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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR325 IGR326 IGR329 IGR328 IGR324 IGR327 IGR330 yprS, - CT392 grpE, - CT395 CT391 hrcA, - CT394 aspC, - CT390 CT389 proS, - CT393 dnaK, - CT396 vacB, - CT397 yprS, - CT392 grpE, - CT395 CT391 hrcA, - CT394 aspC, - CT390 CT389 proS, - CT393 dnaK, - CT396 vacB, - CT397 yprS, - CT392 grpE, - CT395 CT391 hrcA, - CT394 aspC, - CT390 CT389 proS, - CT393 dnaK, - CT396 vacB, - CT397
* Calculated from Protein Sequence

Gene ID: CT393

DNA Molecule Name:
1  

Genbank ID:
3328819

Gene Name:
proS  

Definition:
prolyl-tRNA synthetase

Gene Start:
448027

Gene Stop:
449769

Gene Length:
1743

Molecular Weight*:
65644

pI*:
5.55

Net Charge*:
-10.33

EC:
6.1.1.15  

Functional Class:
translation; aminoacyl-tRNA synthetases  

Pathway: pathway table
Amino Acid Metabolism; Arginine and proline metabolism
Metabolism of Macromolecules; Aminoacyl-tRNA biosynthesis

Primary Evidence:
Schmiel DH and Wyrick PB. 1994. Another putative heat-shock gene and aminoacyl-tRNA synthetase gene are located upstream from the grpE-like and dnaK-like genes in Chlamydia trachomatis. Gene 145: 57-63. Medline: 8045424.

Comment:
This protein is identical to GenBank accession AAC67990. The proximity of this coding sequence to the GrpE-like sequence represented in CT392 has been previously noted. See GenBank L25105.

From Prosite PDOC00363:

Aminoacyl-tRNA synthetases (EC 6.1.1.-) are a group of enzymes which activate amino acids and transfer them to specific tRNA molecules as the first step in protein biosynthesis. In prokaryotic organisms there are at least twenty different types of aminoacyl-tRNA synthetases, one for each different amino acid. In eukaryotes there are generally two aminoacyl-tRNA synthetases for each different amino acid: one cytosolic form and a mitochondrial form. While all these enzymes have a common function, they are widely diverse in terms of subunit size and of quaternary structure.

The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine are referred to as class-II synthetases and probably have a common folding pattern in their catalytic domain for the binding of ATP and amino acid which is different to the Rossmann fold observed for the class I synthetases.


Blast Summary:  PSI-Blast Search
CT393 is orthologously related to Cpn0500: residues 1-567 of CT393
are 71% similar to residues 1-567 of Cpn0500, a predicted prolyl-tRNA synthetase from C. pneumoniae.

Numerous hits in gapped BLAST to pro-tRNA synthetase sequences, e.g., residues 1-567 are 39% similar to SYP_ECOLI. CT393 is identical to the previously sequenced SYP_CHLTR (L25105). CT393 is similar to TP0160 of T.pallidum and to MG283 of M.genitalium, both predicted prolyl-tRNA synthetases; the similarity to the former is by far greatest.



COGS Summary:  COGS Search
BeTs to 17 clades of COG0442
COG name: Prolyl-tRNA synthetase
Functional Class:  J
The phylogenetic pattern of COG0442 is amtkYqvcebrhujgpolinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
None.

ProDom Summary:  Protein Domain Search
The identity to O84398_CHLTR dominates the results. Residues 1-23, 24-165, 176-242, 255-401, 407-551, 552-581 are regarded as domains and are identical to the prolyl tRNA synthetase domains of O84398_CHLTR. Other related sequences are O45869_CAEEL and SYT_ECOLI.


Paralogs:  Local Blast Search
CT393 is weakly similar to CT581, a threonyl-tRNA synthetase,
and very weakly similar to CT729, a seryl-tRNA synthetase:
residues 65-194 are approximately 26% identical to CT581 and 25% identical to CT729.

Pfam Summary:  Pfam Search
Residues 38 to 194 (E-value = 2.6e-49) place CT393 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T) (PF00587)
Residues 247 to 386 (E-value = 1.1e-05) place CT393 in the YbaK family which is described as YbaK / prolyl-tRNA synthetases associated domain (PF04073)
Residues 475 to 566 (E-value = 4e-20) place CT393 in the HGTP_anticodon family which is described as Anticodon binding domain (PF03129)

PDB Hit:
None.

