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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap tRNA-Glu-3 IGR0942 IGR0941 IGR0940.1 IGR0939 IGR0936 IGR0937 IGR0938 IGR0940 IGR0934 IGR0935 IGR0940.2 NG1159 NG1166 pivNg, - NG1163.1 pivNg, - NG1164 NG1156 tehB, - NG1161 NG1165 NG1158 tspB, - NG1167 NG1163 rnh, - NG1162 tpn, - NG1157 thiD, - NG1160 NG1159 NG1166 pivNg, - NG1163.1 pivNg, - NG1164 NG1156 tehB, - NG1161 NG1165 NG1158 tspB, - NG1167 NG1163 rnh, - NG1162 tpn, - NG1157 thiD, - NG1160 Type: inverse, Name:  - 166 Type: direct, Name:  - 122 Type: inverse, Name:  - 160 Type: direct, Name:  - 100 Type: inverse, Name:  - 161 Type: direct, Name:  - 136 Type: direct, Name:  - 111 Type: inverse, Name:  - 181 Type: direct, Name:  - 127 Type: direct, Name:  - 125 NG1159 NG1166 pivNg, - NG1163.1 pivNg, - NG1164 NG1156 tehB, - NG1161 NG1165 NG1158 tspB, - NG1167 rnh, - NG1162 tpn, - NG1157 thiD, - NG1160 NG1163
* Calculated from Protein Sequence

Gene ID: NG1162

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
rnh  

Definition:
Ribonuclease H

Gene Start:
1102252

Gene Stop:
1102686

Gene Length:
435

Molecular Weight*:
16180

pI*:
7.90

Net Charge*:
1.81

EC:
3.1.26.4  

Functional Class:
Transcription; Degradation of RNA  

Pathway: pathway table

Secondary Evidence:
Kanaya,S., Kimura,S., Katsuda,C. and Ikehara,M.
Role of cysteine residues in ribonuclease H from Escherichia coli.
Biochem. J. 271 (1), 59-66 (1990)
Medline: 91024947

Katayanagi,K., Miyagawa,M., Matsushima,M., Ishikawa,M., Kanaya,S., Ikehara,M., Matsuzaki,T. and Morikawa,K.
Three-dimensional structure of ribonuclease H from E. coli
Nature 347 (6290), 306-309 (1990)
Medline: 90384573

Katayanagi,K., Miyagawa,M., Matsushima,M., Ishikawa,M., Kanaya,S., Nakamura,H., Ikehara,M., Matsuzaki,T. and Morikawa,K.
Structural details of ribonuclease H from Escherichia coli as
refined to an atomic resolution
J. Mol. Biol. 223 (4), 1029-1052 (1992)
Medline: 92167248

Yang,W., Hendrickson,W.A., Crouch,R.J. and Satow,Y.
Structure of ribonuclease H phased at 2 A resolution by MAD
analysis of the selenomethionyl protein
Science 249 (4975), 1398-1405 (1990)
Medline: 90385276

Ishikawa,K., Kimura,S., Kanaya,S., Morikawa,K. and Nakamura,H.
Structural study of mutants of Escherichia coli ribonuclease HI
with enhanced thermostability
Protein Eng. 6 (1), 85-91 (1993)
Medline: 93165655

Katayanagi,K., Ishikawa,M., Okumura,M., Ariyoshi,M., Kanaya,S.,
Kawano,Y., Suzuki,M., Tanaka,I. and Morikawa,K.
Crystal structures of ribonuclease HI active site mutants from
Escherichia coli
J. Biol. Chem. 268 (29), 22092-22099 (1993)
Medline: 94012805

Kashiwagi,T., Jeanteur,D., Haruki,M., Katayanagi,K., Kanaya,S. and Morikawa,K.
Proposal for new catalytic roles for two invariant residues in
Escherichia coli ribonuclease HI
Protein Eng. 9 (10), 857-867 (1996)
Medline: 97084791

