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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR574 IGR575 IGR572 IGR573 IGR577 IGR578 IGR571 IGR576 end3, - CT697 thdF, - CT698 psdD, - CT699 CT694 CT695 CT696 pgk, - CT693 CT700 secA, - CT701 end3, - CT697 thdF, - CT698 psdD, - CT699 CT694 CT695 CT696 pgk, - CT693 CT700 secA, - CT701 end3, - CT697 thdF, - CT698 psdD, - CT699 CT694 CT695 CT696 pgk, - CT693 CT700 secA, - CT701
* Calculated from Protein Sequence

Gene ID: CT697

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
end3  

Definition:
endonuclease III

Gene Start:
800526

Gene Stop:
799894

Gene Length:
633

Molecular Weight*:
23414

pI*:
9.71

Net Charge*:
8.20

EC:
4.2.99.18  

Functional Class:
DNA replication and repair  

Pathway: pathway table

Comment:
This endonuclease is said to have apurinic and apyrimidinic activity as well as DNA N-glycosylase activity.

From Prosite PDOC00615:

Escherichia coli endonuclease III (EC 4.2.99.18) (gene nth) is a DNA repair enzyme that acts both as a DNA N-glycosylase, removing oxidized pyrimidines from DNA, and as an apurinic/apyrimidinic (AP) endonuclease, introducing a single-strand nick at the site from which the damaged base was removed. Endonuclease III is an iron-sulfur protein that binds a single 4Fe-4S cluster. The 4Fe-4S cluster does not seem to be important for catalytic activity, but is probably involved in the proper positioning of the enzyme along the DNA strand.


Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to endonuclease III proteins, e.g., 33% similarity to END3_HAEIN, 33% similarity to END3_BACSU.
CT697 is siilar to TP0775, a predicted endonuclease III in T.pallidum; it
is weakly similar to TP0343, an A/G-specific adenine glycosylase.
No similarity to M.genitalium.

CT697 is orthologously related to CPn0837:
residues 10-208 are 73% similar to residues 2-200
of CPn0837.

COGS Summary:  COGS Search
BeTs to 16 clades of COG0177
COG name: Predicted EndoIII-related endonuclease
Functional Class:  L
The phylogenetic pattern of COG0177 is amtkYQvcebrhuj--olinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 40-49, 94-148, 181-208 are significantly matched to BL00764A,B,C, concerned with Endonuclease III iron-sulfur binding region proteins, e.g. END3_ECOLI, UVEN_MICLU and END3_BACSU

ProDom Summary:  Protein Domain Search
Residues 35 to 194 are 39% similar to an apurinic endonuclease domain as seen in MUTY_AERHY, END3_CAEEL and Y613_METJA


Paralogs:  Local Blast Search
CT697 is paralogously related to CT323, an A/G specific adenine glycosylase mutY: residues 7-152 are 21% similar to CT323.

Pfam Summary:  Pfam Search
Residues 39 to 174 (E-value = 4.9e-22) place CT697 in the HhH-GPD family which is described as HhH-GPD superfamily base excision DNA repair protein (PF00730)
Residues 104 to 133 (E-value = 2.3e-05) place CT697 in the HHH family which is described as Helix-hairpin-helix motif (PF00633)

PDB Hit:
gi|1311214|pdb|2ABK| Refinement Of The Native Structure Of Endonuclease Iii To A Resolution Of 1.85 Angstrom Dna-Repair, Dna Glycosylase Mol_id: 1; Molecule: Endonuclease Iii; Chain: Null; Ec: 4.2.99.18

Gene Protein Sequence:
MKSLNVQAKRAFIISTLNRLFPNPAPSLTGWQTPFQLLIAILLSGNSTDK
AVNSVTPSLFAKAPDAQSMSMLAPSEIYSLIAPCGLGERKAAYIHALSHI
LVDRYHQEPPHTLPELTALPGVGRKTASVFLSIYYGENTFPVDTHILRLA
HRWQLSTKRSPSAVEKDLVQFFGPKHSPKLHLQLIYYARAYCPALHHNID
VCPICSFLQTD

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAGTCACTAAATGTACAAGCTAAGCGTGCATTTATTATCTCTACTTT
AAACCGTCTTTTCCCTAATCCTGCGCCTTCGTTAACAGGATGGCAAACTC
CCTTTCAACTCCTCATTGCTATCCTTTTATCTGGAAATTCGACAGACAAA
GCTGTGAACTCTGTCACTCCCTCTCTCTTTGCTAAAGCACCAGATGCACA
ATCTATGAGTATGCTGGCTCCTTCTGAAATCTATTCACTCATTGCTCCTT
GTGGATTAGGAGAACGCAAAGCTGCGTATATTCATGCTCTATCACATATT
CTTGTGGATCGTTATCATCAAGAACCTCCTCACACCCTTCCAGAATTAAC
AGCTCTTCCAGGAGTAGGCAGAAAAACAGCTTCTGTTTTTTTAAGCATTT
ATTACGGAGAAAATACCTTCCCTGTAGATACACATATCCTTCGCTTAGCA
CATCGTTGGCAACTTTCTACGAAACGGAGTCCTTCAGCTGTAGAAAAAGA
TTTAGTACAGTTCTTTGGACCAAAGCACTCTCCGAAATTGCATTTACAAC
TCATCTACTATGCAAGAGCGTATTGTCCAGCGCTCCACCACAACATCGAT
GTGTGTCCTATCTGCTCTTTCTTACAGACAGAC


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