ID I6DEJ8_SHIBO Unreviewed; 795 AA. AC I6DEJ8; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 03-OCT-2012, entry version 2. DE SubName: Full=Phenylalanyl-tRNA synthetase, beta subunit; DE EC=6.1.1.20; GN Name=pheT; ORFNames=SB96558_2311; OS Shigella boydii 965-58. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766138; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=965-58; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- COFACTOR: Binds 2 magnesium ions per tetramer (By similarity). CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Contains 1 B5 domain. CC -!- SIMILARITY: Contains 1 FDX-ACB domain. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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; AKNA01000053; EIQ30190.1; -; Genomic_DNA. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:EC. DR Gene3D; G3DSA:3.50.40.10; B3_4; 1. DR Gene3D; G3DSA:3.30.56.20; B5; 1. DR Gene3D; G3DSA:3.30.70.380; Fdx_AntiC_bd; 1. DR Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1. DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1; -. DR InterPro; IPR005146; B3/B4_tRNA-bd. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR016027; NA-bd_OB-fold-like. DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bac. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR005121; PheS_beta_Fdx_antiC-bd. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF03147; FDX-ACB; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SMART; SM00896; FDX-ACB; 1. DR SUPFAM; SSF56037; B3_4; 1. DR SUPFAM; SSF54991; Fdx_AntiC_bd; 1. DR SUPFAM; SSF50249; Nucleic_acid_OB; 1. DR SUPFAM; SSF46955; Putativ_DNA_bind; 1. DR TIGRFAMs; TIGR00472; pheT_bact; 1. DR PROSITE; PS51483; B5; 1. DR PROSITE; PS51447; FDX_ACB; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Protein biosynthesis; RNA-binding; KW tRNA-binding. SQ SEQUENCE 795 AA; 87308 MW; 41BE2F5672D92A69 CRC64; MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFHGVVVGEV VECAQHPNAD KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP GDFKIKAAKL RGEPSEGMLC SFSELGISDD HSGIIELPAD APIGTDIREY LKLDDNTIEI SVTPNRADCL GIIGVARDVA VLNQLPLVEP EIVPVGATID DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR CGIRSIDAVV DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH GLHTDASHRY ERGVDPALQH KAMERATRLL IDICGGEAGP VIDITSEATL PKRATITLRR SKLDRLIGHH IADEQVTDIL RRLGCEVTEG KDEWQAVAPS WRFDMEIEED LVEEVARVYG YNNIPDEPVQ ASLIMGTHRE ADLSLKRVKT LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLPSPISVE MSAMRLSLWT GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR YEEHWNLAKE TVDFYDLKGA LESVLDLTGK LNEVEFRAEA NPALHPGQSA AIYLKGERIG FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI SRFPANRRDI AVVVAENVPA ADILSECKKV GVNQVVGVNL FDVYRGKGVA EGYKSLAISL ILQDTSRTLE EEEIAATVAK CVEALKERFQ ASLRD //