Yamazaki,T., Yoshida,M., Kanaya,S., Nakamura,H. and Nagayama,K.
Assignments of backbone 1H, 13C, and 15N resonances and secondary
structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy
Biochemistry 30 (24), 6036-6047 (1991)
Medline: 91255229

Yamasaki,K., Ogasahara,K., Yutani,K., Oobatake,M. and Kanaya,S.
Folding pathway of Escherichia coli ribonuclease HI: a circular
dichroism, fluorescence, and NMR study
Biochemistry 34 (51), 16552-16562 (1995)
Medline: 96118372


Comment:
For other 'rnh' genes see NG1789 (rnhB).

Oklahoma ID: NGO.1162

Blast Summary:  PSI-Blast Search
Residues 1-145 in NG1162 have 95% similarity to residues 1-145 in AL162757, N. meningitidis Z2491 ribonuclease HI.
NG1162 also has strong similarity to ribonuclease H proteins in several other organisms, e.g. residues 5-143 are 61% similar to the enzyme from P.aeruginosa (11352491).

COGS Summary:  COGS Search
BeTs to 8 clades of COG0328
COG name: Ribonuclease HI
Functional Class:  L
The phylogenetic pattern of COG0328 is ----y--cebrhuj---l--x
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB002156 (RNase H) with a combined E-value of 6.1e-13.
    IPB002156A    7-17
    IPB002156B    64-74
    IPB002156C    129-138


ProDom Summary:  Protein Domain Search
Residues 113-141 are 68% similar to a (RIBONUCLEASE H RNASE HYDROLASE NUCLEASE ENDONUCLEASE) protein domain (PD010718) which is seen in RNH_SALTY.

Residues 2-110 are 61% similar to a (POLYPROTEIN HYDROLASE PROTEASE POL ASPARTYL RIBONUCLEASE) protein domain (PD000342) which is seen in O69014_ZYMMO.



Paralogs:  Local Blast Search


NG1162 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 2 to 142 (E-value = 2.4e-60) place NG1162 in the RnaseH family which is described as RNase H (PF00075)

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

PDB Hit:
pdb|1RCH|1RCH SOLUTION NMR STRUCTURE OF RIBONUCLEASE HI FROM 194.0 9e-51
pdb|1RBS|1RBS RIBONUCLEASE H (E.C.3.1.26.4) MUTANT WITH HIS 62 193.0 1e-50
pdb|1LAW|1LAW RIBONUCLEASE H (E.C.3.1.26.4) MUTANT WITH VAL 74 193.0 1e-50
pdb|1RBR|1RBR RIBON

Gene Protein Sequence:
MDTPVYLYTDGACKGNPGAGGWGVLMRYGSREKELFGGEAQTTNNRMELT
AVIEGLKSLKRRCTVIICTDSQYVKNGMENWIHGWKRNGWKTAAKQPVKN
DDLWQELDALVGQHQVSWTWVKGHAGHAENERADDLANRGAAQFS

Gene Nucleotide Sequence:  Sequence Viewer
ATGGACACACCCGTTTACCTCTACACGGACGGCGCGTGCAAAGGCAATCC
CGGCGCGGGCGGCTGGGGCGTATTAATGCGCTACGGCAGCCGCGAAAAAG
AACTTTTCGGCGGCGAAGCGCAAACCACCAACAACCGCATGGAGCTGACC
GCCGTTATCGAAGGGCTGAAATCGCTCAAACGCCGCTGCACCGTCATCAT
CTGCACCGACTCGCAATACGTCAAAAACGGCATGGAAAACTGGATACACG
GTTGGAAGCGCAACGGCTGGAAAACCGCCGCCAAACAGCCCGTCAAAAAC
GACGACTTGTGGCAAGAACTCGACGCTCTGGTCGGGCAGCATCAAGTCAG
CTGGACTTGGGTTAAAGGACACGCGGGACACGCGGAAAACGAACGCGCCG
ACGATTTGGCAAACCGTGGCGCGGCACAGTTTTCT


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