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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR717 IGR713 IGR711 IGR715 IGR718 IGR714 IGR712 IGR719 IGR720 HD0993 HD1000 HD0997 HD1001 pth, - HD0996 focA, - HD0991 potD, - HD0994 HD0995 uraA, - HD0998 putP, - HD0999 pflB,pfl, - HD0990 HD0992 HD1002 HD0993 HD1000 HD0997 HD1001 pth, - HD0996 focA, - HD0991 potD, - HD0994 HD0995 uraA, - HD0998 putP, - HD0999 pflB,pfl, - HD0990 HD0992 HD1002 HD0993 HD1000 HD1001 pth, - HD0996 focA, - HD0991 potD, - HD0994 HD0995 uraA, - HD0998 putP, - HD0999 pflB,pfl, - HD0990 HD0997 HD0992 HD1002
* Calculated from Protein Sequence

Gene ID: HD0996

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
pth  

Definition:
peptidyl-tRNA hydrolase

Gene Start:
792205

Gene Stop:
791603

Gene Length:
603

Molecular Weight*:
21685

pI*:
10.20

Net Charge*:
7.63

EC:
3.1.1.29  

Functional Class:
Translation; Amino acyl tRNA synthetases and tRNA modification  

Pathway: pathway table

Secondary Evidence:
Menez J, Buckingham RH, Zamaroczy Md M, Campelli CK.
Peptidyl-tRNA hydrolase in Bacillus subtilis, encoded by spoVC, is essential to vegetative growth,whereas the homologous enzyme in Saccharomyces cerevisiae is dispensable.
Mol Microbiol. 2002 Jul;45(1):123-9.
PMID: 12100553

Bonin PD, Choi GH, Trepod CM, Mott JE, Lyle SB, Cialdella JI, Sarver RW, Marshall VP, Erickson LA.
Expression, purification, and characterization of peptidyl-tRNA hydrolase from Staphylococcus aureus.
Protein Expr Purif. 2002 Feb;24(1):123-30.
PMID: 11812233

Menez J, Remy E, Buckingham RH.
Suppression of thermosensitive peptidyl-tRNA hydrolase mutation in Escherichia coli by gene duplication.
Microbiology. 2001 Jun;147(Pt 6):1581-9.
PMID: 11390689

Garcia-Villegas,M.R., De La Vega,F.M., Galindo,J.M., Segura,M.,
Buckingham,R.H. and Guarneros,G.
Peptidyl-tRNA hydrolase is involved in lambda inhibition of host
protein synthesis
EMBO J. 10 (11), 3549-3555 (1991)
Medline: 92007806


Comment:
From PF01195: Peptidyl-tRNA hydrolase.
Peptidyl-tRNA hydrolase 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.Bacterial PTH has been found to be evolutionary related to a yeast protein.


Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to peptidyl- and aminoacyl-tRNA hydrolase protein; e.g. residues 7-199 are 65% similar to (U32723) peptidyl- and aminoacyl-tRNA hydrolase of Haemophilus influenzae, residues 10-200 are 61% similar to (AE000219) peptidyl- and (D90756) aminoacyl-tRNA hydrolase of Escherichia coli, residues 10-200 are 60% similar to (U31571) peptidyl-tRNA hydrolase of Salmonella typhi.

COGS Summary:  COGS Search
BeTs to 13 clades of COG0193
COG name: Peptidyl-tRNA hydrolase
Functional Class: J
The phylogenetic pattern of COG0193 is ----yqvcebrhujgpolinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001328 (Peptidyl-tRNA hydrolase) with a combined E-value of 6e-54.
    IPB001328A    12-31
    IPB001328B    68-79
    IPB001328C    96-127
    IPB001328D    137-147


ProDom Summary:  Protein Domain Search
Residues 9-196 are 64% similar to a (HYDROLASE PEPTIDYL-TRNA SPORULATION) protein domain (PD005324) which is seen in PTH_HAEIN.



Paralogs:  Local Blast Search
HD0996 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 12 to 196 (E-value = 1.7e-96) place HD0996 in the Pept_tRNA_hydro family which is described as Peptidyl-tRNA hydrolase (PF01195)

PDB Hit:
pdb|2PTH| Peptidyl-Trna Hydrolase From Escherichia Coli 239 2e-064
pdb|2PTH| Peptidyl-Trna Hydrolase From Escherichia Coli 339 2e-094

Gene Protein Sequence:
MNRGNAVSQIKLIVGLANPGAKYEGTRHNAGEWLVNELARMYNTSLKDEA
KYFGKTAKINTVNGDVWLLIPTTFMNLSGKAVGALAHFFRIKAEEILIAH
DELDLPPGVAKLKQGGGHGGHNGLKDIISALGNNNNFYRIRLGIGHPGHK
DQVAGYVLSKPAPQDQQKINAVIDEASRCLEILFKDGVTSATNRLNSFKA
$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAATCGAGGCAATGCTGTGTCACAAATCAAATTGATCGTAGGCTTAGC
TAATCCGGGCGCAAAATATGAAGGTACTCGCCATAATGCAGGTGAATGGT
TAGTTAATGAGCTAGCCAGAATGTATAATACATCGCTCAAAGATGAAGCG
AAATATTTTGGCAAAACCGCCAAAATTAATACGGTAAACGGCGATGTTTG
GCTACTCATTCCCACTACATTTATGAATTTAAGTGGTAAAGCTGTCGGAG
CATTAGCCCATTTTTTCCGAATCAAGGCCGAAGAAATTTTAATTGCTCAC
GATGAATTAGATTTACCGCCAGGTGTGGCAAAACTAAAACAAGGTGGTGG
TCATGGTGGCCATAATGGTTTAAAAGATATTATTAGTGCATTGGGCAATA
ATAATAATTTCTATCGAATTAGACTCGGTATTGGTCATCCCGGGCATAAA
GATCAAGTAGCAGGTTATGTATTAAGCAAACCAGCTCCACAAGATCAACA
AAAAATAAATGCGGTGATTGATGAAGCCAGCCGTTGCCTTGAAATATTAT
TCAAAGATGGGGTCACAAGTGCCACCAACCGCTTAAACAGTTTTAAAGCA
TAA


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