IF2_SYNSC
ID IF2_SYNSC Reviewed; 1104 AA.
AC Q3AHW1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=Syncc9605_2081;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-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; CP000110; ABB35821.1; -; Genomic_DNA.
DR RefSeq; WP_011365030.1; NC_007516.1.
DR AlphaFoldDB; Q3AHW1; -.
DR SMR; Q3AHW1; -.
DR STRING; 110662.Syncc9605_2081; -.
DR EnsemblBacteria; ABB35821; ABB35821; Syncc9605_2081.
DR KEGG; syd:Syncc9605_2081; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 65878at2; -.
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.
FT CHAIN 1..1104
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008365"
FT DOMAIN 596..768
FT /note="tr-type G"
FT REGION 51..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..612
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 630..634
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 655..658
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 709..712
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 745..747
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 187..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 605..612
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 655..659
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 709..712
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1104 AA; 116171 MW; 5905A4775649B80A CRC64;
MTSSGKVRIY ELSKDLGLEN KDVLDAAEKL SIAAKSHSSS ISDAEAGKIR SLLGKGGNGA
KPAAAAPAKP APGKAILSVK KAAPATPSKP TPAVSKPVAK PVAAKPVVTK PAAAVKPQAA
PKPPAAATPK PVISKPAPAL VKAAAAPARP TAAKPVPRPA AAKPQVVSKP AAGKPKLVSK
PKATAKPTAP TPRPTPARPT PRPAGAGSPA RPTPGQGQPK PQIIRSGAPS RPGAPTRAGA
PAKPGAPSRP TPRPELVGKP VPRRPAGTGV PQRQGGPSRP GAPTRQGRPG MPPRSGNTLE
LVGKPIRRDG STTGSGRPGA PTRPGAPGRP GMPAGMRKPV APGELMQLQK PVGRPAAPAP
RRPDAPTKAG AGAGTATPPV ARPNSPSAPR RPSFRPGGPG GQRRPGRPDW DDSARLDALR
SRSPQKQRQK VHIIGENDDS LAAQTGGFAG EQENMVLSAS LARPAKPKSQ QRTAPKPVAA
MRKRKKETAR QRQRRRAMEL RAAREAKQVR PEMIVVPEDN LTVQELADML SVESSEIIKS
LFFKGIIATV TQTLDMPTIE AVADEFGVPV LQDDVEEAAK KTVEMIEEAD KAHLIRRPPV
VTVMGHVDHG KTSLLDAIRQ ARVAAGEAGG ITQHIGAYQV EIEHNNEQRK LTFLDTPGHE
AFTAMRARGT KVTDVAVLVV AADDGVRPQT LEAISHARAA EVPIVVAINK IDKEGSSPER
VKQELSEQNL LAEDWGGDVV MVPVSAIKGE NIDKLLEMLL LVTEVEDLQA NPDRLARGTV
IEAHLDKAKG PVATLLVQNG TLKTGDVLAA GPVLGKVRAM VDDNRQRLKQ AGPSFAVEAL
GFSEVPTAGD EFEVYPDEKS ARAVVGDRAS DARATRLAQQ MASRRVSLTA MSGQANDGEL
KELNLILKAD VQGSVEAILG SLEQLPKDEV QVRVLLSAPG EITETDVDLA AASGAVIVGF
NTSMASGAKK AADATGVDVR DYDVIYKLLE DIQMAMEGLL EPELVEEALG EAEVRAVFTI
GKSAVAGCYV TTGKLHRNCR VRVHRGKQVV YEGDLDSLRR NKDDVKEVAT GFECGVGTDR
FANWEEGDRI EAFKMVTQRR KLTT
