(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_1_PE1312

ID   ACAM1_1_PE1312                       STANDARD;      PRT;   330 AA.
AC   ACAM1_1_PE1312; B0C6I2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Phenylalanyl-tRNA synthetase alpha chain; EC=6.1.1
DE   20;AltName: Full=Phenylalanine--tRNA ligase alpha chain; Short=PheRS;
DE   (ACAM1_1.PE1312).
GN   Name=pheS; OrderedLocusNames=AM1_1373;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE1312.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:SYFA_ACAM1
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 chains (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 chain type 1 subfamily.
CC   -!- GENE_FAMILY: HOG000242675 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0C6I2; -.
DR   EMBL; CP000828; ABW26403.1; -; Genomic_DNA.
DR   RefSeq; YP_001515717.1; NC_009925.1.
DR   ProteinModelPortal; B0C6I2; -.
DR   SMR; B0C6I2; 86-330.
DR   STRING; B0C6I2; -.
DR   GeneID; 5680193; -.
DR   GenomeReviews; CP000828_GR; AM1_1373.
DR   KEGG; amr:AM1_1373; -.
DR   OMA; FRASYFP; -.
DR   ProtClustDB; PRK00488; -.
DR   BioCyc; AMAR329726:AM1_1373-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
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_synth_II_N.
DR   InterPro; IPR022911; Phe_tRNA_synth_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.
DR   HOGENOMDNA; ACAM1_1.PE1312; -.
KW   phenylalanyl-tRNA synthetase subunit alpha;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
SQ   SEQUENCE   330 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTSDLETQLQ QLQTEAVAAI TSADTLDALE TLRVSYLGKK GQLSQILKGM GKLDASERPK
     IGGLANQVKE ALQQGLEQKK SDLNQAAIAA QLAAETLDVT MPGTYIPQGH IHPLNSTIDK
     ALDIFVGLGY TIAQGPEMET DYYNFEALNT PPDHPARDMQ DTFYLPDGNL LRTHTSAVQI
     HYMEDHEPPI RIAAPGRCYR RDTEDATHAA VFHQIEILAV DKGLTFTDLK GTIKVFIEQM
     FGDVPIRFRA SYFPFTEPSA EVDVQWKGRW LEVLGCGMVD PNVLKNVGYD PEVYTGFAAG
     FGVERFAMVL HQIDDIRRLY TSDLRFLRQF
//

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