(data stored in ACNUC7421 zone)

HOGENOM: PROMH_1_PE1001

ID   PROMH_1_PE1001                       STANDARD;      PRT;   327 AA.
AC   PROMH_1_PE1001; B4ETL0;
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   (PROMH_1.PE1001).
GN   Name=pheS; OrderedLocusNames=PMI1038;
OS   PROTEUS MIRABILIS HI4320.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PROMH_1.PE1001.
CC       Proteus mirabilis HI4320 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:SYFA_PROMH
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; B4ETL0; -.
DR   EMBL; AM942759; CAR42262.1; -; Genomic_DNA.
DR   RefSeq; YP_002150788.1; NC_010554.1.
DR   STRING; B4ETL0; -.
DR   GeneID; 6800515; -.
DR   GenomeReviews; AM942759_GR; PMI1038.
DR   OMA; FRASYFP; -.
DR   ProtClustDB; PRK00488; -.
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; PROMH_1.PE1001; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
SQ   SEQUENCE   327 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPHLAELVAQ AKAAIEEAQD VAALDSVRVE YLGKKGHLTL QMSTLRDLPA EERPAAGAVI
     NQAKQEVQQA LNARKEQMES ALLNERLAAE KIDVSLPGRR IENGGLHPVT RTIERIETFF
     GELGFSVESG PEIEDDYHNF DALNIPAHHP ARADHDTFWF DAKRLLRTQT SGVQIRTMQN
     KQPPIRIIAP GRVYRNDYDQ THTPMFHQVE GLIVDKDISF TNLKGTLHDF LKNFFEEDME
     IRFRPSYFPF TEPSAEVDVM GKNGKWLEVL GCGMVHPNVL RNVGIDPEVY SGFAFGMGME
     RLTMLRYGVT DLRSFFENDL RFLKQFK
//

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