Gene Protein Sequence:
MRMSLLFYRTSKNANKEASVLSYELLQKAGYLFKTSKGIYSYTPLFQRVI
LKMTEIIREELNAIGGQEVCLPLLQPAELWEKTGRWKAFLSEKLLYVLKD
RENKAMCLAPTHEEVVSEFVAQWLTGREQLPIHLYQIGTKFRDEIRPRFG
LMRAKEFLMEDSYTFSDSPEQMEEQYAKLRLAYQRIFDRLNLKYVIVAAD
GGKIGKGKSEEFHVLCSLGEDTICVSGSYGANVEAAQAIPPSYVYDSNLL
PVEEVATPNIRTIEDLEVFFNTPKHKILKTLVVKTCQKDSEKFFAICIRG
DRQINLTKVASFLQVDDCELASEEEILKHLHVEKGFIGPLYCPIPCYADE
TTRPMTNFICANNQKDVHCKHVNWGRDIPLPAFGDFLLAEAGDLCPQNGG
APYEIFQGVEVAHIFNLGTRYTESFSVGFQDKNGDKQLCWMGTYGIGVGR
TLAACIEQLADNKGLVWPLAVAPFSITILYNGGDTEGEATALQLYQSLNT
EGFEPLLDDRNERLGFKLKDSDLLGIPYKLIIGKSFQSTGLLEIESRSGE
KCNVSPENLLDWCSKNLPCHTRKIPPLREQN

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGAATGTCCCTCCTGTTTTACAGAACTTCCAAAAATGCAAATAAAGA
AGCCTCCGTTCTTTCCTACGAGCTTCTTCAGAAAGCAGGGTATCTTTTCA
AAACATCTAAAGGGATTTACTCATACACACCTCTCTTCCAACGAGTTATC
CTAAAAATGACCGAAATCATTCGTGAAGAACTCAATGCTATTGGAGGACA
AGAGGTCTGTCTCCCTCTCCTGCAACCAGCAGAACTATGGGAAAAAACCG
GTCGTTGGAAGGCCTTTTTATCGGAAAAATTACTCTATGTGCTTAAGGAT
AGAGAAAATAAGGCAATGTGTTTAGCCCCTACCCACGAAGAGGTTGTCTC
TGAATTCGTGGCTCAGTGGCTAACAGGACGAGAACAGCTCCCTATCCACC
TATACCAAATCGGAACCAAATTCCGAGATGAAATCCGACCTCGCTTTGGG
CTTATGCGTGCCAAAGAGTTCTTAATGGAAGATAGCTATACTTTTTCTGA
CTCTCCAGAACAAATGGAAGAACAGTATGCAAAGCTACGTCTAGCTTACC
AGCGCATCTTTGATCGATTAAATCTCAAATATGTAATTGTTGCTGCAGAT
GGAGGGAAAATTGGTAAGGGGAAATCTGAGGAATTCCATGTTCTCTGCTC
TTTAGGAGAAGACACGATCTGTGTGAGTGGGTCTTACGGAGCGAATGTAG
AAGCAGCACAAGCAATCCCTCCATCCTATGTTTACGATTCAAACCTTCTA
CCTGTAGAAGAAGTTGCGACTCCTAACATTCGAACAATTGAAGACTTAGA
AGTCTTTTTTAACACCCCTAAACATAAAATACTGAAAACTTTAGTTGTTA
AAACTTGCCAAAAAGACTCGGAGAAATTCTTTGCGATTTGTATCCGAGGG
GATCGTCAGATCAACTTAACCAAAGTTGCATCTTTCCTACAAGTTGATGA
CTGCGAGCTGGCTTCTGAGGAAGAGATCCTTAAGCATCTTCATGTTGAAA
AAGGATTTATCGGACCTCTATACTGTCCTATCCCCTGTTATGCAGACGAA
ACAACGCGCCCAATGACTAACTTCATCTGCGCAAACAACCAAAAAGACGT
GCACTGCAAGCATGTGAACTGGGGACGCGATATCCCTCTTCCAGCTTTCG
GAGACTTTCTTTTAGCAGAAGCTGGAGACCTTTGTCCTCAAAATGGAGGA
GCTCCCTATGAAATTTTCCAAGGCGTCGAAGTCGCTCATATCTTCAATCT
GGGAACCCGCTATACGGAGAGCTTCTCCGTAGGGTTCCAGGATAAAAATG
GAGATAAGCAGCTTTGCTGGATGGGGACATATGGTATTGGAGTAGGGAGA
ACCCTTGCTGCATGCATAGAACAGCTCGCTGATAACAAAGGACTGGTTTG
GCCTTTAGCTGTAGCTCCTTTCTCCATCACCATTCTCTATAATGGTGGTG
ATACGGAAGGAGAAGCCACCGCCTTACAACTTTATCAAAGCCTGAATACT
GAAGGCTTTGAGCCTCTACTAGATGATCGCAATGAACGCCTTGGGTTTAA
GTTAAAAGACAGCGATTTACTAGGTATCCCGTACAAATTGATCATTGGGA
AGTCTTTCCAAAGTACAGGCTTATTAGAAATCGAATCACGCTCAGGAGAA
AAATGTAATGTTTCTCCTGAAAACCTATTGGATTGGTGCTCTAAAAATCT
TCCTTGTCATACAAGAAAGATCCCTCCACTCCGAGAACAAAAC


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