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Database: UniProt/SWISS-PROT
Entry: SYFA_CARHZ
LinkDB: SYFA_CARHZ
Original site: SYFA_CARHZ 
ID   SYFA_CARHZ              Reviewed;         340 AA.
AC   Q3ABT4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   14-MAY-2014, entry version 56.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE            Short=PheRS;
GN   Name=pheS; OrderedLocusNames=CHY_1571;
OS   Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z-2901 / DSM 6008;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T.,
RA   Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB15132.1; -; Genomic_DNA.
DR   RefSeq; YP_360400.1; NC_007503.1.
DR   ProteinModelPortal; Q3ABT4; -.
DR   SMR; Q3ABT4; 78-340.
DR   STRING; 246194.CHY_1571; -.
DR   EnsemblBacteria; ABB15132; ABB15132; CHY_1571.
DR   GeneID; 3727234; -.
DR   KEGG; chy:CHY_1571; -.
DR   PATRIC; 21276267; VBICarHyd26463_1505.
DR   eggNOG; COG0016; -.
DR   HOGENOM; HOG000242675; -.
DR   KO; K01889; -.
DR   OMA; IRYFFEN; -.
DR   OrthoDB; EOG6WX4QN; -.
DR   BioCyc; CHYD246194:GJCN-1570-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   CHAIN         1    340       Phenylalanine--tRNA ligase alpha subunit.
FT                                /FTId=PRO_0000231971.
FT   METAL       255    255       Magnesium (By similarity).
SQ   SEQUENCE   340 AA;  38640 MW;  AA764A26ABFF25CF CRC64;
     MNLHNEELWQ KYLGEVIRVS DLNELQTVKV KFLGKKGEVT LALKNLKNLP PELRPEAGHK
     INTVKKLIEE DLEKREQELL QKALEEKLSK EAIDVTLPGY SLKLGKLHPL TQVQHRIVEI
     FTSMGFSVAT GPEIEKDYYN FEALNLPKDH PARDMQDSFY ITEEVLLRTH TSPVQVRVME
     KYAPNLPIRI ISPGKVYRRD DDATHSPMFA QCEGLAVDKN IRFSDLKGVL LTFIKELFGP
     KTKMRLRPSY FPFTEPSAEV DISCVICGGI GCKVCKGSGW LEILGSGMVH PRVLEMAGYD
     SSVVTGFAFG MGLERIAMLL YGIDDLRLFY DNDIRFLQMF
//
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