IF2_CHLAD
ID IF2_CHLAD Reviewed; 753 AA.
AC B8GAE2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Cagg_3681;
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) 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; CP001337; ACL26517.1; -; Genomic_DNA.
DR RefSeq; WP_015942362.1; NC_011831.1.
DR AlphaFoldDB; B8GAE2; -.
DR SMR; B8GAE2; -.
DR STRING; 326427.Cagg_3681; -.
DR EnsemblBacteria; ACL26517; ACL26517; Cagg_3681.
DR KEGG; cag:Cagg_3681; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002508; 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..753
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202765"
FT DOMAIN 249..418
FT /note="tr-type G"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..265
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 283..287
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 304..307
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 358..361
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 394..396
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 304..308
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 358..361
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 753 AA; 80879 MW; C93F65E66306C05A CRC64;
MSEKPRRDTG GTGTGSGRST GQSTNRTSNQ QTGTGRTPTA TGAHRQPANQ STGGGRSSST
GGRNTPTNQG NARPAAPANA RSGNQPARGN NAPAASRSGG STPAPVRGGG ATPAPARGTN
TRNARSQQSR GRPQPEERER EREAVLRRPP TPTTTRPVMR PRGPVALPPV MTVRELSEAT
GIGAADILKT MLKAGMIANI NQQIDYETAA LIMTDFGIET VENMPEQMVG IVEDVKEVLR
SQPPEEMRPR PPVVTIMGHV DHGKTKLLDA IRSTRVAEGE AGGITQHIGA YQVEVNHRKI
TFLDTPGHEA FTAMRARGAQ VTDIVVLVVA ADDGVKPQTE EAIAHVKAAG VPMIVAINKI
DLPTANPDRI KQQLAALDVI VEEYGGNVPC VHVSARQKIN IDGLLEMILL VADLEDLRAN
PNAPAVGTII EAKLDKSRGP VATVLIQNGT LHLEDNVLVG CVAGKIKSMF SDSGKRLRHA
EPSTPVEIIG LEGVPQAGDI LQVMDDLVLA REIALQRQRQ QRAEAMAASA RGTSLEELFG
KVKQGQVKEL NLILKADVQG SLDAIAHLIE QLNQSQNEVQ TRIIHRGVGA ITEGDVNLAL
ASHAIIIGFN ARPDPAARRH AEQHGIDIRF YNIIYQLQDD LKKAMAGMLA PTFKEVVEGY
AEVRNIFRLP TREVVAGVYV TDGKITRTGQ NVRVLRRGVV IHDGKISSLK RFKDDVREVT
AGYECGLIVE GFNDIEIGDA LEFYRQEQVA ATL
