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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0449 IGR0448 IGR0451 IGR0452 IGR0450 IGR0447 IGR0446 NG0547 ptpA, - NG0541 ppiA, - NG0544 glxK, - NG0540 NG0543 mod, - NG0545 res, - NG0546 NG0547 ptpA, - NG0541 ppiA, - NG0544 glxK, - NG0540 NG0543 mod, - NG0545 res, - NG0546 Type: tandem, Name:  - 28 NG0547 ptpA, - NG0541 ppiA, - NG0544 glxK, - NG0540 NG0543 mod, - NG0545 res, - NG0546 NG0542 NG0542
* Calculated from Protein Sequence

Gene ID: NG0545

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
mod  

Definition:
site-specific DNA-methyltransferase; type III restriction-modification system methyltransferase, subunit mod

Gene Start:
518013

Gene Stop:
520073

Gene Length:
2061

Molecular Weight*:
77475

pI*:
5.00

Net Charge*:
-17.23

EC:
2.1.1.72  3.1.21.5  

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

Pathway: pathway table

Secondary Evidence:
Humbelin,M., Suri,B., Rao,D.N., Hornby,D.P., Eberle,H., Pripfl,T., Kenel,S. and Bickle,T.A.
Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1 mod mutants.
J. Mol. Biol. 200 (1), 23-29 (1988)
Medline: 88245189.


Comment:
From GenBANK (gi:135253): type III site-specific deoxyribonuclease in E. coli binds the system-specific DNA recognition site 5'-CAGCAC-3'. It is necessary for both restriction and methylation (of one of the two A's). The reaction: S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine. The protein contains two different subunits, RES and MOD. MOD is a homotetramer.

See also NG0546, subunit RES of type III site-specific deoxyribonuclease.

From GenBANK (gi:4156030): In Helicobacter pylori, expression of this protein is predicted to be regulated by slipped-strand repair at the (G) polynucleotide repeat.

From Medline (88245189): The mod-res operon of phage P1 encodes the two structural genes for the EcoP1 type III restriction and modification system, res and mod. The mod gene product is responsible for binding the system-specific DNA recognition sequences in both restriction and modification; it also catalyses the modification reaction. A comparison of two mod gene product sequences shows that they have conserved amino and carboxyl ends but have completely different sequences in the middle of the molecules.

Oklahoma ID: NGO.545

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to type III site-specific deoxyribonuclease; e.g. residues 45-686 are 43% similar to pir||S03208 type III site-specific deoxyribonuclease (EC 3.1.21.5) EcoP15 chain mod of Escherichia coli.

Residues 149-491 are 28% similar to NMA1590, putative type III restriction/modification system modification methylase, of N.meningitidis (11354118).

COGS Summary:  COGS Search
BeTs to 3 clades of COG2189
COG name: Adenine specific DNA methylase Mod
Functional Class:  L
The phylogenetic pattern of COG2189 is a----------hUJ-------
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** PR00506 (D21 class N6 adenine-specific DNA methyltransferase signature) with a combined E-value of 3.1e-26.
    PR00506A    149-161
    PR00506B    213-232
    PR00506C    448-470
    PR00506D    471-485
***** IPB001091 (N-4 DNA methylase (N4-MTase)) with a combined E-value of 2.2e-11.
    IPB001091A    146-158
    IPB001091B    471-481


ProDom Summary:  Protein Domain Search
Residues 513-686 are 38% similar to a (TYPE III RESTRICTION-MODIFICATION SYSTEM) protein domain (PD022633) which is seen in T3MO_ECOLI.

Residues 432-526 are 43% similar to a (MODIFICATION METHYLASE KPNI EC) protein domain (PD118787) which is seen in MTK1_KLEPN.

Residues 451-506 are 57% similar to a (METHYLTRANSFERASE TRANSFERASE MODIFICATION METHYLASE) protein domain (PD000881) which is seen in T3MO_BPP1.

Residues 121-284 are 71% similar to a (METHYLTRANSFERASE MODIFICATION TRANSFERASE TYPE DNA) protein domain (PD096111) which is seen in T3MO_BPP1.

Residues 45-117 are 58% similar to a (TYPE III RESTRICTION-MODIFICATION SYSTEM) protein domain (PD034727) which is seen in T3MO_BPP1.



Paralogs:  Local Blast Search


NG0545 is paralogously related to NG0641 (type III restriction/modification system modification methylase) (1e-23).


Pfam Summary:  Pfam Search
Residues 217 to 530 (E-value = 2.5e-26) place NG0545 in the N6_N4_Mtase family which is described as DNA methylase (PF01555)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
23

PDB Hit:
pdb|1G60|1G60-A CRYSTAL STRUCTURE OF METHYLTRANSFERASE MBOII 43.8 1e-04
pdb|1EG2|1EG2-A CRYSTAL STRUCTURE OF RHODOBACTER SPHEROIDES (N6 49.7 2e-06

