IF2_DESVV
ID IF2_DESVV Reviewed; 1079 AA.
AC A1VG83;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-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=Dvul_2433;
OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=391774;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP4;
RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA Stahl D.A.;
RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT plasticity.";
RL Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM29449.1; -; Genomic_DNA.
DR RefSeq; WP_011792849.1; NC_008751.1.
DR AlphaFoldDB; A1VG83; -.
DR SMR; A1VG83; -.
DR EnsemblBacteria; ABM29449; ABM29449; Dvul_2433.
DR KEGG; dvl:Dvul_2433; -.
DR HOGENOM; CLU_006301_9_3_7; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000009173; 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.
FT CHAIN 1..1079
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008237"
FT DOMAIN 578..745
FT /note="tr-type G"
FT REGION 52..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..594
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 612..616
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 633..636
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 687..690
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 723..725
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 52..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 587..594
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 633..637
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 687..690
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1079 AA; 115420 MW; 1EA59F81AD3D118F CRC64;
MTENKTKVKD LAAELGVTTK ELGQVLKDMN ISAKTSTSVI AQEDLPRIKE RVQAQRDGGA
RKEGNPDVIV RRRHRDGDRA SARAEAKAPE QEATAAMPET SAPERAEEAD KPAVAKPAKA
PETEAHARAR KEPQAEPVKA RIIRRPDEPA PVAKVVEAAP AETPAPEAPA VKATVTAEAA
PAKTVEPESE RPQADKPATA RVVRPATPDA SAVPDGTSSA PTLPVRSAEP SDTVERADAD
ADGDDDDAQQ RRRKKKRRQP EAVVPQVRVI SRPDPAAVAQ QQMQQQAAQQ QREAGGYRPG
GQRPEGGYRP EGQREGGYRP EGQREGGYRP GGAPRPEGGY RPGGPRPEGG YRPGAPRPEG
GYRPAGGPRP EGQREGGYRP GAPRPEGGYR PAGGAPRPEG QREGGYRPAG GPPRPGGAPR
PGGFGGAPGG MPVPGADGRG DQSKKKRQKG RRTVDFQADG PRGRSDDDVM RGPRGRGKRG
KKDVRPAATQ PLKAIKRKIK VDEAIRVADM AHQMGLKANE IIKVLFGLGV MATINQSLDI
DTATVVAGEF GYEVEKVGFS EDDYLVPKEE DAPETLVTRP PVVTIMGHVD HGKTSLLDAI
RKSNVTAGEA GGITQHIGAY HVTTKKGEIV FLDTPGHEAF TAMRARGAQI TDLVVLVVAA
DDGVMEQTRE AVNHSKAAGV PIMVAVNKMD KEGANPDRVI RELSELGLVA EDWGGDTIFA
KVSAKTREGL DELLELIAIQ AEILELKANP DKAARGHVVE AKLDKGRGPL ATVLVQEGTL
RQGDAFVCGV FAGRVRAMFD DQGRKVKEAG PSTPVEVQGF DGVVEAGEEF VSVADDKVAR
RIAESRAVKQ RERELAKESK VTLETFLSRR ADAAEALTLN LVLKADVQGT LEAISEAVRK
LSTEKVKINI IHGGAGAITE SDILLASASD AIIIGFNVRP TSKVKDIAEQ ENVDIRFYDI
IYKLVDEIKS AMAGMLAPVQ REVYLGQAEV RETFSVPKIG VIAGCHVADG KVTRNAGVRL
LRDGVVVYTG KITSLKRFKD DVRDVQKGYE CGMGLENFND IKVGDVIEAF EMVEEAATL
