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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0820.1 IGR0825 IGR0826 IGR0823 IGR0824 IGR0820 IGR0821 IGR0827 IGR0822 IGR0819 NG1000 NG1004 NG1002 NG0995 NG1001 NG1003 azu,H.8, - NG0994 secA, - NG0997 dnaG,priM, - NG0998 rpoD, - NG0999 NG0996 NG1000 NG1004 NG1002 NG0995 NG1001 NG1003 azu,H.8, - NG0994 secA, - NG0997 dnaG,priM, - NG0998 rpoD, - NG0999 NG0996 NG0995 NG1001 NG1003 azu,H.8, - NG0994 NG1000 NG1004 NG1002 secA, - NG0997 dnaG,priM, - NG0998 rpoD, - NG0999 NG0996
* Calculated from Protein Sequence

Gene ID: NG0998

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
dnaG  priM  

Definition:
DNA primase

Gene Start:
968910

Gene Stop:
970679

Gene Length:
1770

Molecular Weight*:
65792

pI*:
6.50

Net Charge*:
-4.67

EC:
2.7.7.-  

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

Pathway: pathway table
DNA polymerase
Porphyrin and chlorophyll metabolism
Ubiquinone biosynthesis

Secondary Evidence:
Burton,Z.F., Gross,C.A., Watanabe,K.K. and Burgess,R.R.
The operon that encodes the sigma subunit of RNA polymerase also encodes ribosomal protein S21 and DNA primase in E. coli K12. Cell 32 (2): 335-349 (1983)
[Medline: 83129424].

Smiley,B.L., Lupski,J.R., Svec,P.S., McMacken,R. and Godson,G.N. Sequences of the Escherichia coli dnaG primase gene and regulation of its expression.
Proc. Natl. Acad. Sci. U.S.A. 79 (15): 4550-4554 (1982)
[Medline: 83014926].

Stamford,N.P., Lilley,P.E. and Dixon,N.E.
Enriched sources of Escherichia coli replication proteins. The dnaG primase is a zinc metalloprotein.
Biochim. Biophys. Acta 1132 (1): 17-25 (1992)
[Medline: 92379087].

Comment:
For other 'dna' genes, see NG0002 (dnaN), NG0078 (dnaE), NG0235 (dnaJ), NG0451 (dnaB), NG0485 (dnaB), NG0551 (dnaJ), NG0973 (dnaQ), NG0001 (dnaA), NG1110 (dnaC), NG1429 (dnaK), NG1636 (dnaC) and NG1901 (dnaJ).

From GenBANK (gi:130908): DNA primase is the polymerase that synthesizes small RNA primers for the okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis. As a cofactor, it binds one zinc ion per molecule.

Oklahoma ID: NGO.998

Blast Summary:  PSI-Blast Search
NG0998 is orthologous to AE002503, N. meningitidis MC58 DNA primase: residues 1-590 have 96% similarity to residues 1-590 in NG0998.

NG0998 also has very strong (P-value < 1e-100) similarity to DNA primases (DnaG proteins) in several other organisms; e.g. residues 1-432 are 51% similar to 11348452 of Pseudomonas aeruginosa.

COGS Summary:  COGS Search
BeTs to 16 clades of COG0358
COG name: DNA primase (bacterial type)
Functional Class:  L
The phylogenetic pattern of COG0358 is amtk-qvcebrhujGPolinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB002694 (CHC2 zinc finger) with a combined E-value of 1.9e-130.
    IPB002694A    37-82
    IPB002694B    141-161
    IPB002694C    193-217
    IPB002694D    224-243
    IPB002694E    258-295
    IPB002694F    297-310
    IPB002694G    336-346


ProDom Summary:  Protein Domain Search
Residues 209-356 are 60% similar to a (PRIMASE DNA TRANSFERASE REPLICATION DNA-DIRECTED RNA) protein domain (PD002276) which is seen in PRIM_HAEIN.

Residues 362-521 are 25% similar to a (DNA PRIMASE TRANSFERASE REPLICATION) protein domain (PD011358) which is seen in PRIM_HAEIN.

Residues 111-208 are 44% similar to a (PRIMASE DNA TRANSFERASE REPLICATION) protein domain (PD003861) which is seen in PRIM_ECOLI.

Residues 33-87 are 72% similar to a (PRIMASE DNA TRANSFERASE REPLICATION) protein domain (PD002988) which is seen in O33470_PSEPU.



Paralogs:  Local Blast Search


NG0998 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 2 to 99 (E-value = 5.1e-60) place NG0998 in the zf-CHC2 family which is described as CHC2 zinc finger (PF01807)
Residues 255 to 337 (E-value = 2.2e-22) place NG0998 in the Toprim family which is described as Toprim domain (PF01751)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
242  
282
transmembrane  
266  
282
coil-coil  
542  
579

PDB Hit:
pdb|1DD9|1DD9-A STRUCTURE OF THE DNAG CATALYTIC CORE 304.0 3e-83
pdb|1EQN|1EQN-A E.COLI PRIMASE CATALYTIC CORE 303.0 7e-83
pdb|1D0Q|1D0Q-A STRUCTURE OF THE ZINC-BINDING DOMAIN OF 102.0 2e-22
pdb|1DD9|1DD9-A STRU

Gene Protein Sequence:
MIPSDFIDELLAKTDIVGIIDEQVPLKKGGANYMACCPFHKEKTPSFSVS
PTKQFYHCFSCGAHGSAIGFVMEHQGLSFPEAVQFLADRVGMIVPKVRGQ
NDNPEVRAERKKKQQTLEETTAAAADFYAQQLKFNPAAKAYLDKRGLSAE
VIAHYGLGYAPDGWQPLAQVFQPYPNTALVDTGMVIDNEGRHYDRFRHRI
MFPIRNPRGQVIGFGGRVLDDSKPKYLNSPDTPLFDKGKNLYGLYEGRAA
VKEAERILVVEGYMDVVALAQFGVGYGVAALGTATTAEHVKILMRQADSI
YFCFDGDSAGRKAAWRALENALPQLKDDKSLHFLFLPEEHDPDSYIRAYG
KAQFEDALLNQSKPLSEYFWEHLSDGIHLNTQEGKAELVKTSSPLLVQIT
APALAYLLKQRLSELVGIDPDNLAQLLGQEAPKRHVKQKNYKLPPISVKQ
PVMPTLVQRQIRSLLINPDWAAYIDLPDYLALDGDFACLANLAETIKNHP
SVPATAQVLEHMRGSPYEETINRIFRSALQSEEMEGGGEEDCENFQIGIK
KLLNELKYSQIETLKQKSLQSGLNESEKKLLLSLLTAKQN

Gene Nucleotide Sequence:  Sequence Viewer
ATGATTCCATCCGACTTCATTGACGAGCTTCTGGCCAAAACCGATATTGT
CGGCATCATCGACGAGCAGGTTCCGCTGAAAAAAGGCGGGGCGAACTATA
TGGCGTGTTGCCCGTTCCACAAGGAAAAAACACCGTCGTTTTCGGTCAGT
CCGACCAAGCAGTTTTATCATTGTTTCAGTTGCGGGGCGCATGGTTCGGC
GATTGGTTTTGTGATGGAACATCAGGGACTGTCGTTTCCGGAGGCGGTTC
AGTTCCTTGCCGACCGCGTAGGTATGATTGTGCCTAAAGTGCGCGGGCAG
AACGATAATCCCGAAGTCCGTGCCGAGCGCAAGAAAAAACAGCAGACGCT
GGAAGAAACGACGGCGGCGGCAGCTGATTTTTACGCGCAGCAGCTGAAAT
TCAATCCGGCTGCGAAAGCTTATTTGGACAAACGCGGCTTGAGCGCGGAA
GTCATCGCGCATTATGGTTTGGGCTACGCGCCCGACGGCTGGCAGCCTTT
GGCGCAAGTGTTCCAACCGTATCCGAATACCGCGTTGGTGGATACGGGGA
TGGTGATTGACAATGAGGGGCGGCATTACGACCGCTTCCGCCATCGGATT
ATGTTCCCCATCCGCAATCCGCGCGGGCAGGTCATCGGTTTCGGCGGCAG
GGTGCTGGACGACTCGAAACCGAAATATTTGAATTCGCCCGATACGCCTT
TGTTCGATAAGGGGAAAAACCTTTACGGCTTGTATGAGGGGCGTGCTGCT
GTAAAAGAGGCAGAACGGATTTTGGTGGTCGAAGGCTATATGGACGTGGT
CGCGCTGGCACAGTTCGGCGTGGGCTACGGTGTGGCGGCCTTGGGCACGG
CGACGACGGCGGAACACGTCAAAATCCTGATGCGGCAGGCGGACAGTATT
TATTTCTGTTTCGACGGCGACAGCGCGGGGCGAAAAGCGGCTTGGCGCGC
GCTGGAAAACGCGCTGCCGCAGTTGAAAGACGACAAATCGCTGCATTTTT
TATTCCTGCCGGAAGAACACGACCCCGACAGCTACATCCGCGCCTACGGC
AAAGCGCAATTTGAAGACGCGCTTCTGAATCAAAGCAAGCCTTTGTCGGA
ATATTTCTGGGAACACCTTTCAGACGGCATTCATCTCAATACGCAGGAAG
GCAAGGCGGAATTGGTGAAAACCAGTTCGCCGCTTTTGGTGCAGATTACC
GCACCGGCATTGGCTTATTTGTTAAAACAACGGCTTAGCGAGCTGGTCGG
CATCGACCCCGACAACCTCGCGCAACTGCTCGGACAGGAAGCGCCAAAGC
GGCACGTCAAACAAAAAAACTACAAACTGCCTCCGATTTCCGTCAAACAG
CCCGTTATGCCGACATTGGTGCAACGGCAAATCCGCAGCCTCTTGATAAA
TCCGGATTGGGCTGCATATATAGACCTGCCCGATTATCTGGCGTTGGACG
GCGATTTCGCCTGCCTTGCCAACCTCGCCGAAACCATTAAAAACCATCCT
TCCGTGCCGGCAACCGCACAGGTTTTGGAACATATGCGCGGTTCGCCCTA
CGAAGAAACAATCAACCGCATCTTCCGGTCGGCCCTTCAATCGGAAGAAA
TGGAAGGCGGCGGCGAAGAAGATTGCGAAAACTTCCAAATCGGCATCAAA
AAACTGCTCAATGAGTTAAAATACAGCCAAATTGAAACATTAAAACAAAA
AAGCCTGCAATCCGGCTTAAATGAAAGCGAGAAAAAACTTTTGCTGTCGC
TGCTGACCGCAAAACAAAAT


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