IF2_RHOPS
ID IF2_RHOPS Reviewed; 883 AA.
AC Q13EL8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RPD_0231;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5;
RG US DOE Joint Genome Institute;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-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; CP000283; ABE37471.1; -; Genomic_DNA.
DR AlphaFoldDB; Q13EL8; -.
DR SMR; Q13EL8; -.
DR STRING; 316057.RPD_0231; -.
DR EnsemblBacteria; ABE37471; ABE37471; RPD_0231.
DR KEGG; rpd:RPD_0231; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; RPAL316057:RPD_RS01170-MON; -.
DR Proteomes; UP000001818; 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; 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; PF03144; GTP_EFTU_D2; 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.
FT CHAIN 1..883
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008317"
FT DOMAIN 380..551
FT /note="tr-type G"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..259
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 437..440
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 491..494
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 527..529
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Polar 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 437..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 491..494
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 883 AA; 95349 MW; 653950FBA3D9B8FE CRC64;
MVDTKTPGDK TLSMPTKTLT LKPRVEQGVV RQSFSHGRSK QVVVEKRGKR RVGGDGPAEP
AAAAPEVVKK PTPAPPAVSP RQQPRPSPQQ QARSGMVLRT LTEDERSARA TALADARVRE
VEERRLAEIE AQRRAAQELV DKAEREAAEV RRKAEEERHR HEEETKRKAE TEAKKRFGEA
EPAKKPADGR PASTSTTTTA PRAPVTTTTR PPAVAAEAGD DDEAPRMVRR GPGGGPARPA
PPPKQPAAKP GASKQRGRLT LVTALTADDV RERSIASFRR RTQRLKGHAS NEPKEKLVRE
VIVPEAISIQ ELANRMSERA VDVIRMLMKQ GAMHKINDVI DADTAQLIAE ELGHTVKRVA
ASDVEEGLFD VVDNSTDTEP RSPVVTVMGH VDHGKTSLLD ALRHANVVSG EAGGITQHIG
AYQVTSPETG TKITFIDTPG HAAFTAMRAR GAKVTDIVIL VVAADDGVMP QTVEAINHAK
AAGVPIIVAI NKIDKPDAKP ERVRTELLQY NVQVESLGGD VVDVEVSAKN KTNLDKLLEM
IALQAELLDL KTNESRPAEG TVIEAKLDRG RGPVATVLVQ RGTLKVGDII VAGAEMGRVR
ALISDQGDNV DFAGPSVPVE VLGFNGPPEA GDRLAVVENE ARARQVTSYR AHQKREKAAS
IVGMRGSLEQ MMSQLKTTGR KDFPLIVKAD VQGSLEAILG SLEKLGTDEV AARILHAGVG
GISESDVTLA EGFSAVILGF SVRANKEAAA AAKRNGIEIR YYNIIYDLVD DVKKAMSGLL
APTLRETMLG NAQILEIFNI SKVGKVAGCR VTDGTVERGA NVRLIRDNVV VHEGKLSTLK
RFKDEVKEVQ SGQECGMAFE NYTDMRAGDV IECYRVETIQ RSL
