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Chlamydia pneumoniae Search Results

Record: 1 of 1  
MiniMap IGR395 IGR399 IGR398 IGR396 IGR400 IGR397 CPn0498 CPn0499 aspC, - CPn0495 hrcA, - CPn0501 proS, - CPn0500 dnaK, - CPn0503 vacB, - CPn0504 CPn0498 CPn0499 aspC, - CPn0495 hrcA, - CPn0501 proS, - CPn0500 dnaK, - CPn0503 vacB, - CPn0504 CPn0498 CPn0499 CPn0497 CPn0497 hrcA, - CPn0501 proS, - CPn0500 dnaK, - CPn0503 vacB, - CPn0504 grpE, - CPn0502 CPn0496 grpE, - CPn0502 CPn0496 aspC, - CPn0495
* Calculated from Protein Sequence

Gene ID: CPn0500

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
proS  

Definition:
prolyl-tRNA synthetase

Gene Start:
580659

Gene Stop:
582365

Gene Length:
1707

Molecular Weight*:
63798

pI*:
5.10

Net Charge*:
-18.28

EC:
6.1.1.15  

Functional Class:
translation; tRNA aminoacylation  

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

Comment:
Prolyl-tRNA synthetase, by similarity, is a homodimer and appears to be cytoplasmically located.:
Through similarity, prolyl-tRNA synthetase belongs to class-II aminoacyl-tRNA synthetases.
Reaction: ATP + l-proline + tRNA(pro) = AMP + pyrophosphate + l-prolyl-tRNA(pro).

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
Cpn0500 is orthologously related to CT393: residues 1-567 of CPn0500 are 71% similar to residues 1-567 of CT393, a predicted prolyl-tRNA synthetase from C. trachomatis.
CPn0500 is also similar to TP0160.

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


ProDom Summary:  Protein Domain Search


Paralogs:  Local Blast Search
No paralogs in C. pneumoniae.

Pfam Summary:  Pfam Search
Residues 38 to 194 (E-value = 4.4e-49) place CPn0500 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 = 2.2e-13) place CPn0500 in the YbaK family which is described as YbaK / prolyl-tRNA synthetases associated domain (PF04073)
Residues 475 to 566 (E-value = 1.9e-21) place CPn0500 in the HGTP_anticodon family which is described as Anticodon binding domain (PF03129)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
497  
568

PDB Hit:


Gene Protein Sequence:
MKTSQLFYKTSKNANKSAAVLSNELLEKAGYLFKVSKGVYTYTPLLWRVV
SKMMNIIREELNAIGGQELLLPLLHNAELWQHTGRWEAFTSEGLLYTLKD
REGKSHCLAPTHEEVICSFVAQWLSSKRQLPLHLYQIATKFRDEIRPRFG
LIRSRELLMEDSYTFSDSPEQMNEQYEKLRSAYSKIFDRLGLAYVIVTAD
GGKIGKGKSEEFQVLCSLGEDTICVSGSYGANIEAAVSIPPQHAYDREFL
PVEEVATPGITTIEALANFFSIPLHKILKTLVVKLSYSNEEKFIAIGMRG
DRQVNLVKVASKLNADDIALASDEEIERVLGTEKGFIGPLNCPIDFFADE
TTSPMTNFVCAGNAKDKHYVNVNWDRDLLPPQYGDFLLAEEGDTCPENPG
HPYRIYQGIEVAHIFNLGTRYTDSFEVNFQDEHGQTQQCWMGTYGIGVGR
TLAACVEQLADDRGIVWPKALAPFSITIAFNGGDTVSQELAETIYHELQS
QGYEPLLDDRDERLGFKLKDSDLIGIPYKLILGKSYQSSGIFEIESRSGE
KYTVSPEAFPTWCQNHLA$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAACGTCTCAACTCTTTTATAAGACTTCAAAAAATGCAAATAAAAG
CGCTGCTGTGCTCTCAAACGAGCTCCTAGAAAAGGCAGGATACCTATTTA
AAGTAAGTAAAGGAGTCTATACCTATACACCCCTGTTATGGCGCGTGGTC
TCCAAGATGATGAACATCATTAGAGAGGAACTTAATGCGATTGGAGGTCA
AGAACTTCTACTCCCACTTCTCCACAATGCTGAACTTTGGCAACATACAG
GGAGATGGGAGGCATTTACTTCGGAAGGACTGCTCTACACTCTCAAAGAC
CGCGAAGGAAAATCTCATTGCCTAGCTCCTACACATGAAGAGGTCATCTG
CTCTTTTGTTGCACAATGGCTCTCCTCAAAAAGACAACTTCCTCTCCACC
TTTACCAAATTGCTACAAAATTCCGAGACGAGATTCGCCCTCGATTCGGT
CTCATTCGCTCTCGAGAGCTCCTTATGGAAGACAGCTATACCTTCTCAGA
CTCTCCCGAACAAATGAACGAGCAATATGAAAAACTCCGCTCTGCGTATA
GTAAGATCTTTGATCGTCTCGGTCTTGCCTATGTCATCGTTACAGCTGAT
GGAGGGAAAATCGGCAAAGGAAAGTCTGAGGAATTTCAGGTCCTTTGCTC
TCTAGGCGAGGACACGATCTGCGTCAGCGGTTCCTATGGAGCTAATATTG
AGGCTGCTGTCTCCATTCCTCCACAGCATGCCTACGATCGCGAGTTTCTT
CCCGTCGAAGAAGTGGCCACCCCTGGGATTACAACAATAGAAGCTCTAGC
AAACTTCTTCTCTATCCCCTTACATAAAATTTTAAAAACCCTTGTCGTAA
AACTCTCCTACTCAAATGAAGAAAAATTCATTGCCATTGGAATGAGAGGA
GATCGGCAAGTCAACCTAGTGAAGGTCGCTTCCAAACTGAATGCCGATGA
TATTGCTCTAGCTTCTGATGAAGAAATCGAACGCGTTCTAGGCACAGAAA
AAGGATTCATCGGTCCCCTAAACTGTCCCATAGACTTTTTCGCAGACGAA
ACAACGTCCCCAATGACGAACTTTGTTTGTGCGGGCAATGCTAAAGATAA
GCACTACGTAAATGTAAACTGGGATCGCGACCTCCTCCCCCCCCAATACG
GTGACTTTCTACTCGCTGAAGAGGGAGACACATGTCCTGAAAATCCTGGC
CATCCTTACCGCATTTATCAAGGCATAGAAGTTGCTCATATTTTCAATCT
CGGGACACGCTATACCGATAGTTTTGAGGTAAACTTCCAAGATGAACACG
GGCAAACCCAGCAGTGCTGGATGGGGACCTACGGCATTGGAGTCGGAAGA
ACATTAGCCGCTTGTGTAGAACAGCTTGCCGACGACCGTGGTATTGTTTG
GCCAAAAGCACTCGCTCCCTTCTCTATCACTATCGCCTTTAACGGAGGAG
ACACTGTATCTCAAGAGCTTGCGGAAACTATTTATCATGAGCTACAAAGT
CAAGGCTATGAGCCCCTTCTTGATGATCGAGATGAAAGACTCGGATTTAA
ACTTAAAGACAGTGACCTTATCGGCATTCCTTATAAGCTTATTTTAGGAA
AGTCCTACCAATCTTCGGGAATATTCGAAATTGAATCCCGATCTGGAGAA
AAGTATACAGTCTCCCCGGAGGCCTTCCCTACTTGGTGTCAGAATCACTT
AGCCTAG


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