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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1689 IGR1690 IGR1687 IGR1688 IGR1691 IGR1686 IGR1685 gna33, - NG2048 glmS, - NG2045 metS,metG, - NG2044 NG2046 NG2043 NG2047 pilS, - NG2042 gna33, - NG2048 glmS, - NG2045 metS,metG, - NG2044 NG2046 NG2043 NG2047 pilS, - NG2042 Type: tandem, Name:  - 92 gna33, - NG2048 glmS, - NG2045 metS,metG, - NG2044 NG2043 NG2047 pilS, - NG2042 NG2046
* Calculated from Protein Sequence

Gene ID: NG2044

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
metS  metG  

Definition:
methionyl-tRNA synthetase (MetG)

Gene Start:
2019505

Gene Stop:
2017454

Gene Length:
2052

Molecular Weight*:
76937

pI*:
5.50

Net Charge*:
-16.87

EC:
6.1.1.10  

Functional Class:
Translation; Amino acyl tRNA synthetases and tRNA modification  

Pathway: pathway table
Aminoacyl-tRNA biosynthesis
Methionine metabolism
Selenoamino acid metabolism

Secondary Evidence:
Fourmy,D., Dardel,F. and Blanquet,S.
Methionyl-tRNA synthetase zinc binding domain. Three-dimensional
structure and homology with rubredoxin and gag retroviral proteins
J. Mol. Biol. 231 (4), 1078-1089 (1993)
Medline: 93294859

Fourmy,D., Meinnel,T., Mechulam,Y. and Blanquet,S.
Mapping of the zinc binding domain of Escherichia coli
methionyl-tRNA synthetase
J. Mol. Biol. 231 (4), 1068-1077 (1993)
Medline: 93294858



Fourmy,D., Mechulam,Y., Brunie,S., Blanquet,S. and Fayat,G.
Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase
FEBS Lett. 292 (1-2), 259-263 (1991)
Medline: 92070503

Meinnel,T., Mechulam,Y., Dardel,F., Schmitter,J.M., Hountondji,C.,
Brunie,S., Dessen,P., Fayat,G. and Blanquet,S.
Methionyl-tRNA synthetase from E. coli--a review
Biochimie 72 (8), 625-632 (1990)
Medline: 91129305

Hountondji,C., Schmitter,J.M., Beauvallet,C. and Blanquet,S.
Mapping of the active site of Escherichia coli methionyl-tRNA
synthetase: identification of amino acid residues labeled by
periodate-oxidized tRNA(fMet) molecules having modified lengths at
the 3'-acceptor end
Biochemistry 29 (35), 8190-8198 (1990)
Medline: 91084494


Brunie,S., Zelwer,C. and Risler,J.L.
Crystallographic study at 2.5 A resolution of the interaction of
methionyl-tRNA synthetase from Escherichia coli with ATP
J. Mol. Biol. 216 (2), 411-424 (1990)
Medline: 91073404

Dardel,F., Panvert,M. and Fayat,G.
Transcription and regulation of expression of the Escherichia coli
methionyl-tRNA synthetase gene
Mol. Gen. Genet. 223 (1), 121-133 (1990)
Medline: 91080852

Dardel,F., Fayat,G. and Blanquet,S.
Molecular cloning and primary structure of the Escherichia coli
methionyl-tRNA synthetase gene
J. Bacteriol. 160 (3), 1115-1122 (1984)
Medline: 85054627

Barker,D.G., Ebel,J.P., Jakes,R. and Bruton,C.J.
Methionyl-tRNA synthetase from Escherichia coli. Primary structure
of the active crystallised tryptic fragment
Eur. J. Biochem. 127 (3), 449-457 (1982)
Medline: 83079258

Zelwer,C., Risler,J.L. and Brunie,S.
Crystal structure of Escherichia coli methionyl-tRNA synthetase at
2.5 A resolution
J. Mol. Biol. 155 (1), 63-81 (1982)
Medline: 82192427




Comment:
This protein is probably essential for cell survival. It is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA aminoacylation.

See also NG2027, methionine biosynthesis transcriptional regulator (MetR). In addition, other 'met' genes include: NG0928, metE; NG1149, metZ; NG0933, metX; NG0929, metF; NG0386, metC/metB2; and NG0106, metK, all involved in methionine biosynthesis.

Oklahoma ID: NGO.2044c

Blast Summary:  PSI-Blast Search
Matches in gapped BLAST to met-tRNA synthetases. Residues 3-683 are 57% similar to SYM_HAEIN (1174532).

Residues 1-684 are 95% similar to NMA0275 in N.meningitidis (11271474).

