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IF2_MICAN
ID   IF2_MICAN               Reviewed;        1010 AA.
AC   B0JU67;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MAE_14330;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(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; AP009552; BAG01255.1; -; Genomic_DNA.
DR   RefSeq; WP_012264842.1; NC_010296.1.
DR   AlphaFoldDB; B0JU67; -.
DR   SMR; B0JU67; -.
DR   STRING; 449447.MAE_14330; -.
DR   PaxDb; B0JU67; -.
DR   EnsemblBacteria; BAG01255; BAG01255; MAE_14330.
DR   KEGG; mar:MAE_14330; -.
DR   PATRIC; fig|449447.4.peg.1314; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3170; Bacteria.
DR   HOGENOM; CLU_006301_5_1_3; -.
DR   OMA; NIAVKSH; -.
DR   OrthoDB; 347113at2; -.
DR   BioCyc; MAER449447:MAE_RS06305-MON; -.
DR   Proteomes; UP000001510; 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; Reference proteome.
FT   CHAIN           1..1010
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000075608"
FT   DOMAIN          502..675
FT                   /note="tr-type G"
FT   REGION          54..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..518
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          536..540
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          561..564
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          615..618
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          651..653
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        56..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..177
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         511..518
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         561..565
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         615..618
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1010 AA;  109510 MW;  A886B7BEDB268859 CRC64;
     MSNTKVRIYD LSKELNLDNK DILDICDQLN IEYKSHSSTI SEEDAQRIKA IAAKGLASST
     SKNSTGQRES ASPAEEKKQK ILALHKHNRP ETGEEGESYP GQAGSSAKPT LISPPRPPVK
     PLVAPPGRDE AAEKTPPTAA EMLSHSPSVK ETPTETPLVP EAAPTLIAPP NRPSLTPKPR
     PETASGRPEP RSKNAPGSND RPRGEKRERG ESENAPSPER RVGLAKPEKP TLNRKPDGKS
     PKLAEPAREV RETVELKRPV RPGLPAKISA TSEEETDTTK KSGVDGTEID TDTGLLGADG
     PKKLKRPTMP PRMAKKSTWE EEEEEEKKAA KTAKTAGKNK RRTQALFEDD DDLESELSGL
     INTPSFTLST ARPPKPPTAK AAPPGTPTAV KVKRPSKPTA HTGSPKSERQ EPQEEKRPES
     IVVTGSLTVR DLSELMKVPE TEIIRTLFFK GMAVNITQTL DVDTIEMIAR DFEIAVETPS
     TQSAAIKTTE MIDVSDWESL QRRPPVVTIM GHVDHGKTTL LDSIRKTKVA QGEAGGITQH
     IGAYHVDVEH NGKPEQIVFL DTPGHEAFTA MRARGARVTD IAVLVVAADD GVQPQTKEAI
     SHARAAEVPI VVAINKVDKP SANPDRIKQE LTEQGLVAED WGGETIMVPV SALRGENLDN
     LLEMILLVAE VEELVANPDR LAKGTVIEAN LDRTKGPVAT LLVQNGTLRV GDSIVAGSVF
     GKIRAMIDDR GQKVEAATPS FAVEILGLSD VPAAGDEFDV YESEKEARSI ADQRAIERRN
     TRLQQALSSR RVSLSTLSIQ AQEGQLKELN LILKADVQGS VEAILGALKQ LPQNEVQIRV
     LLASPGEITE TDVDLAAASG AVVVGFNTTL ASGARASADR EGVDIRDYNI IYKLLDDIQG
     AMEGLLDPEE VEEHLGFAEV RAVFTVGRGA VAGCYVQSGK LVRNRFLRVR RGKEIVYQGV
     LDSLKRMKED AREVATGFEC GVGVSKFNDW KEGDIIEAYE MVMKRRTLSS
 
 
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