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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap tRNA-Val-2 tRNA-Ser-4 IGR699 IGR692 IGR700 IGR697 IGR695 IGR696 IGR701 IGR691 IGR693 IGR698 IGR690 IGR694 CT832 murB, - CT831 CT839 CT838 rl35, - CT834 rl20, - CT835 yggH, - CT829 infC, - CT833 ytgB, - CT830 pheS, - CT836 CT837 CT832 murB, - CT831 CT839 CT838 rl35, - CT834 rl20, - CT835 yggH, - CT829 infC, - CT833 ytgB, - CT830 pheS, - CT836 CT837 CT832 murB, - CT831 CT839 CT838 rl20, - CT835 yggH, - CT829 infC, - CT833 ytgB, - CT830 pheS, - CT836 CT837 rl35, - CT834
* Calculated from Protein Sequence

Gene ID: CT836

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
pheS  

Definition:
phenylalanyl-tRNA synthetase alpha chain

Gene Start:
983301

Gene Stop:
984326

Gene Length:
1026

Molecular Weight*:
38674

pI*:
6.16

Net Charge*:
-5.75

EC:
6.1.1.20  

Functional Class:
translation; aminoacyl-tRNA synthetases  

Pathway: pathway table
Amino Acid Metabolism; Phenylalanine, tyrosine and tryptophan biosynthesis
Metabolism of Macromolecules; Aminoacyl-tRNA biosynthesis

Secondary Evidence:
Kast,P., Wehrli,C. and Hennecke,H. 1991. Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases. FEBS Lett. 293(1-2): 160-163. Medline: 92070551.

Brakhage,A.A., Wozny,M. and Putzer,H. 1990. Structure and nucleotide sequence of the Bacillus subtilis phenylalanyl-tRNA synthetase genes. Biochimie 72(10): 725-734. Medline: 91175935.

Fayat,G., Mayaux,J.F., Sacerdot,C., Fromant,M., Springer,M., Grunberg-Manago,M. and Blanquet,S. 1983. Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20. J. Mol. Biol. 171(3): 239-261. Medline: 84090239.

Comment:
The phenylalanyl-tRNA synthetase is typically a heteroterameric molecule consisting of two alpha and two beta chains. For the beta chain, see CT475.

Phenylalanyl-tRNA synthetase alpha chain is likely to be a
cytoplasmically located tetramer of two alpha and two beta chains
belonging to class-II aminoacyl-tRNA synthetases.
Reaction: ATP + l-phenylalanine + tRNA(Phe) = AMP + pyrophosphate + l-phenylalanyl-tRNA(Phe).


Blast Summary:  PSI-Blast Search
Numerous hits in BLAST to phe-tRNA synthetase alpha chain sequences,
e.g. residues 3-341 are 40% similar to SYFA_BACSU. CT836 is similar to TP0973 in T.pallidum and to MG194 in M.genitalium, both predicted phe-tRNA synthetases.

CT836 is orthologously related to CPn0993: residues 1-342 of CT836 are 69% similar to residues 1-339 of CPn0993, a predicted phenylalanyl-tRNA synthetase alpha chain from C. pneumoniae. This protein is also similar to PG1545, a predicted phenylalanyl-tRNA synthetase from Porphyromonas gingivalis.

COGS Summary:  COGS Search
BeTs to 17 clades of COG0016
COG name: Phenylalanyl-tRNA synthetase alpha subunit
Functional Class:  J
The phylogenetic pattern of COG0016 is amtkYqvcebrhujgpolinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 312-332 are matched to block PR00628B, concerned with insulin
receptor signatures, e.g. IRS1_HUMAN.

ProDom Summary:  Protein Domain Search
Residues 137-298 are 47% similar to a phe-tRNA synthetase alpha chain domain
as observed in SYFA_BACSU. Residues 27-74 and 300-341 also correspond to defined
domains for phe-tRNA synthetase alpha sequences, as seen in SYFA_ECOLI, SYFA_HAEIN.

Paralogs:  Local Blast Search
There is no evidence of paralogs in C.trachomatis.

