IF2_SYNS9
ID IF2_SYNS9 Reviewed; 1176 AA.
AC Q3AZB7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=Syncc9902_0592;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) 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; CP000097; ABB25560.1; -; Genomic_DNA.
DR RefSeq; WP_011359405.1; NC_007513.1.
DR AlphaFoldDB; Q3AZB7; -.
DR SMR; Q3AZB7; -.
DR STRING; 316279.Syncc9902_0592; -.
DR EnsemblBacteria; ABB25560; ABB25560; Syncc9902_0592.
DR KEGG; sye:Syncc9902_0592; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 65878at2; -.
DR Proteomes; UP000002712; 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 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..1176
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008364"
FT DOMAIN 668..840
FT /note="tr-type G"
FT REGION 32..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..684
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 702..706
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 727..730
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 781..784
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 817..819
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 130..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..274
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 677..684
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 727..731
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 781..784
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1176 AA; 122800 MW; BC4C2252CA6DB827 CRC64;
MTSSGKVRIY ELSKDLGLEN KDVLDAAEKL SIAAKSHSSS ISDSEAGKIR SLLGKGASPS
QPTAPAAKPA PAKPAAGKSI LSVKKAPASP GVTAPVAAAK PQAPAQPAAS KPLQPSVKAV
APPARPAPAG STSAGSTPNK PATAPARPTA ATTTSTPRPA AAAAPSRPAP SKPQGAPKPQ
VVGKPSAPEL VSKPTPATKP TGAAKPAIVS KPITAAKPAV VAKPAAAKPT IVKPTAPTPR
PASSPAAASS APPPASTPRP APSRPTPRPA AAPSRPGAPQ GQKPQIVSRA GAPPRPGTPP
RVGAPTKTGT PARPTPRPEL VGKPVPRRTG GVGAPQRPGT GVPQRQGGPA RPGAPTRTGK
PGAPTRPGGN TLELVGKPIR RDGSSASGRP GAPTRPGAPT RPGMPGGMRK PVAPGELMQL
QKPISRPAAP APRRPDAPNR PTEAAGTATP PVARPTAPSA PRRPGFRPGA PGGQRRPGRP
DWDDSAKLEA LRSRSPQKQR QKVHIIGEND DALAAQTGGF AGEQQAMVLS ASLARPAKPK
AQQRTAPKPV AAVRKRRKET ARQRQRRRAM ELRAAREAKQ VRPEMIVVPE DNLTVQELAD
MLSIESSEII KSLFFKGVIA TVTQTLDMPT IEAVAKEFDV PVLQDDVEEA AKKTVEMIEE
ADLKHLIRRP PVVTVMGHVD HGKTSLLDAI RQARVAAGEA GGITQHIGAY QVEIQHKDEA
RKLTFLDTPG HAAFTAMRAR GTKVTDVAVL VVAADDGVRP QTLEAISHAR AAEVPIVVAI
NKIDKEGASA DRVKQELSEQ NLLAEEWGGD VVMVPVSAIK GENIDKLLEM LLLVTEVEDL
QANPDRPARG TVIEAHLDKA KGPVATLLIQ NGTLKTGDVL AAGPVLGKVR AMVDDNRQRL
KEAGPSFAVE ALGFSEVPTA GDEFEVYPDE KAARAVVGDR ASNARATRLA QQMASRRVSL
TAMSGQANEG ELKELNLILK ADVQGSVEAI LGSLEQLPKD EVQVRVLLSA PGEITETDVD
LAAASGAVII GFNTSMASGA KKAADATGVD VRDYDVIYKL LEDIQLAMEG LLEPELIEEA
LGEAEVRAVF TIGKSAVAGC YVNTGKLHRN CRVRVHRGKQ VVYTGDLDSL RRNKDDVKEV
ATGFECGVGA DRFANWEEGD RIEAFKMVTQ RRKLTT