Gene Protein Sequence:
MLPTQPNPTQPNPTQPNPTQPNPSPDLSDTAGANTEAIYTSDGITANSTQ
LEQLKKLFPACFDADGNFLIDRLQAEIAPQTDIGREFYEMNWLGKSYARL
LRNLPPETLISEDKTHNAKPENAGSQNLLIRGDNLEVLKHLKNAYANSVK
MIYIDPPYNTGSDGFVYQDDRKFTPAELALLANIDEDEAARILDFTDKGS
NSHSAWLTFMYPRLYIARELLKDDGVIFISIDDNEAAQLKLLCDEVFGEG
NFVAQLPWRKRTAKSDVPFGISQDYEWIFVFAKSCQFIAATKGKERRYYE
TDDFPDRPWRTHDLTKQTTAAERPNSFFTMVDPKTGKKYPANPNATWRVT
KDTFQDYYNKGKIVFPDDYDFLNISNPVMRYFKDDDMKKAGEDFGKVAVS
SRLPENVGTLADAVAEYLAIFSRTLPENIGMTKEGTKEITDLFGSKIFTF
PKPSQLIKFLVSISSKSNDLILDFFAGSGTTAHAVMQLNAEGQNGNRRYI
CVQLPEKTAEKSEARKAGYPTIFDITKARIEKAAAKIRVEHPDYTGDSGF
KIFQTADNFRQHPDKDFSPEQPDLPLNDELSEEQLQTLLTTWTLYDGAAL
TTPVEPVRLGSYTAYLCEKRLYLLNKGFTSADLLAFIKKLDDDADFNPNR
VIVFGSNMASAMQHELDQAVRGYTNKKEIELNVIIRV

Gene Nucleotide Sequence:  Sequence Viewer
ATGCTGCCAACCCAACCCAACCCAACCCAACCCAACCCAACCCAACCCAA
CCCAACCCAACCCAACCCAAGCCCTGATCTAAGCGACACAGCCGGGGCGA
ACACTGAGGCAATCTACACTTCAGACGGCATTACCGCCAACTCTACCCAA
CTCGAACAGCTCAAAAAACTGTTTCCCGCCTGTTTTGACGCAGACGGAAA
TTTCCTTATCGACAGATTACAAGCCGAAATTGCGCCACAGACCGACATCG
GACGCGAATTTTACGAAATGAACTGGCTGGGCAAATCATATGCCCGCCTG
CTTCGCAACCTGCCGCCCGAAACCCTGATAAGTGAAGACAAAACGCACAA
CGCCAAGCCCGAAAATGCAGGCAGCCAAAATCTGCTGATTCGCGGCGATA
ATCTGGAAGTGTTGAAACACTTAAAAAACGCCTACGCAAACAGCGTGAAG
ATGATTTACATCGACCCGCCCTACAACACCGGATCGGACGGCTTTGTCTA
TCAGGACGACCGCAAATTCACACCCGCCGAACTTGCCCTCCTGGCGAATA
TTGACGAAGACGAAGCCGCGCGGATTTTAGATTTCACCGACAAAGGCTCA
AACTCGCACAGCGCGTGGCTGACCTTTATGTATCCGCGCCTGTATATCGC
CCGCGAACTGTTAAAGGACGACGGCGTGATTTTTATCTCGATTGACGATA
ACGAAGCGGCGCAGTTGAAATTGTTGTGTGATGAAGTGTTTGGGGAAGGG
AATTTTGTTGCACAATTGCCTTGGCGAAAAAGAACAGCTAAATCAGATGT
GCCTTTTGGTATTTCGCAGGATTATGAATGGATATTTGTATTCGCAAAAT
CTTGCCAATTTATTGCAGCAACTAAAGGCAAGGAACGACGCTATTATGAG
ACTGATGATTTCCCCGATCGTCCTTGGCGTACCCACGACTTAACGAAACA
AACAACTGCGGCGGAAAGGCCAAATAGTTTTTTCACAATGGTTGATCCCA
AGACAGGAAAAAAATATCCAGCAAATCCAAATGCAACTTGGCGTGTAACC
AAAGATACATTTCAAGATTATTATAATAAAGGAAAAATCGTTTTCCCTGA
TGATTATGATTTCTTAAATATCAGCAATCCAGTTATGCGTTACTTTAAAG
ATGACGACATGAAAAAAGCTGGCGAGGATTTTGGCAAAGTAGCTGTAAGC
AGTAGATTACCTGAAAATGTTGGTACATTAGCCGATGCAGTAGCCGAATA
TTTGGCTATTTTTAGTAGGACGCTACCTGAAAATATCGGAATGACTAAAG
AAGGCACAAAAGAAATCACAGATTTATTTGGTAGCAAAATATTTACCTTC
CCCAAGCCTAGTCAATTGATTAAATTTTTAGTTTCAATAAGTTCAAAGAG
TAATGACCTAATCCTAGACTTCTTCGCAGGCAGCGGCACAACCGCCCACG
CCGTGATGCAGCTTAACGCCGAAGGACAAAACGGTAACCGCCGCTATATC
TGTGTACAGCTTCCCGAAAAAACCGCTGAAAAATCCGAAGCCCGTAAAGC
AGGCTACCCGACCATCTTCGACATCACCAAAGCCCGCATAGAAAAAGCCG
CCGCCAAAATCCGCGTCGAACATCCCGATTACACGGGCGATTCCGGCTTC
AAAATCTTTCAAACGGCAGACAATTTCAGGCAGCATCCAGACAAGGATTT
TTCGCCCGAACAACCGGATTTGCCGCTTAACGATGAATTAAGCGAAGAAC
AGCTGCAAACGCTTCTGACCACCTGGACGCTGTATGACGGGGCGGCACTG
ACCACGCCGGTTGAGCCTGTGCGGTTGGGCAGTTATACGGCGTATCTGTG
CGAAAAACGGCTGTATCTGCTTAACAAGGGTTTTACTTCCGCCGATTTGC
TGGCGTTTATCAAGAAGCTGGACGACGATGCGGATTTCAATCCCAACCGT
GTGATTGTATTCGGCAGCAATATGGCAAGCGCCATGCAGCACGAACTCGA
CCAGGCGGTTCGCGGTTATACCAATAAAAAAGAGATTGAGTTGAATGTGA
TTATCAGGGTG


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