COGS Summary:  COGS Search
BeTs to 17 clades of COG0143
COG name: Methionyl-tRNA synthetase
Functional Class:  J
The phylogenetic pattern of COG0143 is amtkYqvcebrhujgpolinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB002547 (Putative tRNA binding domain) with a combined E-value of 7e-08.
    IPB002547A    26-40
    IPB002547B    643-660
***** IPB001412 (Aminoacyl-transfer RNA synthetases class-I) with a combined E-value of 6.4e-07.
    IPB001412A    12-22
    IPB001412B    336-346


ProDom Summary:  Protein Domain Search
Residues 79-144 are 69% similar to a (METHIONYL-TRNA SYNTHETASE) protein domain (PD006341) which is seen in SYM_HAEIN.

Residues 327-468 are 55% similar to a (SYNTHETASE AMINOACYL-TRNA PROTEIN LIGASE BIOSYNTHESIS) protein domain (PD000476) which is seen in SYM_HAEIN.

Residues 150-324 are 64% similar to a (SYNTHETASE AMINOACYL-TRNA LIGASE PROTEIN BIOSYNTHESIS) protein domain (PD000647) which is seen in SYM_ECOLI.

Residues 3-402 are 25% similar to a (PUTATIVE TRNA SYNTHETASE AMINOACYL-TRNA) protein domain (PD217233) which is seen in Q9ZBH7_STRCO.

Residues 3-74 are 70% similar to a (SYNTHETASE AMINOACYL-TRNA LIGASE PROTEIN BIOSYNTHESIS) protein domain (PD000389) which is seen in SYM_ECOLI.

Residues 470-565 are 41% similar to a (METHIONYL-TRNA SYNTHETASE) protein domain (PD038617) which is seen in SYM_ECOLI.

Residues 580-683 are 63% similar to a (SYNTHETASE AMINOACYL-TRNA PROTEIN LIGASE BIOSYNTHESIS) protein domain (PD002123) which is seen in SYM_HAEIN.



Paralogs:  Local Blast Search


NG2044 is paralogously related to NG0006 (leucyl-tRNA synthetase) (4e-07), NG0069 (isoleucyl-tRNA synthetase) (3e-06) and NG1993 (cysteinyl-tRNA synthetase) (4e-05).


Pfam Summary:  Pfam Search
Residues 2 to 383 (E-value = 4.9e-05) place NG2044 in the tRNA-synt_1 family which is described as tRNA synthetases class I (I, L, M and V) (PF00133)
Residues 587 to 682 (E-value = 5.5e-33) place NG2044 in the tRNA_bind family which is described as Putative tRNA binding domain (PF01588)

Structural Feature(s):
Feature Type  Start  Stop
uncleavable N-terminal sequence N-terminal sequence  
1  
16

PDB Hit:
pdb|1F4L|1F4L-A CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA 668.0 0.000000
pdb|1QQT|1QQT-A METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI 668.0 0.000000
pdb|1A8H|1A8H METHIONYL-TRNA SYNTHETASE FROM THERMUS 148.0 4e-36
pdb|1MKH|1MKH-A

Gene Protein Sequence:
MTRKILVTSALPYANGSIHLGHMVEHIQTDVWVRFQKLRGHECYYCCADD
THGTPVMLAAQKQGIAPEDMIAKVRKEHLADFTGFFIGYDNYYSTHSTEN
KQFSQDIYRALKANGKIESRVIEQLFDPEKQMFLPDRFVKGECPKCHAQD
QYGDNCEVCGTTYSPTELINPYSAVSGAKPELRESEHFFFKLGECADFLK
AWTSGNNPHDGKPHLQPEALNKMKEWLGEGEETTLSDWDISRDAPYFGFE
IPDAPGKYFYVWLDAPVGYMASFKNLCDRIGIDFDEYFKADSQTEMYHFI
GKDILYFHALFWPAMLHFSGHRAPTGVYAHGFLTVDGQKMSKSRGTFITA
KSYLEQGLNPEWMRYYIAAKLNGKIEDTDLNLQDFISRVNSDLVGKYVNI
AARASGFIAKRFEGRPKDVSGSALLAKLAAESDTIAEQYENREYARALRD
IMALADIVNEYVDANKPWELAKQEGQDERLHEVCSELINAFTMLTAYLAP
VLPQTAANAARFLNLDAITWKNTRETLGEHAINKYEHLMQRVEQKQVDDL
IEANKQSIQTASAPVEEGKYEKVAEQAGFDDFMKIDMRVAKVLNCEAVEG
STKLLKFDLDFGFEKRIIFSGIAASYPNPAELNGRMVIAVANFAPRKMAK
FGVSEGMILSAATADGKLKLLDVDAGAQPGDKVG