Pfam Summary:  Pfam Search
Residues 19 to 91 (E-value = 2.8e-25) place CT836 in the Phe_tRNA-synt_N family which is described as Aminoacyl tRNA synthetase class II, N-terminal domain (PF02912)
Residues 112 to 328 (E-value = 8.2e-128) place CT836 in the tRNA-synt_2d family which is described as tRNA synthetases class II core domain (F) (PF01409)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
57  
123

PDB Hit:
gi|2781285|pdb|1PYS|A Chain A, Phenylalanyl-Trna Synthetase From Thermus Thermophilus Phenylalanyl-Trna Synthetase, Class Ii Aminoacyl-Trna Synthetase, Thermus Thermophilus, Rbd Domain, Sh3 Domain, Helix-Turn-Helix Motif Mol_id: 1; Molecule: Phenylalanyl-

Gene Protein Sequence:
MTIQEELEAVKQQFSCDVSLAHSSKDLFDVKVKYLGKKGIFRGFADQLRK
YPIEQKATVGASINACKQYVEEVLLERGKAVLAKEEAEEFLKEKIDISLP
GSEEAALGGKHVIKKVLDDVVDIFVRFGFCVREAPNIESEKNNFSLLNFE
EDHPARQMQDTFYLDPTTVLRTHTSNVQSRELARNKPPVRIVAPGECFRN
EDVSARSHVIFHQVEAFCVDKDISFSDLTSMLAGFYHIFFGRKVELRFRH
SYFPFVEPGIEVDISCECHGAGCSLCKHAGWLEVAGAGMIHPNVLRKASI
DPEEYSGYALGMGIERLAMLKYGISDIRLFSENDLRFLRQFS

Gene Nucleotide Sequence:  Sequence Viewer
ATGACAATTCAAGAGGAACTTGAGGCTGTTAAACAGCAGTTTAGTTGTGA
TGTAAGCCTTGCGCATTCTTCTAAAGATCTTTTCGATGTGAAAGTAAAAT
ACCTGGGAAAGAAGGGAATCTTTCGAGGTTTTGCTGATCAGTTGAGGAAG
TACCCTATAGAGCAGAAAGCGACTGTTGGCGCTTCCATTAACGCTTGTAA
GCAATACGTGGAGGAAGTTTTACTCGAGAGAGGCAAGGCCGTTTTGGCTA
AAGAAGAAGCAGAAGAGTTCCTTAAGGAGAAGATAGATATCAGTTTACCT
GGTAGCGAAGAAGCTGCTCTTGGTGGTAAGCATGTTATCAAGAAAGTCCT
TGATGATGTTGTAGATATCTTTGTTCGCTTTGGATTTTGTGTTCGGGAAG
CTCCTAATATCGAAAGTGAAAAAAACAATTTTTCTCTTCTTAATTTCGAA
GAAGATCATCCTGCTCGACAGATGCAGGATACTTTCTATTTGGATCCCAC
CACGGTCTTGCGTACGCACACGTCGAATGTGCAGTCTCGGGAGTTAGCGA
GAAACAAACCTCCTGTTAGAATTGTCGCTCCAGGAGAGTGTTTCCGTAAT
GAAGACGTTTCTGCGCGTTCGCATGTGATTTTTCACCAAGTAGAGGCTTT
CTGCGTAGATAAAGATATTTCTTTTTCAGACTTGACATCGATGTTGGCAG
GGTTTTACCATATCTTCTTTGGACGCAAAGTGGAGTTGCGGTTTAGACAC
AGCTATTTCCCTTTTGTCGAGCCAGGGATCGAGGTAGACATTTCTTGTGA
ATGTCATGGAGCCGGATGTTCTTTGTGTAAGCATGCTGGTTGGTTGGAAG
TTGCTGGAGCAGGAATGATTCATCCGAATGTCTTGCGTAAGGCAAGCATT
GATCCAGAAGAGTATTCTGGGTATGCCTTGGGGATGGGTATAGAGCGTCT
CGCGATGCTCAAGTACGGTATTTCCGATATTCGATTGTTTAGTGAGAACG
ATTTGCGGTTTTTACGGCAATTTTCT


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