ID IF2_STRCO Reviewed; 1033 AA.
AC Q8CJQ8;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SCO5706;
GN ORFNames=SC5H4.30, SC9F2.10c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(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; AL939124; CAD55362.1; -; Genomic_DNA.
DR PIR; T35989; T35989.
DR RefSeq; NP_733671.1; NC_003888.3.
DR RefSeq; WP_011030402.1; NZ_VNID01000024.1.
DR AlphaFoldDB; Q8CJQ8; -.
DR SMR; Q8CJQ8; -.
DR STRING; 100226.gene:17763362; -.
DR PaxDb; 100226-SCO5706; -.
DR PATRIC; fig|100226.15.peg.5795; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_11; -.
DR InParanoid; Q8CJQ8; -.
DR OrthoDB; 9811804at2; -.
DR PhylomeDB; Q8CJQ8; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..1033
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137261"
FT DOMAIN 526..698
FT /note="tr-type G"
FT REGION 49..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..542
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 560..564
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 585..588
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 639..642
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 675..677
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 110..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 535..542
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 585..589
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 639..642
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1033 AA; 105658 MW; 47D581FB0072A045 CRC64;
MAKVRVYELA KEFGVESKVV MAKLQELGEF VRSASSTIEA PVVRKLTDAF QQGGGNGRSA
GRPAAPKKAA PRPSAPSPAQ AGPSQAAPAA GDRAAAPRPS AAPKAPAAQQ PAAPSAPAPA
PSQGPRPTPG PKPAPRPAPA APEFTAPPAA PAAPSTPAPA PSGPKPGGAR PGAPKPGGAR
PSGPGQDRGQ QGGQGRPGGQ RPGAPAQRPG GRPGGPRPGN NPFTSGGNAG MARPSAPRPQ
GGPRPGGPGG APGGGPRPQG PGGQGGGPRP QAPGGNRPSP GSMPRPQGGG AGPRPGGGPR
PNPGMMPQRP AAGPRPGPGG GGRGPGGAGR PGGGGGRPGG GGFAGRPGGG GGGRPGGGGG
FAGRPGGGGG FGGGGGRPGF GGRPGGPGGR GGTQGAFGRP GGPARRGRKS KRQRRQEYEA
MQAPSVGGVM LPRGNGETIR LSRGASLTDF AEKINANPAS LVAVMMNLGE MVTATQSVSD
ETLHLLAGEM NYTVQIVSPE EEDRELLESF DLEFGEDEGS EEDLVVRPPV VTVMGHVDHG
KTRLLDAIRK TNVIAGEAGG ITQHIGAYQV ATEVNDEERK ITFIDTPGHE AFTAMRARGA
RSTDIAILVV AANDGVMPQT VEALNHAKAA EVPIVVAVNK IDVEGADPTK VRGQLTEYGL
VAEEYGGDTM FVDISAKQGL HIDSLLEAVV LTADASLDLR ANPVQDAQGI SIESRLDRGR
GAVATVLVQR GTLRVGDTMV VGDAYGRVRA MLDDNGNNVA EAGPSTPVQV LGLTNVPGAG
DNFIVVEEDR TARQIAEKRA ARERNAAFAK RTRRVSLEDL DKVLKAGEVQ QLNLIIKGDA
SGSVEALESS LLQLDVGEEV DIRVLHRGVG AVTESDIDLA MGSDAIVIGF NVRAAGRAAQ
MAEREGVDVR YYSVIYQAIE EIEAALKGML KPEYEEVELG TAEIREVFRS SKLGNIAGVL
IRSGEVKRNT KARLLRDGKV IAENLNIEGL RRFKDDVTEI REGFEGGINL GNFNDIKVDD
VIATYEMREK PRV
//
