ID IF2_PROMT Reviewed; 1183 AA. AC Q46J13; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 110. 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=PMN2A_1025; OS Prochlorococcus marinus (strain NATL2A). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=59920; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NATL2A; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000095; AAZ58515.1; -; Genomic_DNA. DR RefSeq; WP_011295370.1; NC_007335.2. DR AlphaFoldDB; Q46J13; -. DR SMR; Q46J13; -. DR STRING; 59920.PMN2A_1025; -. DR KEGG; pmn:PMN2A_1025; -. DR HOGENOM; CLU_006301_5_1_3; -. DR OrthoDB; 9811804at2; -. DR PhylomeDB; Q46J13; -. DR Proteomes; UP000002535; 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; 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; Reference proteome. FT CHAIN 1..1183 FT /note="Translation initiation factor IF-2" FT /id="PRO_0000228226" FT DOMAIN 675..847 FT /note="tr-type G" FT REGION 65..512 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 540..579 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 684..691 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 709..713 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 734..737 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 788..791 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 824..826 FT /note="G5" FT /evidence="ECO:0000250" FT COMPBIAS 65..80 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 81..100 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 101..145 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..278 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 321..368 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 426..450 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 484..512 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 556..570 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 684..691 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 734..738 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 788..791 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" SQ SEQUENCE 1183 AA; 128121 MW; 7ECFDD0DC206B4C0 CRC64; MTSSGKIRIY ELSKDLSLDN KDVLDAARKL AIAAKSHSSS ISSLEANQIK DFLKKSNTIN TTIKSSKNLD KQILSVKKNP VKTQKDQKTE PKKKNHDQTE LSQAKLNTLL KPSQTLIKSQ GSSQANNQKA LKNKFPAKQQ ITSPSKPNKP LPPNPRVEVK PIISKPLTQA ERAIPQSEQK KDGQFINQPK RSELAKKSIG QPKQINPQEP KRPLAPPSRP KIDIQDKKPL QPNNQKAKTR INQGEISPQK VGQGNIQKIK SQNKQNAPSR TPQPPTKGNT LELVGAPIRK EKPVNKPHTN EVRNKPVMPS RPGAPKPPTA ANRQGLSNRP GSNNRIGGTG RPGSPNRQGP NRGGVANRTT QGQNRPGANN RAGAPVRSGS PNRGGMQNRP GVPTRSLGGP NRSNNRPGVP SGMRKPVAPS ELMQLQKPQA RPNAPQRKTD SPTSLRPKRE NSTGARPPVN RPTPAAPKKP AHRPGGTAAA PRRTGRPDWD DSAKLDALRN KSPQKQRQKV HIIGENDDAL TAERGGFAGE QQAVVLSASL ARPSKPKVGK RNNGKPLTAL KKRKKETTRQ RQRRRAMELR ASREAKLVRP EMIVVPEDNL TVQELADMLS VESSEIIKSL FFKGITATVT QSLDLATIET VAEEFGVPVL QDDVEEAAKK TVEMIEEGDL KYLIRRPPVV TVMGHVDHGK TSLLDAIRKA RVAAGEAGGI TQHIGAYQIE TEHDGSTKKL TFLDTPGHEA FTAMRARGTR VTDVAILVVA ADDGVRPQTL EAISHARAAK VPIVVAINKI DKEGSSPDRV KQELSEQDLL SEEWGGDVVM VPVSAIKGEN IDKLLEMVLL VTEVEDLQAN PDRLAKGTVI EAHLDKAKGP VATLLVQNGT LKSGDVVAAG PVLGKVRAMV DENGSRIKEA GPSCPVEALG FSEVPTAGDE FEVYPDEKAA RAVVGERATD ARAARLAQQM ASRRVSLSSM SGQASEGELK ELNIILKADV QGSLEAILGS LEQLPKDEVQ VRVLLSAPGE ITETDIDLAA ASGAVIVGFN TSMASGAKRA ADANGVDVRE YEVIYKLLED IQLAMEGLLE PEMIEEALGV AEVRAIFSIG KSAVAGCYVT NGKIQRNCRA RVKRGKQIVF EGDLDSLKRN KDDVKDVSTG FECGIGCDRF ANWEEGDQIE AFKLVTQRRK LNN //