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 27-MAR-2024, entry version 106.
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; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RX PubMed=25831533; DOI=10.1073/pnas.1422332112;
RA Walworth N., Pfreundt U., Nelson W.C., Mincer T., Heidelberg J.F., Fu F.,
RA Waterbury J.B., Glavina del Rio T., Goodwin L., Kyrpides N.C., Land M.L.,
RA Woyke T., Hutchins D.A., Hess W.R., Webb E.A.;
RT "Trichodesmium genome maintains abundant, widespread noncoding DNA in situ,
RT despite oligotrophic lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4251-4256(2015).
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 AlphaFoldDB; Q10XM3; -.
DR SMR; Q10XM3; -.
DR STRING; 203124.Tery_3976; -.
DR KEGG; ter:Tery_3976; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OrthoDB; 9811804at2; -.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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
//
