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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
 
 
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