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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0568 IGR0566 IGR0567 IGR0570 IGR0571 IGR0565 IGR0573 IGR0569 IGR0564 IGR0572 NG0678 leuD, - NG0677 rngoV, - NG0675 spoU, - NG0670 leu3, - NG0674 mtb5,mngoV, - NG0676 leuC,leu3, - NG0679 NG0672 tpn, - NG0673 radC, - NG0681 suhB, - NG0671 gshA, - NG0680 NG0678 leuD, - NG0677 rngoV, - NG0675 spoU, - NG0670 leu3, - NG0674 mtb5,mngoV, - NG0676 leuC,leu3, - NG0679 NG0672 tpn, - NG0673 radC, - NG0681 suhB, - NG0671 gshA, - NG0680 NG0678 leuD, - NG0677 rngoV, - NG0675 spoU, - NG0670 leu3, - NG0674 mtb5,mngoV, - NG0676 leuC,leu3, - NG0679 tpn, - NG0673 suhB, - NG0671 gshA, - NG0680 NG0672
* Calculated from Protein Sequence

Gene ID: NG0676

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
mtb5  mngoV  

Definition:
modification methylase M.NgoV (site-specific DNA-methyltransferase)

Gene Start:
666106

Gene Stop:
664838

Gene Length:
1269

Molecular Weight*:
47548

pI*:
9.60

Net Charge*:
10.24

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 'ngo'genes see NG1991 (ngoI), NG0675 (rngoV),NG1795 (NgoPII).

See also: the restriction enzyme of this res/mod system, NG0675.

Oklahoma ID: NGO.676c

Blast Summary:  PSI-Blast Search
NG0676 is 98% identical to a previously sequenced Neisseria gonorrhoeae protein in GenBank, 1165242.

Numerous significant hits in gapped BLAST to DNA modification methylases; e.g. residues 3-419 are 42% similar to D00704 of Aneurinibacillus aneurinilyticus.

NG0676 is orthologous to AL162756, N. meningitidis Z2491 DNA modification methylase: residues 1-423 have 96% similarity to residues 1-423 in NG0676.

NG0676 is orthologous to U06074, N. lactamica M.NlaIV: residues 1-423 have 95% similarity to residues 1-423 in NG0676.

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 1.1e-53.
    IPB001525A    7-20
    IPB001525B    72-87
    IPB001525C    96-123
    IPB001525D    150-176
    IPB001525E    373-388
    IPB001525F    400-409


ProDom Summary:  Protein Domain Search
Residues 291-423 are 98% similar to a (METHYLTRANSFERASE MODIFICATION METHYLASE) protein domain (PD154973) which is seen in Q59605_NEIGO.

Residues 73-182 are 99% similar to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000445) which is seen in Q59605_NEIGO.

Residues 291-419 are 36% similar to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000554) which is seen in MTBA_BACAR.

Residues 194-290 are 84% similar to a (METHYLTRANSFERASE MODIFICATION METHYLASE) protein domain (PD016135) which is seen in MTN4_NEILA.

Residues 7-72 are identical to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION) protein domain (PD000515) which is seen in Q59605_NEIGO.



Paralogs:  Local Blast Search


NG0676 is paralogously related to NG1991 (cytosine DNA methylase M.NgoI) (1e-49), NG0365 (site-specific DNA-methyltransferase (cytosine-specific) NgoVII) (5e-31), NG1795 (site-specific DNA-methyltransferase (cytosine-specific)) (4e-26), NG1894 (5-methylcytosine methyltransferase) (1e-22), NG1209 (DNA (cytosine-5-)-methyl transferase) (6e-18) and NG0873 (DNA modification methylase) (6e-18).


