IF2_ROSCS
ID IF2_ROSCS Reviewed; 738 AA.
AC A7NID1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Rcas_1132;
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) 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; CP000804; ABU57231.1; -; Genomic_DNA.
DR RefSeq; WP_012119661.1; NC_009767.1.
DR AlphaFoldDB; A7NID1; -.
DR SMR; A7NID1; -.
DR STRING; 383372.Rcas_1132; -.
DR PRIDE; A7NID1; -.
DR EnsemblBacteria; ABU57231; ABU57231; Rcas_1132.
DR KEGG; rca:Rcas_1132; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000263; 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..738
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335504"
FT DOMAIN 238..405
FT /note="tr-type G"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..254
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 272..276
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 293..296
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 347..350
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 383..385
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 101..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 293..297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 347..350
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 738 AA; 78190 MW; C1F603E012C09990 CRC64;
MNSMRISGHQ SAVDARDHIE FAGGGRGPGN PGGGRGPGSP GGGRGPGSPG GGRGPGSPGG
GRGPGSPGGG RGPGSPGGGR GPGSPGGGRG PGGGRGPSGG RGGDGRRREE SPTDHEDGRI
NRSGRSTSTT TTRTSSTLAR PTTVRAPVRP KGPIALPVTM TVREFSEATG VGAAEILKAL
LKAGVVANIN QQIDYETAAV IAADFGIETV EYVPPQLEGI VENIRDVLAA QDPKDLKPRP
PVVTIMGHVD HGKTKLLDAI RSTRVAESEA GGITQHIGAY QVELHGRKIT FLDTPGHEAF
TAMRARGAQV TDIVVLVVAA DDGVMPQTLE AISHVKAAGV PMIVAINKID APNANPDRVR
QQLANAGVIV EQFGGDVPSV EVSAKLKKNI DGLLEMILLV ADLNEYKANP NAPAVGTIVE
AEMDRTRGPV ATVLVQNGTL RLEDNVLVGA TTGTIRTMFN DAGKRLRFAE PATPVVILGL
NDVPQAGDIL QVMPDLTVAR EIALQRQRKQ RLEAMASTRG VSLDGLFSSI QQGKIKELNI
ILKADVQGSI GAIEHALSQL NTDEVQIRII HRGTGTITES DVNLAIASHA IIIGFNARPD
PAARRQAEQY GVDIRFYNII YQLTEDIKKA MIGMLEPEYR EVTEGFAEVR TTFRLPTREI
VAGLYVTEGK ITRQYNVRVL RNGVVIHDGK IASLKRFKDD VREVQAGYEC GLIVEGFNDI
TPGDTMEFYR RERVERTV
