IF2_SYNS3
ID IF2_SYNS3 Reviewed; 1129 AA.
AC Q0I7K2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=sync_2373;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI47785.1; -; Genomic_DNA.
DR RefSeq; WP_011620280.1; NC_008319.1.
DR AlphaFoldDB; Q0I7K2; -.
DR SMR; Q0I7K2; -.
DR STRING; 64471.sync_2373; -.
DR EnsemblBacteria; ABI47785; ABI47785; sync_2373.
DR KEGG; syg:sync_2373; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001961; 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..1129
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008363"
FT DOMAIN 621..793
FT /note="tr-type G"
FT REGION 33..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..637
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 655..659
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 680..683
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 734..737
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 770..772
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 87..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..515
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 630..637
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 680..684
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 734..737
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1129 AA; 118580 MW; 765D622197447654 CRC64;
MTSSGKVRIY ELSKDLGLEN KDVLDAAEKL SIAARSHSSS ISETEAGKIR TLLKQGGSPV
ASAPAKPAPG KAILSVRKAS SPAAPSMPSK PAAPAAAKPS PKPSAPSRPE APLPLIVQKP
VSRQAAPQKP VSRQSTPAAA APAAAPSAPA PSAPTPRPKP TAPKASAPAP TASAPSAPPR
PTSARPTPAP ARPTGTSPVK RPGSEASSPR PTAPPTRPQP KAPVNRGAPA RPAPKPELVG
RPQPKRAAPG APVRQIGQRP GVSPRPSGPP GQRANMPQRP AGSQRPGAPT RPGNAPSKPG
QPRSGASSLE LVGKPIRRDG SNDGAGGRSD GQGRPPGAPR PGAPRPGGMP GMRKPVAPGE
LMQLQKPNSR PSAPPPRRVD GTPVATRSGE AAAGGAKATP PVSRPTATPP AAPRRPGFRP
GPGAGGQRRP GRPDWDDSAK LEALRSKSPQ KQRQKVHIIG ENDDALTAET GGFAGERQAM
VLSASLARPS KPRTKHKPAP KPVAAIRKRR KETARQRQRR RAMELRAARE AKQVRPEMIV
VPEDNLTVQE LADMLSIESS EIIKSLFFKG VIATVTQTLD MPTIEAVAQE FGVPVLQDDV
EEAAKKTVEM IEEKDHAHLI RRPPVVTVMG HVDHGKTSLL DAIRQARVAA GEAGGITQHI
GAYQVEIQHN DSPQRLTFLD TPGHEAFTAM RARGTKVTDV AVLVVAADDG VRPQTLEAIS
HARAAEVPVV VAINKIDKEG ASPDRVKQEL SEQNLLAEDW GGDVVMVPVS ALRGENIDKL
LEMILLVTEV EDLQANPDRL AKGTVIEAHL DKAKGPVATL LVQNGTLRTG DVLAAGPVLG
KVRAMVDDGG GRLKEAGPSC AVEALGFSEV PTAGDEFEVY PDEKSARAVV GDRASDARAS
RLAQQMASRR VSLTAMSGQA KEGELKELNL ILKADVQGSV EAILGSLEQL PKDEVQVRVL
LSAPGEVTET DVDLAAASGA VIVGFNTSMA SGAKRAADAN SVDVRDYDVI YKLLEDIQLA
MEGLLEPELV EESLGEAEVR AVFTIGKSAV AGCYVTTGKL QRNCKVRVRR GKEIVFAGDL
DSLRRNKDDV KDVATGFECG IGCDRFANWK DGDIVEGYKL VTQRRKLAT
