Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1556 IGR1554 IGR1555 IGR1552 IGR1557 IGR1553 IGR1554.1 NG1891 dcrH, - NG1892 damH,hpyIM, - NG1893 NG1889 gltS, - NG1890 NG1895 galE, - NG1896 rfbD,rmlB, - NG1897 NG1891 dcrH, - NG1892 damH,hpyIM, - NG1893 NG1889 gltS, - NG1890 NG1895 galE, - NG1896 rfbD,rmlB, - NG1897 NG1891 dcrH, - NG1892 damH,hpyIM, - NG1893 NG1889 gltS, - NG1890 NG1895 dcmH, - NG1894 dcmH, - NG1894 galE, - NG1896 rfbD,rmlB, - NG1897
* Calculated from Protein Sequence

Gene ID: NG1894

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
dcmH  

Definition:
5-methylcytosine methyltransferase

Gene Start:
1861722

Gene Stop:
1860724

Gene Length:
999

Molecular Weight*:
37224

pI*:
8.70

Net Charge*:
7.13

EC:
2.1.1.73  

Functional Class:
Replication; DNA replication, restriction, modification, recombination, and repair  

Pathway: pathway table

Primary Evidence:
Stein,D.C., Gunn,J.S. and Piekarowicz,A. Sequence similarities between the genes encoding the S.NgoI and HaeII restriction/modification systems.
Biol. Chem. 379 (4-5), 575-578 (1998) Medline: 98290322

Labbe,D.,Holtke,H.J. and Lau,P.C.
Cloning and characterization of two tandemly arranged DNA methyltransferase genes of Neisseria lactamica: an
adenine-specific M.NlaIII and a cytosine-type methylase
Mol. Gen. Genet. 224 (1), 101-110 (1990) Medline: 91117164

Stein,D.C., Gunn,J.S., Radlinska,M. and Piekarowicz,A.
Restriction and modification systems of Neisseria
gonorrhoeae Gene 157 (1-2), 19-22 (1995) Medline: 95331562

Sullivan,K.M. and Saunders,J.R.
Sequence analysis of the NgoPII methyltransferase gene
from Neisseria gonorrhoeae P9: homologies with other enzymes recognizing the sequence 5'-GGCC-3'
Nucleic Acids Res. 16 (10), 4369-4387 (1988)
Medline: 88247748

Sullivan,K.M. and Saunders,J.R.
Nucleotide sequence and genetic organization of the NgoPII restriction-modification system of Neisseria gonorrhoeae
Mol. Gen. Genet. 216 (2-3), 380-387 (1989)
Medline: 89313677

Gunn,J.S. and Stein,D.C.
Natural variation of the NgoII restriction-modification system of Neisseria gonorrhoeae
Gene 132 (1), 15-20 (1993) Medline: 94010340

Stein,D.C., Chien,R. and Seifert,H.S.
Construction of a Neisseria gonorrhoeae MS11 derivative deficient in NgoMI restriction and modification
J. Bacteriol. 174 (15), 4899-4906 (1992) Medline: 92332422

Comment:
For other 'dcm' genes see NG0365 (dcmG), NG0873 (dcmD) ,NG1795 (dcmH) ,NG1893 (damH) and NG1991 (dcm).



Oklahoma ID: NGO.1894c

Blast Summary:  PSI-Blast Search
NG1894 is 100% identical to a previously sequenced N.gonorrhoeae protein in GenBank, 2330911, a predicted 5-methylcytosine methyltransferase. See also 1165245, 227054, 1399076.

Numerous significant hits in gapped BLAST; e.g. residues 5-329 are 27% similar to dbj|BAB35376.1| (AP002556) putative methyltransferase of Escherichia coli O157:H7.

Residues 22-327 are 31% similar to emb|CAB83726.1| (AL162753) modification methylase (cytosine-specific DNA methylase) of Neisseria meningitidis Z2491.




COGS Summary:  COGS Search
BeTs to 7 clades of COG0270
COG name: Site-specific DNA methylase dcm
Functional Class:  L
The phylogenetic pattern of COG0270 is -Mtk---ceB-hUJ-------
Number of proteins in this genome belonging to this COG is 8

Blocks Summary:  Blocks Search
***** IPB001525 (C-5 cytosine-specific DNA methylase) with a combined E-value of 6e-62.
    IPB001525A    8-21
    IPB001525B    74-89
    IPB001525C    100-127
    IPB001525D    147-173
    IPB001525E    280-295
    IPB001525F    307-316
***** IPB002857 (CXXC zinc finger) with a combined E-value of 1.6e-08.
    IPB002857C    107-153
    IPB002857F    265-317


ProDom Summary:  Protein Domain Search
Residues 75-180 are identical to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000445) which is seen in O30357_NEIGO.

Residues 209-329 are identical to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000554) which is seen in O30357_NEIGO.

