IF2_SYNY3
ID IF2_SYNY3 Reviewed; 1001 AA.
AC P72689;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=slr0744;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA16696.1; -; Genomic_DNA.
DR PIR; S74544; S74544.
DR AlphaFoldDB; P72689; -.
DR SMR; P72689; -.
DR IntAct; P72689; 4.
DR STRING; 1148.1651769; -.
DR PaxDb; P72689; -.
DR PRIDE; P72689; -.
DR EnsemblBacteria; BAA16696; BAA16696; BAA16696.
DR KEGG; syn:slr0744; -.
DR eggNOG; COG0532; Bacteria.
DR InParanoid; P72689; -.
DR OMA; NIAVKSH; -.
DR PhylomeDB; P72689; -.
DR Proteomes; UP000001425; 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; 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..1001
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137269"
FT DOMAIN 493..666
FT /note="tr-type G"
FT REGION 34..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..509
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 527..531
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 552..555
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 606..609
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 642..644
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 65..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 502..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 552..556
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 606..609
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1001 AA; 108119 MW; 4C7F00DEE56CE31C CRC64;
MNNAKVRIYD LSKELNLENR DILDICERLN VAAKSHSSTI SESDAERIKA AAEKFTPQQP
KKPRVASRPE SKEDKSDPKQ QKILAIHHKQ EKSGGPSPAR PTPPPRPKLQ APKAPTPPQP
PVAKASAPKI QKQEEPAQEA PKSVAPPTQP LAPPPVPSLQ SPPSKPAPPT PPAKKAAPAP
RLAGPPGRTA SPNKTAVPAP AKPKVNRPEI VSLKDNRGQA RSPGDREEKV AIAAPEPPKP
KVELRRPKPP RPEEDENLPE LLEFPPLSRG KGVDGDNDAD DGDLLSTEKP KPKLKRPTPP
RLGKPDQWED DEDEKANKAK AANKGKRRPK MDDDDDDLDI DGDNGPKPTL VSLSIARPPK
PKSLAAKPST PTVAKVKKPT LKSEAGSSAG GSSRSRGDRR DRKEVVQKPE VIMLDRSLTV
RDLADLLKIS ETDIIKRLFL KGVAVQITQT LDEETARMVA ESFEVAVETP ERVAAAAKTT
EMLDEADLDN LVRRPPVVTI MGHVDHGKTT LLDSIRKTKV AQGEAGGITQ HIGAYHVEVE
HNDKTEQIVF LDTPGHEAFT AMRARGAKVT DIAILVVAAD DGVQPQTKEA ISHAKAAGVP
LIVAINKVDK PEANPDRIKQ ELSELGLLAE EWGGDTIMVP VSALNGDNLD GLLEMILLVS
EVEELVANPN RQAKGTVIEA NLDRTRGPVA TLLIQNGTLR VGDAIVVGAV YGKIRAMIDD
RGDKVEEASP SFAVEILGLG DVPAAGDEFE VFTNEKDARL QAEARAMEDR QTRLQQAMSS
RKVTLSSISA QAQEGELKEL NIILKADVQG SLGAILGSLE QLPQGEVQIR VLLASPGEVT
ETDVDLAAAS GAIIIGFNTT LASGARQAAD QEGVDIREYD IIYKLLDDIQ GAMEGLLDPE
EIESSLGTAE VRAVFPVGRG NIAGCYVQSG KIIRNRNLRV RRGDQVLFEG NIDSLKRIKE
DVREVNAGYE CGIGCSKFND WKEGDIIEAY EMTMKRRTLA T
