IF2_SYNPW
ID IF2_SYNPW Reviewed; 1123 AA.
AC A5GNJ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=SynWH7803_2079;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT971583; CAK24505.1; -; Genomic_DNA.
DR RefSeq; WP_011933970.1; NC_009481.1.
DR AlphaFoldDB; A5GNJ0; -.
DR SMR; A5GNJ0; -.
DR STRING; 32051.SynWH7803_2079; -.
DR EnsemblBacteria; CAK24505; CAK24505; SynWH7803_2079.
DR KEGG; syx:SynWH7803_2079; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001566; 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..1123
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008361"
FT DOMAIN 615..787
FT /note="tr-type G"
FT REGION 52..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..631
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 649..653
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 674..677
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 728..731
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 764..766
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..266
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 624..631
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 674..678
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 728..731
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1123 AA; 118866 MW; DA4C132DF5A3EAA1 CRC64;
MTSSGKVRIY ELSKDLGLDN KDVLDAAEKL SIAAKSHSSS ISETEAGKIR SLLKAGSAPR
AAASPSKPAP GKAILSVQKA GSGSNSPARP EQPKPAASSP PAAPAAPTKA KSPQQPPARP
AAPSRPAAPK ASATQTSAPQ KPVVRQQPTA QQPVPRPKPK TAPERTVSRP PSPPARPVPQ
QPSPPSAKPR GTAPIRRAAP NDAPRPANAP PSRPQPKTPV NRTAPPPQRP AAKPELVGRP
QPRRPEGPPT RQGAGPGSPR PAVSPRPSAP GSQRNMPQRP AGAQRPGAPT RPGTGAGRPS
RPGGNTLELV GKPIRRDGSG NRGEGGRPPG GARPAGGGNR PAMPPGMRKP VAPGELMQLQ
KPSGRPGVPP PRRPDGTPVT PRGDGPKATP PVSRPTATPP SPATAPRRPG GFRPGAGPGG
QRRPGRPDWD DSAKLDALRN RSPQKQRQKV HIIGENDDSL AAQTGGFAGE QQNMVLSASL
ARPSKPKSQQ KAAPKPVAAM RKRRKETTRQ RQRRRAMELR AAREAKQVRP EMIVVPEDNL
TVQELADMLS VESSEIIKSL FFKGIIATVT QSLDMPTIET VAEEFGVPVL QDDVEEAAKK
TVEMIEEQDL EHLIRRPPVV TVMGHVDHGK TSLLDAIRKA RVAAGEAGGI TQHIGAYQVE
IEHSGEPRRL TFLDTPGHEA FTAMRARGTK VTDVAVLVVA ADDGVRPQTL EAISHARAAE
VPIVVAINKI DKEGASPDRV KQELSEQNLL AEEWGGDVVM VPVSAIKSEN IDKLLEMLLL
VTEVEDLQAN PDRLARGTVI EAHLDKAKGP VATLLVQNGT LRTGDVVAAG PVLGKVRAMV
DDASVRLKEA GPSCAVEALG FSEVPTAGDE FEVYPDEKSA RAVVGDRASD ARATRLAQQM
ASRRVSLTAM SGQANDGDLK ELNLILKADV QGSVEAILGS LEQLPKDEVQ VRVLLSAPGE
ITETDVDLAA ASGAVIVGFN TSMASGARKA ADANGVDVRD YDVIYKLLED IQLAMEGLLE
PELVEEALGE AEVRAVFTIG KSAVAGCYVT TGKLQRNCKV RVHRGKEIVY AGDLDSLRRN
KDDVKEVATG FECGVGTDRF ANWQDGDRIE AFKMVTQRRK LTT
