IF2_CALS4
ID IF2_CALS4 Reviewed; 707 AA.
AC Q8RA37;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=TTE1393;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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; AE008691; AAM24615.1; -; Genomic_DNA.
DR RefSeq; WP_011025678.1; NC_003869.1.
DR AlphaFoldDB; Q8RA37; -.
DR SMR; Q8RA37; -.
DR STRING; 273068.TTE1393; -.
DR PRIDE; Q8RA37; -.
DR EnsemblBacteria; AAM24615; AAM24615; TTE1393.
DR KEGG; tte:TTE1393; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000555; 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; 2.
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; Reference proteome.
FT CHAIN 1..707
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137274"
FT DOMAIN 209..378
FT /note="tr-type G"
FT REGION 55..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..225
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 243..247
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 264..267
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 318..321
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 354..356
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 264..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 318..321
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 707 AA; 78857 MW; 4E134B2BC0ED0AEC CRC64;
MEVNNMSKTR VYELAKELNI SSKDLLSKLS DLDIKVKNHM STLEDEEVEL IKDLLAEKPK
EEKQKDQKNH EQEAQDKEEK EIEEDSFYED REEKRAYKKS FKKGGKKNKK LQKKFVSEES
AKEDEIKIIT IPEFLTVKEL AEKMKVNPTE IIKKLIAQGI MVTVNQQIDF ETASKIAEEY
GFLVDKEEVK DELEAIFEDT PDREEDLKPR PPIVTVMGHV DHGKTSLLDA IRKTNVTMKE
MGGITQHIGA SVVEINDKKV VFLDTPGHEA FTAMRARGAS VTDIVVLVVA ADDGVMPQTI
EAINHVKAAN VPLIVAINKI DLPTANPDRV KTELSELGLV PEEWGGNTIC VPVSAKKNIG
IDDLLEMILL VAEMEDLKAN PNKPARGTVI EAKLEKGKGP VATVIVQNGT LQVGDAVIAG
TTYGKVRAMF DDKGRKIKKA GPSMPVEILG FSEVPEAGDK FVVVENEKKA RELAEKRREV
QRELELKKKQ KVSLEDLFRQ IQEGTVKELN VIIKADVQGS VEALRKSLEE LSNEEVRIRV
IHGAVGAITE TDVMLASASN AIIIGFNVRP ETNAKALAEK EKVEIKLYRI IYDAIEDVKA
AMKGMLEPKY KEVELGRAEV RAVFKIPGVG NVAGCYVLNG KIARNADVRI VRDGIVIYEG
KIASLKRFKD DVREVQQGFE CGIGIEKFND IKEGDIIEAY TMEEIPR
