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IF2_TRIEI
ID   IF2_TRIEI               Reviewed;        1059 AA.
AC   Q10XM3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Tery_3976;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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; CP000393; ABG53001.1; -; Genomic_DNA.
DR   RefSeq; WP_011613331.1; NC_008312.1.
DR   AlphaFoldDB; Q10XM3; -.
DR   SMR; Q10XM3; -.
DR   STRING; 203124.Tery_3976; -.
DR   EnsemblBacteria; ABG53001; ABG53001; Tery_3976.
DR   KEGG; ter:Tery_3976; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_7_0_3; -.
DR   OMA; NIAVKSH; -.
DR   OrthoDB; 347113at2; -.
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..1059
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008369"
FT   DOMAIN          556..733
FT                   /note="tr-type G"
FT   REGION          55..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..572
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          590..594
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          615..618
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          669..672
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          705..707
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        102..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         565..572
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         615..619
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         669..672
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1059 AA;  116624 MW;  1649D4D691A7C675 CRC64;
     MNNGKVRIYE LSKELNLENK DILAVCQRLN ISVKSHSSTI TESEAELIRT TAENLPHSPS
     LSAAPEKSNS QNQDSGIGYN EQKKQQILEV RKPKPLLEKS QQKNHSKINN NLVTTPPNTS
     VLNNQVERVG ISRPNSSLKS ETLKDNSEVG DNSLVQHPNR PLNKDNTVKE NYVPQKTDSN
     EKSKVEVPKL VAPPARPAPP SLNRNLRNTG VNKPNQKNKK PKQEGKKRKD KEEKPFEKPA
     IVSKKENKDT SIEKPTIASK KENKDTFQNR ESVKTSASDT SSQLKPKHRE KPTVKLKQEQ
     KPQLAPKPKL TTPLKEESTD VNLGLDLEGK EPEDNVAETV SYDLEKPRRK TIAPSKPTLT
     KDKKVSKWEE EEEDTSEVIQ KNAKSSAKNK RLRLKPLLED EDEELAELLN KPAPVTMSLS
     LARPAKPKSF TEKNKPQPGS NISNLKKKSS QSHESVQSES NEQTQSAELK PVEKLVISAS
     MTVQELALAL AIPETEIIRR LFMKGIAVNI TESLDIPTIE MVVKEEGIPI EVPEEQSAAK
     KTTEILEETD LASLQRRPPV VTIMGHVDHG KTSLLDSIRA TKVAAGEAGG ITQHIGAYHV
     DVEHEGQMQQ VVFLDTPGHE AFTAMRARGA RVTDVAVLVV AADDGVQPQT IEAISHAKAA
     EVPLIVAINK IDKEEANPDR VKQELMEHGL VPEEWGGDAI MVPVSAIQKQ NLDTLLEMIL
     LVSEVEDLQA NPERLAKGTV IEANLDKARG PVATLLVQNG TLKVGDIIVA GSVYGKVRAM
     IDDRGYRVDK ASPSFAVEVL GLRDVPQAGD EFKVFKNEKE ASAITTERAD AKRESRIMRR
     TSLGAVSVRA QEGELKELNL ILKGDVQGSI EAIVAALRQL PQKEVQLRLL LSGAGEVTET
     DIDLAAASEA VIIGFNTTMA SGARQAADAA GVDVREYNVI YKLLDDIQGA MEGLLDPELI
     EEPLGQVEVR AVFTINRGAV AGCYVLSGKV VRNCKVRVRR NGEIVYQGIL DSLRRMKDDV
     KEVNAGYECG VSFDNFNNWS EGDIIEAYQM VTKRRKLST
 
 
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