GenomeNet

Database: UniProt/TrEMBL
Entry: G8RQ70_MYCRN
LinkDB: G8RQ70_MYCRN
Original site: G8RQ70_MYCRN 
ID   G8RQ70_MYCRN            Unreviewed;       347 AA.
AC   G8RQ70;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   19-FEB-2014, entry version 11.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
GN   Name=pheS; OrderedLocusNames=MycrhN_4657;
OS   Mycobacterium rhodesiae (strain NBB3).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=710685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) 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: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP003169; AEV75143.1; -; Genomic_DNA.
DR   RefSeq; YP_005002358.1; NC_016604.1.
DR   EnsemblBacteria; AEV75143; AEV75143; MycrhN_4657.
DR   GeneID; 11642013; -.
DR   KEGG; mrh:MycrhN_4657; -.
DR   KO; K01889; -.
DR   BioCyc; MRHO710685:GI37-4650-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR   InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   METAL       265    265       Magnesium (By similarity).
SQ   SEQUENCE   347 AA;  38195 MW;  6D526941CB9A4142 CRC64;
     MAEQPVELSE EALTNAVSAA RRAFDAAGDL DALARAKTEQ LGDRSPIALA RQALGSLPKT
     DRADAGKRVN VARTEAQQAY DERLAALRAE RDAAVLIAER IDVTLPSTRQ PLGARHPITI
     LAEHVADTFV AMGWELAEGP EVETEQFNFD ALNFPPDHPA RSEQDTFYVA PEGSRQVLRT
     HTSPVQIRAL LERELPVYII SIGRTFRTDE LDSTHTPVFH QVEGLAVDKG LTMAHLRGTL
     DAFARSEFGP EGRTRFRPHF FPFTEPSAEV DIWFANKKGG PGWVEWGGCG MVNPNVLRAC
     GIDPEVYSGF AFGMGLERTL QFRNGIPDMR DMVEGDVRFS LPFGVGV
//
DBGET integrated database retrieval system