IF2_SYNR3
ID IF2_SYNR3 Reviewed; 1106 AA.
AC A5GVG4;
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=SynRCC307_1970;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
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; CT978603; CAK28873.1; -; Genomic_DNA.
DR RefSeq; WP_011936385.1; NC_009482.1.
DR AlphaFoldDB; A5GVG4; -.
DR SMR; A5GVG4; -.
DR STRING; 316278.SynRCC307_1970; -.
DR PRIDE; A5GVG4; -.
DR EnsemblBacteria; CAK28873; CAK28873; SynRCC307_1970.
DR KEGG; syr:SynRCC307_1970; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001115; 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..1106
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008362"
FT DOMAIN 598..771
FT /note="tr-type G"
FT REGION 57..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..614
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 632..636
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 657..660
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 711..714
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 747..749
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 77..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 607..614
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 657..661
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 711..714
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1106 AA; 116652 MW; DC7C2971774FF948 CRC64;
MTSGGKVRIY ELSRDLGLDN RDVLNAAEKL SIAAKSHSSS ISDGEAAKIK ALLNSNGKAA
GGAKAPAKPD AGNQILSLKK APSTPSQSAG APASAPPSRK PEIVAKPAAP ASPAKPAPSA
PPSRKPEIVA KPAAPASPAK PAPSAPPSRK PEVVAKPAAP ASPAKPAPKP VAKPVAKPAS
APAPARPAQP LRPQASNRPP QQPSNRPPAR PAAKPPVVMS KPTAPPPRPA RPGAPAPRRD
QNRPAVPMRP PNQQQRPSPQ RSGPPRSGAP IRPGAPQRPG MPGRGGAPQQ RRGPGGPGGR
PPSSLELVGK PIRREPNAPQ GRQGGAPSRP GGPGGMRKPV SPGELMQLQK PGSRPTPGDG
PRRPPARPGS EAPRRPGEAP NRPNAPTAPP RRPGYRPAAA PGMAGRPRRP DWDDSARLDA
LRSRSPQKQR QKVHIIGEND DSLAAQTGGF AGGQEALVLQ ASLARPSKPK NLPGNKGARP
VALRRRKKET TRQRQRRRAM ELRQAREAKQ IRPEMLVVPE GNLTVQELAD KLSVESSEII
KSLFFKGIIA TVTQTLDLES IEKVSQEFGV PVLQDDIEEA AKKTVEMIEE SDLDHLIRRP
PVVTVMGHVD HGKTSLLDAI RKTRVAAGEA GGITQHIGAY QVDVDHAGAS KKVTFLDTPG
HEAFTAMRAR GTKVTDVAIL VVAADDGVRP QTLEAISHAR AAEVPIVVAI NKVDKEGAQI
DRVKQELSDQ SLLAEDWGGD TVMVPVSALK GEGLDKLLEM ILLVTEVEDL KANPERMAKG
TVVEAHLDKA KGPVATLLVQ NGTLRPGDVV AAGPVLGKVR AMVNDSGRRV KEAAPSSAVE
VLGFSEVPAA GDEFEVYPDE KAARSVVGDR ASEARATRLA QQMASRRVSL TSMSGQASEG
ELKELNLILK ADVQGSVEAI LGMLEQLPQG EVQVRVLLSA PGEVTETDVD LAAASGAVIV
GFNTTLASGA RRAAELAGVD VRDYNVIYKL LEDIQAAMEG LLEPELVESP LGEAEVRAVF
SIGKSAVAGC YVTSGSIQRN CKIRVHRGKQ LVFSGDLDSL KRMKNDVKEV NTGFECGFGC
DRFADWQEGD RVEAFAMVTQ RRTLAT