Residues 209-274 are 53% similar to a (MODIFICATION METHYLASE EC 2.1.1.73) protein domain (PD084562) which is seen in Q59620_NEIME.

Residues 181-208 are identical to a (METHYLTRANSFERASE MODIFICATION METHYLASE) protein domain (PD189910) which is seen in O30357_NEIGO.

Residues 8-64 are 78% similar to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000515) which is seen in O30357_NEIGO.



Paralogs:  Local Blast Search


NG1894 is paralogously related to NG0365 (site-specific DNA-methyltransferase (cytosine-specific) NgoVII) (1e-45), NG1795 (site-specific DNA-methyltransferase (cytosine-specific)) (4e-38), NG0873 (DNA modification methylase) (4e-34), NG1991 (cytosine DNA methylase M.NgoI) (3e-32), NG1209 (DNA (cytosine-5-)-methyl transferase) (3e-26), NG0676 (modification methylase M.NgoV (site-specific DNA-methyltransferase)) (1e-22) and NG1175 (cytosine specific DNA methyltransferase) (2e-11).


Pfam Summary:  Pfam Search
Residues 5 to 328 (E-value = 8.7e-80) place NG1894 in the DNA_methylase family which is described as C-5 cytosine-specific DNA methylase (PF00145)

Structural Feature(s):
Feature Type  Start  Stop
No predicted structural features.  
  

PDB Hit:
pdb|1DCT|1DCT-A DNA (CYTOSINE-5) METHYLASE FROM HAEIII 124.0 2e-29
pdb|10MH|10MH-A TERNARY STRUCTURE OF HHAI METHYLTRANSFERASE WITH 83.9 4e-17
pdb|1FJX|1FJX-A STRUCTURE OF TERNARY COMPLEX OF HHAI 83.1 7e-17
pdb|1G55|1G55-A STRU

Gene Protein Sequence:
MHTPLTYIDLFSGAGGLSLGFEQAGFQQLLSVEMESDYCQTYRTNFPRHQ
LLQKDLTTLTEQDLTNCLNGQSVDLVIGGPPCQGFSMAGKIGRTFTDDPR
NHLFKEFVRIVKIVQPYFFVMENVARLYTHNSGKTRIEIIQAFQNIGYSV
ECKILSAADFGVPQIRSRVIFIGRRDKGKISFPEPLQISHQTVGSAIGHF
PKLAAGESNPHVANHEAMNHSAQMLEKMAFVKNGGNRNDIPEPLRPKTGD
IRKYIRYNSNKPAVCITGDMRKVFHYEQNRALTVRELAALQSFPDNFIFC
GSKIAQQQQVGNAVPPLLAKAIAESILKMSENE

Gene Nucleotide Sequence:  Sequence Viewer
ATGCACACACCACTTACCTATATTGACCTTTTCTCAGGAGCAGGAGGCCT
ATCCTTGGGTTTTGAACAAGCCGGATTCCAACAATTGCTTTCTGTTGAAA
TGGAGTCTGATTATTGTCAGACTTACCGTACCAACTTCCCCCGTCATCAA
TTACTGCAAAAAGATTTAACCACACTAACCGAACAAGATTTAACCAATTG
TCTTAACGGACAATCAGTTGATTTGGTTATTGGAGGACCACCTTGTCAAG
GTTTTAGTATGGCAGGAAAGATTGGACGGACATTTACAGATGACCCACGC
AACCATTTATTTAAAGAGTTTGTCCGAATAGTTAAAATTGTCCAACCATA
TTTTTTTGTTATGGAAAATGTAGCGCGACTCTATACACACAATTCAGGTA
AAACACGTATTGAGATTATTCAAGCATTTCAGAATATCGGTTATTCGGTG
GAATGTAAGATACTGAGTGCAGCCGATTTCGGTGTTCCTCAGATACGTAG
CCGAGTGATATTTATCGGGAGGAGGGATAAAGGCAAAATTTCCTTTCCCG
AACCTTTGCAGATTTCCCATCAGACTGTTGGATCAGCAATAGGACATTTT
CCAAAACTGGCTGCTGGCGAAAGCAATCCACACGTTGCAAATCATGAAGC
TATGAATCATTCGGCACAAATGTTAGAAAAAATGGCATTTGTTAAAAATG
GAGGTAACCGTAACGATATTCCTGAACCATTACGTCCGAAAACAGGTGAT
ATCCGTAAATACATCCGTTACAACAGCAACAAACCAGCCGTTTGTATTAC
AGGAGATATGCGCAAAGTTTTTCACTATGAACAGAATCGGGCTTTAACCG
TTCGTGAATTAGCTGCCTTACAATCTTTCCCTGATAATTTTATTTTTTGC
GGCAGCAAAATTGCCCAGCAGCAGCAGGTTGGTAACGCCGTGCCGCCTTT
ATTGGCAAAAGCTATTGCTGAAAGTATTTTAAAAATGAGTGAAAATGAA


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy