IF2_THEFY
ID IF2_THEFY Reviewed; 955 AA.
AC Q47RV1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Tfu_0778;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54816.1; -; Genomic_DNA.
DR RefSeq; WP_011291225.1; NC_007333.1.
DR AlphaFoldDB; Q47RV1; -.
DR SMR; Q47RV1; -.
DR STRING; 269800.Tfu_0778; -.
DR PRIDE; Q47RV1; -.
DR EnsemblBacteria; AAZ54816; AAZ54816; Tfu_0778.
DR KEGG; tfu:Tfu_0778; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_4_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
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 PRINTS; PR00315; ELONGATNFCT.
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..955
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228254"
FT DOMAIN 448..620
FT /note="tr-type G"
FT REGION 49..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..464
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 482..486
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 507..510
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 561..564
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 597..599
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 93..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 507..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 561..564
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 955 AA; 100542 MW; FAFA0FF27CF70995 CRC64;
MAKVRVYELA KEFGVESKAV LAKLQEMGEF VRSASSTVEA PVVRRLKEAF SQSSESTEGA
KGGQEKKKPS PKPQPSPQQQ TKASAPSAGG ETPRPAVPKP GPGLKPGPRP VPKPGPRPGP
RPEGGAGKAG QQPSGAQGPA RPESGKTPRP VPKPGPRPGN NPFSSTASGM GTRPTPRPPA
SGGTGAPRPG PRPHPGMMPP RPGASAGGPP RPQAPRPQAP RPGPGTAGGR PGSSAGGPPR
PVPRPGPRPS PMNMPASRPT PPGGARPSTS SRSGGGRGRG GGGGAGPRGG GAGGGAPRTG
FGGRPGGGRG RGGTAGAFGR PGGRPSRSRK SKKQRRQELK DMQAPSFGGV KIPSGNGKVI
RLSRGASLAD FGERIDVNPA SLVQVVMTQL GEMVTATQSL PDETLQLLGE ELNYTVEVVS
PEDEDRELLE SFSIEFGEDI GSEEDLKPRA PVVTVMGHVD HGKTRLLDAI RNTNVASGEA
GGITQHIGAY QVTTTVDGEE RKITFIDTPG HEAFTAMRAR GAQATDIAVL VVAADDGVKP
QTAEAIDHAK AADVPIVVAV NKIDLPTADP QKVRAQLTEY GLVAEEYGGN VQFVDISAKE
NLNIDQLLEA IILTADAELD LKANPDMPAQ GLAIEAYLDR GRGSMATVLV QRGTLRVGDS
IVCGDAYGRV RAMLDENGNR VKEAEPSRPV QVLGLTNVPS AGDSFLVVKD DRVARQIAQQ
REARERFAQQ AKASRRVTLD NWQKTLEEGQ REELLLIIKG DMSGSVEALE ESLLKIDPGT
DEVAIRVIGR GVGAITQNDI NLAASSGAVI IGFNVRPEGK NSELAERMGV DIRYYSVIYQ
AIEEVEAALK GMLKPEYEEV QLGTAEIREI FKVPRVGNVA GAVVRSGVIK RNAKARLIRD
GVVVSDNLTV ESLRRFKDDV TEVREGFECG IGIGYNDIRV EDIIETFEMR EKPRD
