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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0302 IGR0303 IGR0301 IGR0300 IGR0304 IGR0306 IGR0305 NG0368 dcrG, - NG0364 dcmG, - NG0365 NG0363 recB, - NG0370 NG0366 hemE, - NG0362 NG0361 sms,radA, - NG0367 NG0368 dcrG, - NG0364 dcmG, - NG0365 NG0363 recB, - NG0370 NG0366 hemE, - NG0362 NG0361 sms,radA, - NG0367 Type: tandem, Name:  - 17 NG0368 dcrG, - NG0364 dcmG, - NG0365 NG0363 recB, - NG0370 pspE, - NG0369 pspE, - NG0369 NG0366 hemE, - NG0362 NG0361 sms,radA, - NG0367
* Calculated from Protein Sequence

Gene ID: NG0365

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
dcmG  

Definition:
site-specific DNA-methyltransferase (cytosine-specific) NgoVII

Gene Start:
358440

Gene Stop:
357319

Gene Length:
1122

Molecular Weight*:
42088

pI*:
7.50

Net Charge*:
2.15

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 NG1893 (damH), NG1894 (dcmH), NG0873 (dcmD) , NG1795 (dcmH) and NG1991 (dcm).


Oklahoma ID: NGO.365c

Blast Summary:  PSI-Blast Search
NG0365 is 99% identical to a previously sequenced N.gonhorroeae protein, M.NgoVII, in GenBank, 1165245.

NG0365 is orthologous to D81836, N.meningitidis (Z2491) site-specific DNA-methyltransferase (cytosine-specific) protein: residues 5-202 are 38% similar to residues 17-201 of NG0365.

Numerous significant hits in gapped BLAST; e.g. residues 13-367 are 61% similar to 1808696 putative type II 5-cytosoine methyltransferase of Corynebacterium glutamicum, residues 15-338 are 35% similar to 9622224 cytosine-specific methyltransferase of Bacillus sp. LU11, residues 19-338 are 35% similar to emb|CAA59690.1| site-specific DNA-methyltransferase (cytosine-specific) of Haemophilus parahaemolyticus.

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 5.4e-61.
    IPB001525A    19-32
    IPB001525B    80-95
    IPB001525C    104-131
    IPB001525D    151-177
    IPB001525E    291-306
    IPB001525F    318-327
***** IPB002857 (CXXC zinc finger) with a combined E-value of 5.9e-06.
    IPB002857C    111-157
    IPB002857F    276-328


ProDom Summary:  Protein Domain Search
Residues 81-181 are identical to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000445) which is seen in Q59797_NEIGO.

Residues 339-374 are identical to a (MODIFICATION METHYLASE EC 2.1.1.73) protein domain (PD084558) which is seen in Q59606_NEIGO.

Residues 220-338 are 91% similar to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000554) which is seen in Q59606_NEIGO.

Residues 182-219 are identical to a (METHYLTRANSFERASE MODIFICATION METHYLASE) protein domain (PD189912) which is seen in Q59797_NEIGO.

Residues 20-80 are identical to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000515) which is seen in Q59606_NEIGO.



Paralogs:  Local Blast Search


NG0365 is paralogously related to NG1894 (5-methylcytosine methyltransferase) (1e-45), NG1795 (site-specific DNA-methyltransferase (cytosine-specific)) (3e-39), NG1991 (cytosine DNA methylase M.NgoI) (2e-38), NG1209 (DNA (cytosine-5-)-methyl transferase) (2e-35), NG0676 (modification methylase M.NgoV (site-specific DNA-methyltransferase)) (4e-31), NG0873 (DNA modification methylase) (1e-27) and NG1175 (cytosine specific DNA methyltransferase) (6e-07).


Pfam Summary:  Pfam Search
Residues 16 to 339 (E-value = 1.3e-88) place NG0365 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 153.0 4e-38
pdb|1FJX|1FJX-A STRUCTURE OF TERNARY COMPLEX OF HHAI 131.0 3e-31
pdb|10MH|10MH-A TERNARY STRUCTURE OF HHAI METHYLTRANSFERASE WITH130.0 5e-31
pdb|1G55|1G55-A STRU

Gene Protein Sequence:
MLSKQISNLNSSSNKPKILSLFSGCGGLDLGFHQAGCETVWANDFSHWAC
ESFRKNIGDVIVEGDIEQINPNDPTIPDCDIILGGFPCQDFSMIWKQPGL
EGERGNLYKSFLRFVNAKKPKVFVAENVKGLLTANKKKAIQQIITDFENC
GYYVQAKLYNFAEFGVPQFRERVLIVGVRLDTGFDFRHPEPTHNETGENG
LKPYVTAGQAISNIPQNASNNELLKISDKTRRMLELIPEGGNFTDIPKDH
PLYVKGMISHVYRRMHRNEPSKTIIAAGGGGTWGYHFPEPRAFTNRERAR
LQSFPDDFEFVGSTTEVRRQIGNAVPPQGVVELAKSILPIFSDNYEKVDL
HEKLVEEKEILFHDRLSKIRGGKQ

Gene Nucleotide Sequence:  Sequence Viewer
ATGCTATCTAAACAAATCTCAAATCTTAATTCTTCTAGTAACAAACCAAA
AATCCTATCTCTATTTTCAGGATGTGGCGGTTTGGATTTGGGCTTTCATC
AAGCTGGTTGTGAAACTGTTTGGGCGAACGATTTCTCCCATTGGGCTTGC
GAAAGTTTCCGTAAAAATATCGGCGATGTCATCGTAGAAGGTGATATTGA
ACAAATTAATCCGAATGATCCAACTATTCCCGATTGCGACATCATTTTAG
GCGGATTCCCTTGTCAAGATTTTTCCATGATTTGGAAACAGCCGGGCTTA
GAGGGTGAGCGCGGCAATCTTTATAAAAGCTTTTTACGTTTTGTAAATGC
AAAAAAACCGAAAGTTTTTGTTGCTGAGAATGTGAAAGGTTTATTGACTG
CCAACAAGAAAAAAGCCATCCAGCAAATTATTACCGACTTTGAAAATTGC
GGTTATTACGTTCAGGCGAAGCTGTATAACTTTGCAGAATTTGGCGTACC
TCAATTTCGTGAACGTGTGCTGATTGTCGGAGTACGTTTGGATACAGGAT
TTGATTTTCGCCATCCGGAACCGACGCACAATGAAACTGGCGAAAACGGC
TTAAAACCATATGTAACAGCAGGTCAGGCCATATCCAATATTCCACAAAA
TGCCAGTAATAATGAATTACTGAAAATCAGCGATAAAACACGCCGTATGT
TGGAATTAATTCCTGAAGGTGGAAATTTTACCGATATTCCTAAAGATCAT
CCTTTATATGTGAAAGGTATGATTAGCCACGTTTATCGTCGTATGCATCG
GAACGAGCCATCAAAAACAATTATTGCAGCAGGTGGCGGTGGTACTTGGG
GCTATCACTTCCCTGAACCGCGTGCTTTTACTAATAGAGAACGAGCAAGG
CTTCAAAGTTTTCCTGATGATTTTGAGTTTGTCGGATCAACAACTGAAGT
ACGTCGCCAGATTGGTAATGCTGTTCCTCCTCAGGGCGTGGTTGAACTGG
CAAAAAGCATTTTACCGATTTTTTCAGACAACTATGAGAAAGTAGATTTG
CATGAGAAATTAGTCGAAGAAAAAGAAATTTTATTCCATGACCGACTAAG
CAAAATTCGAGGGGGAAAACAA


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