DNA.
DR RefSeq; WP_011748874.1; NC_008686.1.
DR AlphaFoldDB; A1B587; -.
DR SMR; A1B587; -.
DR STRING; 318586.Pden_2594; -.
DR PRIDE; A1B587; -.
DR EnsemblBacteria; ABL70681; ABL70681; Pden_2594.
DR KEGG; pde:Pden_2594; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000361; Chromosome 1.
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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 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..848
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008293"
FT DOMAIN 346..514
FT /note="tr-type G"
FT REGION 1..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..362
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 380..384
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 402..405
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 456..459
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 492..494
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 72..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355..362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 402..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 456..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 848 AA; 91294 MW; B7DB50802DADE02D CRC64;
MSDTDGKKPL GLGGGRSGHV KQSFSHGRTH NVVVETKRKR VVVPGKTGAA AGGGRSGSPS
AVSGDPSKRP AGISDAEMER RMAALRAAKA REVEEAAQRI ADEKAREEER ERRRLELEAK
EREEREREEA LRLKAEEDER RAREAELREK KKAEIAKPKT EARPATPADR AAAEAAAVRA
ETKGVSAAGP RKTDRDRDTR GGGGDDRDSR NKGRDDSRRT GKLSLSQALD GEGGRQRSLA
AMKRKQEKAR QKAMGGNQRA EKQVRDVQLP ETIVVSELAN RMAERTPDVI KSLMRMGMMV
TANQSIDADT AELVIDEFGH HAVRVSDADV EQVIDQVEDK PEDLQPRAPI ITIMGHVDHG
KTSLLDAIRH ANVVAGEAGG ITQHIGAYQV KASNGAVLTF LDTPGHAAFT SMRARGAQVT
DIVVLVVAAD DAVMPQTVEA INHAKAAKVP MIVAINKIDK PAANPQKVRT DLLLHEVVVE
AMSGEVQDVE VSAKTGQGLD TLLEAIALQA EILELKANPD RPAQGAVIEA QLDVGRGPVA
TVLVQNGTLK RGDIFVVGEQ WGKVRALIND KGERVDEAGP SVPVEVLGLN GTPEAGDVLN
VVSTEAQARE IADYRIQAAK DKRAAAGAAI TLDQMLAKAK ADENVAELPV VIKADVQGSA
EAIVQALEKI GNDEVRVRVL HYGVGAITES DIGLAEASQA PVIGFNVRAN APARNAANQK
GVEIRYYSII YDLVDDIKAA ASGLLSAEVR ENFIGYAEIK EVFRVSGVGN VAGCLVTEGV
ARRSAGVRLL RDNVVIHEGT LKTLKRFKDE VKEVQSGQEC GMAFENYDDI RKGDVIEIFE
REEVQRQL
