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Mycoplasma genitalium Search Results

Record: 1 of 1  
MiniMap IGR60 IGR59 IGR57 IGR61 IGR64 IGR63 IGR62 IGR58 rpL11, - MG081 rpS12, - MG087 rpS7, - MG088 rpL1, - MG082 MG084 lgt, - MG086 oppD, - MG079 fus, - MG089 oppF, - MG080 rpL11, - MG081 rpS12, - MG087 rpS7, - MG088 rpL1, - MG082 MG084 lgt, - MG086 oppD, - MG079 fus, - MG089 oppF, - MG080 rpL11, - MG081 rpS12, - MG087 rpS7, - MG088 rpL1, - MG082 MG084 lgt, - MG086 oppD, - MG079 fus, - MG089 oppF, - MG080 pth, - MG083 ptsK,hprK, - MG085 pth, - MG083 ptsK,hprK, - MG085
* Calculated from Protein Sequence

Gene ID: MG083

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
pth  

Definition:
peptidyl-tRNA hydrolase

Gene Start:
110355

Gene Stop:
110921

Gene Length:
567

Molecular Weight*:
21818

pI*:
10.03

Net Charge*:
6.16

EC:
3.1.1.29  

Functional Class:
Translation; tRNA modification  

Pathway: pathway table
Miscellaneous enzymes

Comment:
In other bacteria, pth appears to promote the hydrolysis of peptide chains from tRNAs, perhaps as peptidyl-tRNAs exit ribosomes. See De La Vega et al., Gene 169:97 (1996) and Engel et al., J.Bact. 172:6959

See Prosite PDOC00920.

From Prosite: Peptidyl-tRNA hydrolase (EC 3.1.1.29) (PTH) is a bacterial enzyme that cleaves peptidyl-tRNA or N-acyl-aminoacyl-tRNA to yield free peptides or N-acyl-amino acids and tRNA. The natural substrate for this enzyme may be peptidyl-tRNA which drop off the ribosome during protein synthesis.


Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to Peptidyl-tRNA hydrolase sequences,
e.g. residues 1-187 are 58% similar to PTH_MYCPN.
MG083 is similar to T.pallidum TP1011, a peptidyl-tRNA
hydrolase (pth). It is also similar to C.trachomatis peptidyl-tRNA
hydrolase sequence CT800.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0193 is ehgpc-y.
COG name: Peptidyl-tRNA hydrolase.
Functional Class: J
BeTs to h,g,c,y.

Blocks Summary:  Blocks Search
Residues 6-31, 59-70, 87-125, 129-137 are members of blocks
BL01195A-D(Peptidyl-tRNA hydrolase proteins).

ProDom Summary:  Protein Domain Search
Residues 6-135, 136-185 constitute defined domains of PTH_MYCGE.
Residues 6-166 support this assignment, e.g. PTH_YEAST.

Paralogs:  Local Blast Search
No evidence of paralogs in M.genitalium.

Pfam Summary:  Pfam Search
Residues 6 to 187 (E-value = 1.6e-110) place MG083 in the Pept_tRNA_hydro family which is described as Peptidyl-tRNA hydrolase (PF01195)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
159  
189

PDB Hit:
gi|3114515|pdb|2PTH| Peptidyl-Trna Hydrolase From Escherichia Coli Hydrolase, Peptidyl-Trna Mol_id: 1; Molecule: Peptidyl-Trna Hydrolase; Chain: Null; Ec: 3.1.1.29; Engineered: Yes; Biological_unit: Monomer

Gene Protein Sequence:
MPTYKLIVGLGNLGKKYEKTRHNAGFMVLDRLASLFHLNFDKTNKLGDYL
FIKEKAAILAKPATFMNNSGLFVKWLQDHFQIPLANIMIVHDEIAFDLGV
IRLKMQGSANNHNGIKSVIRHLDTEQFNRLRFGIKSQNTSNILHEQVMSE
FQNSELTKLEVAITKSVELLKRYIEGEELQRLMEYYHHG

Gene Nucleotide Sequence:  Sequence Viewer
ATGCCCACCTATAAACTAATTGTTGGTTTAGGTAACTTAGGTAAAAAGTA
TGAGAAAACTCGCCATAATGCTGGTTTTATGGTGTTAGATAGACTAGCTA
GTTTATTCCACTTAAACTTTGATAAAACCAACAAGTTAGGTGATTATCTT
TTTATTAAAGAAAAAGCAGCAATCTTAGCAAAACCTGCTACCTTTATGAA
TAATAGCGGTCTTTTTGTGAAATGGTTACAAGATCACTTTCAAATTCCGC
TTGCAAACATAATGATAGTCCATGATGAAATAGCGTTTGATTTGGGAGTA
ATTAGGCTTAAAATGCAAGGGAGTGCTAACAATCATAATGGCATAAAATC
AGTAATTAGACATTTAGATACTGAACAGTTCAATCGTTTACGCTTTGGGA
TTAAATCACAAAATACGAGTAACATATTGCATGAACAGGTAATGAGTGAA
TTCCAGAATAGTGAACTGACTAAACTGGAAGTTGCGATTACAAAGTCTGT
TGAACTGTTGAAGCGTTATATTGAAGGAGAAGAGTTACAAAGGTTAATGG
AATATTATCATCATGGC


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