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 01-MAY-2013, entry version 52.
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; LTHTPMF; -.
DR BioCyc; CHYD246194:GJCN-1570-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 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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