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IF2_SYNP6
ID   IF2_SYNP6               Reviewed;        1030 AA.
AC   Q5N0A5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=syc2075_d;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
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; AP008231; BAD80265.1; -; Genomic_DNA.
DR   RefSeq; WP_011244385.1; NC_006576.1.
DR   AlphaFoldDB; Q5N0A5; -.
DR   SMR; Q5N0A5; -.
DR   STRING; 269084.syc2075_d; -.
DR   EnsemblBacteria; BAD80265; BAD80265; syc2075_d.
DR   KEGG; syc:syc2075_d; -.
DR   eggNOG; COG0532; Bacteria.
DR   OMA; NIAVKSH; -.
DR   Proteomes; UP000001175; 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.
FT   CHAIN           1..1030
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228253"
FT   DOMAIN          522..695
FT                   /note="tr-type G"
FT   REGION          56..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..538
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          556..560
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          581..584
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          635..638
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          671..673
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        183..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         531..538
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         581..585
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         635..638
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1030 AA;  110570 MW;  0AB450400867F9E5 CRC64;
     MNNGKVRIYE LSKELNLDNK DVLAVCDRLE IPYKSYSSTL SEEQVVQVRQ VLAGAAPSEP
     VAAASAADSP KAERKQEIVS VRRPTPQAAG GAKPEIVGRP TASEKPQAER PNIVAPPRRP
     AAANEPAKAP IKPARPEKSA EKPEIVTPRP PAPAASAEPA KSPSRPAPAA TPRPVAETKK
     PKPAAAELLR KPEIVRRSEA KPERTSEAPT PRPKIERRPE QTGPARPQLG QPVAGNGVSK
     PAKPVKPIEL VAPPSRPKVA ASASGVPAAA SRVLPNKPQK PTAPGGPELK QRPKPAAPAS
     GEDLAATVDV FQPVPPLELR RPTAPARPAR PRKGWEEEED ERAAANRKAG NKAAAKAKRR
     QLIQDDDDDD LLTAEQELAA ADALNLAMSL ARPSKPKVPQ AKPAVAVMPT KGRKPRRESA
     RERQHRRRME REQKPVRPEL ISLRSSMTVQ ELAQLMVVPE TDIIKSLFFK GIAATVTQSL
     DVATIEQVAE EFGILVEQET EESGARKTTQ MVEDADAESL QTLPPVVTAM GHVDHGKTTL
     LDAIRKTRVA AGEAGGITQH IGAYHVDVEH NGDQHQIVFL DTPGHEAFTA MRARGARVTD
     IAILVVAADD GVRPQTLEAI SHAKAAEVPL IVAINKCDKE EAQPDRVKQE LTEYGLVPEE
     WGGETVMVPV SAIKGENIDQ LLEMILLVTE VEELVANPDR AARGTVIEAH LDKARGPVAT
     LLVQNGTLRV GDVLVAGSVL GKVRAMVDDR GDRVEAATPS FAVEVLGLGD VPAAGDEFEV
     YSDEKSARAV ATSRADEQRQ SRLQQAMASR RVSLGTVSAQ AQEGELKELN LILKADVQGS
     VEAILGSLEQ LPQKQVQVRV LLAAPGEITE TDVDLAAASG AVIVGFNTTL ASGAKRAADE
     AGVDVRDYDI IYKLLEDIQA AMEGLLEPEL VEEPLGQVEV RAVFSIGRGA VAGCYVQSGK
     AIRNCNIRVR RGSNLVYTGT LDSLKRMKED VKEVNSGYEC GIGLDSFSAW QEGDIIETYR
     MVTKRRTLEV
 
 
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