ID G8RQ70_MYCRN Unreviewed; 347 AA.
AC G8RQ70;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 03-APR-2013, entry version 8.
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.
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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 GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA: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; tRNA_binding_arm; 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
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