Pfam Summary:  Pfam Search
Residues 4 to 421 (E-value = 2.2e-94) place NG0676 in the DNA_methylase family which is described as C-5 cytosine-specific DNA methylase (PF00145)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
174  
245

PDB Hit:
pdb|10MH|10MH-A TERNARY STRUCTURE OF HHAI METHYLTRANSFERASE WITH162.0 8e-41
pdb|1FJX|1FJX-A STRUCTURE OF TERNARY COMPLEX OF HHAI 162.0 8e-41
pdb|1DCT|1DCT-A DNA (CYTOSINE-5) METHYLASE FROM HAEIII 102.0 9e-23
pdb|1G55|1G55-A STRU

Gene Protein Sequence:
MQQIKFIDLFSGMSGIRKGFEQACRKQSVACECVFTSEIKPAALEVLKQN
YPDEVPYGDITKIETGDIPDFDILLAGFPCQAFSFAGKRLGFEDTRGTLF
FDVARILKAKKPKGFILENVEGLVTHDRKDSTQKIGRTLTVILETLEALG
YYVSWKVLNAKDFGIPQNRKRIYLTGSLKSKPDLSFETSPSPKLKNILES
GLPTESSPFIKKLLKKFPPSELYGKSVKDKRGGKNNIHSWDIELKGAVTE
EEKQLLNILLKERRKKKWASEIGIDWMDGMPLTKAQISTFYKHPDLQNIL
DSLTDKGYLVLEHPKQKIGGQRIKDESLPKGYNIVSGKKSFEINKILDPN
DVAPTLVAMDMEHLFVVDNGGLRTLTGKEGLRLFGYPDDYSFDIPKKDRC
DLLGNTVAVPVIKAVSERLLHTL

Gene Nucleotide Sequence:  Sequence Viewer
ATGCAACAAATTAAATTTATTGACTTATTTTCCGGAATGAGTGGCATCAG
GAAAGGATTCGAACAAGCCTGTCGGAAACAGTCGGTTGCTTGCGAATGTG
TTTTTACTTCAGAAATCAAACCGGCAGCTTTGGAAGTATTGAAGCAAAAC
TACCCTGATGAAGTGCCGTATGGAGATATAACGAAAATTGAAACAGGGGA
TATTCCCGATTTTGACATCCTGTTGGCAGGCTTCCCTTGTCAGGCTTTTT
CTTTCGCCGGAAAAAGATTAGGCTTTGAAGATACACGGGGAACGCTTTTC
TTTGATGTGGCAAGGATTTTAAAGGCAAAAAAACCAAAAGGTTTTATTTT
GGAAAATGTGGAAGGATTGGTGACACACGATAGAAAAGATTCGACACAAA
AAATAGGGCGCACCCTGACCGTTATTTTGGAAACCTTGGAAGCATTGGGC
TACTATGTTTCTTGGAAAGTTTTAAATGCAAAAGATTTCGGCATTCCCCA
AAACAGGAAGCGCATTTATCTGACAGGCAGTTTGAAATCCAAACCCGACT
TATCTTTCGAAACAAGCCCAAGTCCGAAATTAAAAAATATTTTGGAATCG
GGACTGCCTACTGAAAGCAGCCCTTTCATCAAAAAATTGCTAAAAAAATT
TCCCCCGTCCGAACTGTACGGAAAATCAGTAAAAGACAAACGGGGAGGGA
AAAACAATATTCACAGTTGGGATATTGAATTAAAAGGCGCAGTAACCGAA
GAAGAGAAGCAATTGTTAAATATCCTTCTAAAAGAACGGAGGAAAAAAAA
ATGGGCTTCAGAAATCGGCATAGATTGGATGGATGGGATGCCTTTGACAA
AAGCGCAAATTTCAACTTTCTATAAACACCCCGATCTCCAAAATATTTTG
GACAGCCTGACAGACAAAGGCTATTTGGTTTTAGAGCATCCGAAACAAAA
AATTGGCGGGCAAAGAATCAAAGATGAATCCCTGCCCAAAGGCTACAATA
TTGTTTCAGGTAAAAAATCTTTTGAAATCAATAAAATATTAGATCCAAAC
GATGTTGCGCCAACCTTGGTTGCAATGGATATGGAGCACCTTTTCGTCGT
TGACAACGGCGGTTTGCGTACACTTACCGGAAAAGAAGGGTTACGCTTAT
TCGGCTATCCGGACGATTATTCGTTTGATATTCCCAAAAAAGACAGATGC
GATTTATTGGGTAATACCGTTGCCGTCCCTGTGATTAAGGCGGTATCTGA
AAGACTTCTGCATACTTTA


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