IF2_RHOP2
ID IF2_RHOP2 Reviewed; 886 AA.
AC Q2J2J9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RPB_0600;
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-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; CP000250; ABD05311.1; -; Genomic_DNA.
DR RefSeq; WP_011439501.1; NC_007778.1.
DR AlphaFoldDB; Q2J2J9; -.
DR SMR; Q2J2J9; -.
DR STRING; 316058.RPB_0600; -.
DR EnsemblBacteria; ABD05311; ABD05311; RPB_0600.
DR KEGG; rpb:RPB_0600; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008809; 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..886
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008314"
FT DOMAIN 383..554
FT /note="tr-type G"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..399
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 417..421
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 440..443
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 494..497
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 530..532
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 65..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 440..444
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 494..497
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 886 AA; 95490 MW; 05BE9F6CF93272CE CRC64;
MVDTKTPGDK TLSMPSKTLT LKPRVEQGVV RQSFSHGRSK QVVVEKRGKR RIGGDGAPEP
AAAPEVAKKP APAPAPAAPS PRQQPRPSPQ QQARSGMVLR TLTEDERSAR ATALADARVR
EVEERRQAEI EAQRRAAQEV VDKAEREAAE ARRKAEEERH RHEEETKRKA ETEAKKRFGE
TEPAARKPAD GGRPAAGATT TAPRAPVTTT TTRPPAVAAE AGDDDEAPRM VRRGPGGGPA
RPAPPPKQPA AKPGASKQRG RLTLVTALNA DDVRERSIAS FRRRTQRLKG HASNEPKEKL
VREVIVPEAI SIQELANRMS ERAVDVIRLL MKQGAMHKIN DVIDADTAQL IAEELGHTVK
RVAASDVEEG LFDVVDNSTD TEPRSPVVTV MGHVDHGKTS LLDALRHANV VSGEAGGITQ
HIGAYQVTSP ESGKKITFID TPGHAAFTAM RARGAKVTDI VVLVVAADDG VMPQTIEAIN
HAKAANVPII VAINKIDKPD AKPERVRTEL LQYNVQVESL GGDVVDVEVS AKNKTNLDKL
LEMIALQAEL LDLKTNEQRP AEGTVIEAKL DRGRGPVATV LVQRGTLKVG DIIVAGAEMG
RVRALISDQG DTVDSAGPSV PVEVLGFNGP PEAGDRLAVV ENEARARQVT SYRAHQKREK
AASIVGMRGS LEQMMSQLKT TGRKDFPLIV KADVQGSLEA ILGSLEKLGT DEVAARILHA
GVGGISESDV TLAEGFSAVI LGFSVRANKE AAAAAKRNGI EIRYYNIIYD LVDDIKKAMS
GLLAPTLRET MLGNAQILEI FNISKVGKVA GCRVTDGTVE RGANVRLIRD NVVVHEGKLS
TLKRFKDEVK EVQSGQECGM AFENYTDMRA GDVIECYRVE TIQRSL
