ID E1VCP7_HALED Unreviewed; 339 AA.
AC E1VCP7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 01-MAY-2013, entry version 17.
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=HELO_2518;
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB
OS 2198 / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain: DSM 2581;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.-.P., Pfeiffer F.,
RA Oesterhelt D., Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the Industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 0:0-0(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F.,
RA Oesterhelt D., Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
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; FN869568; CBV42402.1; -; Genomic_DNA.
DR RefSeq; YP_003897587.1; NC_014532.1.
DR EnsemblBacteria; CBV42402; CBV42402; HELO_2518.
DR GeneID; 9748430; -.
DR KEGG; hel:HELO_2518; -.
DR PATRIC; 42354392; VBIHalElo161731_1628.
DR HOGENOM; HOG000242675; -.
DR KO; K01889; -.
DR BioCyc; HELO768066:GJEE-1568-MONOMER; -.
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 253 253 Magnesium (By similarity).
SQ SEQUENCE 339 AA; 37876 MW; 2366EF6711D6DD52 CRC64;
MDHLPTLVAE ARDAIQAAES MAALDELRVR YLGKKGEITA LLKGLGQLPA EERPAAGERI
NQAKQALSAD LEERKQALEK ADLEARLAAE TLDVTLPGRG QPSGGLHPVT RTLERIEGLF
THVGFDVAVG PEIEDDYHNF EALNIPAHHP ARGMADTFYF DATRLLRTHT SPVQVRTMKS
TEPPIRIVCP GRVYRSDSDL THTPMFHQVE GLLVDEDVRF SDLKGTIQDF LHAFFERDDL
AVRFRPSYFP FTEPSAEVDI QCVMCDGAGC RVCSHSGWLE VMGCGMVHPE VFRHSGIDSE
RYTGFAFGMG AERLAMLRYG VNDLRLFFDN DLRFLQQFA
//
