IF2_SYNJB
ID IF2_SYNJB Reviewed; 1054 AA.
AC Q2JMD7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CYB_1127;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(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; CP000240; ABD02104.1; -; Genomic_DNA.
DR RefSeq; WP_011432757.1; NC_007776.1.
DR AlphaFoldDB; Q2JMD7; -.
DR SMR; Q2JMD7; -.
DR STRING; 321332.CYB_1127; -.
DR KEGG; cyb:CYB_1127; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001938; 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 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; Reference proteome.
FT CHAIN 1..1054
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335514"
FT DOMAIN 545..718
FT /note="tr-type G"
FT REGION 48..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..561
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 579..583
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 604..607
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 658..661
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 694..696
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 57..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 554..561
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 604..608
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 658..661
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1054 AA; 113440 MW; B601E1AC6C036CED CRC64;
MTDKVRIYDI AREMGRDSRD VLEVCEQLGI PFKTHSSTIS PEQAELVRSK LGAPHIVKPP
RPRPKPPSES LPPEPPAEAK VGERPQQKVP GTASAIVGIR RPAPAQQPAP VGEAKTAETL
PAAKPSLSRP ERVSPEKGSA GGAQLIGPPR RQVTPLVRSS EATQKPETVS QPATPPTPSE
SAAAKASGSE PSPVAKRPIV LSPPQRATSG TKPPAERPEP PQKAPEPSRP SPSEAPSPSH
ARVPQPAEEK APSPPPAQRP RPQLVSAPVR PGTRSPATKE DSVSSGKAGE APRPQRRMEL
VGPPTRPVAK PAPPEPDAAS PLPERIPGER PSPVLVEAPV RPTPPKVKRK TEEEEDDELQ
ALSRRAARVQ AKRKRSRRRG EGDGDGLDLD PMTIISAVKQ AELNALKPLA RPTAKPPSYR
PPAATAAPPA RPRPAARLQQ QPTSAEAGAA DRASGTEPLP EEKVLLLDGS LTVQELAHRL
RVAETEIIKT LFFKGVMVTI NQVLDESLAE SVAKELGYEI RRPKAEPEAK KTEMLDVEDI
DHLVSRPPVV TIMGHVDHGK TTLLDAIRDT KVAQGEAGGI TQRIGAYHVD VNFEGQKRRI
VFLDTPGHQA FTAMRARGAR VTDIAVLVVA ADDGVQPQTL EAISHARAAQ VPIIVAINKI
DKPGSQPERI KQQLAEHGLL PEEWGGDTPM VEVSALTRRN LDALLEMILL VADVAELQAN
PNRPARGTVI EAHLDKARGP VATLLVQNGT LRVGDTLVAG AVLGRVKAMM DDRGQRLQEA
GPSSAVQLLG LDEVPAAGDE FQVYTDEKEA RRIAQERAEV LRQTRLQQAL LSRRVSLGSV
SAKAQEGQLK ELNLIIKTDV QGSAEAIQTA LRDLPQEEVQ LRVLLAAPGE ITETDVDLAA
ASDAIILGFN TTLAPGARQA ADDKGVDVRE YDIIYNLLDD LRAAMEGLLE PEEVEEPLGQ
AEVRLVIPIG RGAVAGSYVL SGKVQRNALV RVRRRGEVVY EGRLDSLKRF KDDVREVAAG
FECGIGIDKF QSWQEGDIIE VYQMVTKRRT LASV