Gene Nucleotide Sequence:  Sequence Viewer
ATGACACGCAAAATCTTAGTTACCTCCGCCCTGCCCTATGCCAACGGCAG
CATCCACCTCGGCCACATGGTCGAACACATCCAAACCGACGTTTGGGTGC
GCTTTCAAAAACTGCGCGGCCACGAATGCTACTACTGCTGCGCCGACGAC
ACCCACGGCACGCCCGTTATGCTTGCCGCGCAAAAACAAGGCATCGCGCC
CGAAGACATGATTGCCAAAGTGCGCAAAGAGCACCTTGCCGACTTTACCG
GCTTTTTCATCGGCTACGACAATTATTACAGCACCCATTCCACTGAAAAC
AAACAGTTTTCCCAAGACATTTACCGCGCGCTGAAAGCCAACGGCAAAAT
CGAAAGCCGCGTCATCGAGCAGCTTTTCGACCCCGAAAAACAAATGTTCC
TGCCCGACCGCTTCGTCAAAGGCGAATGCCCGAAATGCCACGCCCAAGAC
CAATACGGCGACAACTGCGAAGTCTGCGGCACGACCTATTCCCCGACCGA
ACTGATCAACCCGTATTCCGCCGTTTCCGGCGCGAAACCCGAATTGCGCG
AATCCGAACACTTCTTCTTCAAACTGGGCGAATGCGCCGACTTCCTCAAA
GCATGGACTTCCGGCAACAACCCGCACGACGGCAAGCCCCATCTGCAACC
CGAAGCCCTCAACAAAATGAAGGAATGGCTGGGCGAAGGCGAAGAAACCA
CCCTGTCCGACTGGGACATTTCCCGCGACGCGCCGTATTTCGGTTTTGAA
ATCCCCGACGCGCCGGGCAAATACTTCTACGTTTGGCTGGACGCGCCCGT
CGGCTATATGGCGTCGTTTAAAAACCTGTGCGACCGCATCGGCATCGATT
TCGACGAATACTTCAAAGCCGACAGCCAAACCGAGATGTACCACTTCATC
GGCAAAGACATCCTCTATTTCCACGCCCTGTTCTGGCCCGCCATGCTGCA
TTTCTCCGGCCACCGCGCCCCGACCGGCGTGTACGCACACGGCTTTTTGA
CCGTGGACGGACAAAAAATGTCCAAATCGCGCGGCACCTTCATCACCGCC
AAATCTTATCTGGAACAAGGCCTGAACCCCGAGTGGATGCGCTACTACAT
CGCCGCCAAGCTCAACGGCAAAATCGAAGACACCGATTTGAACCTGCAAG
ACTTTATTTCCCGCGTCAACAGCGACCTTGTCGGCAAATACGTCAACATC
GCCGCCCGCGCTTCGGGTTTCATCGCCAAACGCTTTGAAGGTCGTCCGAA
AGACGTTTCAGGCAGCGCATTGCTGGCAAAACTCGCCGCCGAAAGCGACA
CCATCGCCGAGCAATACGAAAACCGCGAATACGCCCGCGCCCTGCGCGAC
ATCATGGCATTGGCAGACATTGTCAACGAATACGTCGATGCCAACAAGCC
GTGGGAGCTCGCCAAACAAGAAGGTCAAGACGAACGCCTGCACGAAGTAT
GCAGCGAACTCATCAACGCCTTCACCATGCTGACCGCCTACCTCGCCCCC
GTGTTGCCGCAAACCGCCGCCAACGCCGCGCGTTTCCTCAATCTGGACGC
GATTACCTGGAAGAACACGCGCGAAACCCTAGGCGAACACGCCATCAACA
AATACGAACATTTAATGCAACGAGTGGAGCAAAAACAAGTGGACGATTTG
ATCGAAGCCAACAAACAAAGCATTCAGACGGCATCCGCGCCCGTTGAAGA
GGGTAAATACGAAAAAGTCGCCGAACAGGCGGGCTTCGACGACTTTATGA
AAATCGATATGCGCGTCGCCAAAGTATTGAACTGCGAAGCCGTCGAAGGC
AGCACCAAACTTTTGAAATTCGACCTCGATTTCGGTTTTGAAAAACGCAT
CATCTTCTCCGGCATCGCCGCGTCTTACCCAAATCCTGCCGAATTGAACG
GTCGCATGGTCATCGCAGTCGCCAACTTCGCCCCACGCAAAATGGCAAAA
TTCGGCGTATCCGAAGGTATGATCCTCTCCGCCGCCACGGCAGACGGCAA
ACTGAAGCTGCTTGACGTGGATGCGGGCGCTCAGCCGGGCGACAAAGTCG
GT


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