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Mycoplasma genitalium Search Results

Record: 1 of 1  
MiniMap IGR28 IGR27 IGR29 IGR26 tdk, - MG034 glpK, - MG038 glpF, - MG033 aspS, - MG036 MG040 MG032 tdk, - MG034 glpK, - MG038 glpF, - MG033 aspS, - MG036 MG040 MG032 tdk, - MG034 glpK, - MG038 glpA, - MG039 glpA, - MG039 glpF, - MG033 aspS, - MG036 MG040 MG032 hisS, - MG035 pbeF, - MG037 hisS, - MG035 pbeF, - MG037
* Calculated from Protein Sequence

Gene ID: MG036

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
aspS  

Definition:
aspartyl-tRNA synthetase

Gene Start:
41777

Gene Stop:
43426

Gene Length:
1650

Molecular Weight*:
64228

pI*:
9.54

Net Charge*:
12.17

EC:
6.1.1.12  

Functional Class:
Translation; Aminoacyl-tRNA synthetases  

Pathway: pathway table
Amino Acid Metabolism; Alanine and Aspartate metabolism
Metabolism of Macromolecules; Aminoacyl-tRNA biosynthesis

Comment:
See Prosite PDOC00363.

From Prosite:

Aminoacyl-tRNA synthetases (EC 6.1.1.-) are a group of enzymes which activate amino acids and transfer them to specific tRNA molecules as the first step in protein biosynthesis. In prokaryotic organisms there are at least twenty different types of aminoacyl-tRNA synthetases, one for each different amino acid. In eukaryotes there are generally two aminoacyl-tRNA synthetases for each different amino acid: one cytosolic form and a mitochondrial form. While all these enzymes have a common function, they are widely diverse in terms of subunit size and of quaternary structure.

The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine are referred to as class-II synthetases and probably have a common folding pattern in their catalytic domain for the binding of ATP and amino acid which is different to the Rossmann fold observed for the class I synthetases.


Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to aspartyl-tRNA synthetase sequences, e.g.
residues 2-550 are 66% similar to SYD_MYCPN.
MG036 is similar to T.pallidum TP0985(aspartyl-tRNA synthetase),
, it also shows weak similarity to TP1040(lysyl-tRNA synthetase)
and TP0609(asparaginyl-tRNA synthetase). It is also similar to
C.trachomatis aspartyl-tRNA synthetase and lysyl-tRNA synthetase
sequences CT542 and CT781.


COGS Summary:  COGS Search
The phylogenetic pattern of COG0173 is ehgpc-y.
COG name: Aspartyl-tRNA synthetase.
Functional Class: J
BeTs to h,g,c,y.

Blocks Summary:  Blocks Search
Residues 448-472 are member of block BL01272C(Glucokinase regulatory
protein family proteins).

ProDom Summary:  Protein Domain Search
Residues 1-94, 133-448, 449-519 constitute defined domains of
SYD_MYCGE.
Residues 464-479 are 56% similar to a lysyl-tRNA domain
from SYK_MYCHO.

Paralogs:  Local Blast Search
MG036 is paralogously related to MG136(lysyl-tRNA synthetase),
MG113(asparaginyl-tRNA synthetase): residues 13-521 are 23% similar to
to MG136 and residues 18-521 are 22% similar to MG113.

Pfam Summary:  Pfam Search
Residues 21 to 91 (E-value = 4.5e-13) place MG036 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain (PF01336)
Residues 108 to 524 (E-value = 3.2e-14) place MG036 in the tRNA-synt_2 family which is described as tRNA synthetases class II (D, K and N) (PF00152)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
85

PDB Hit:
gi|1311301|pdb|1LYL|A Chain A, Lysyl-Trna Synthetase (Lysu) (E.C.6.1.1.6) Complexed With Lysine Mol_id: 1; Molecule: Lysyl-Trna Synthetase (Lysu); Chain: A, B, C; Ec: 6.1.1.6; Mol_id: 2; Molecule: Lysine; Chain: X, Y, Z

Gene Protein Sequence:
MCFNQRILIGSISTEQLNKTIVIIGWIKRIKKLGEINFIIVGDKSGTIQV
TCKDKEQIQQLTREDIVIVKAKLQRLDSVRFELINPTIKLFSKSKTPPLI
IEDETDALEEVRLKYRYLDLRRRLMQKRLLLRHQFILAIRNWFNQQGFIE
IETPTLSKSTPEGAQDFLVPARIRKDCFYALVQSPQIYKQLLMIAGVEKY
FQIARVYRDEDSRKDRQPEHTQIDFEISFCNQKMIMNLVEKLFFSVFLDV
FQIKIKKTFPVFKFSELFERFGSDKPDLRYGFEIKDFTSLFQDHQNQFTK
LIEAKGIIGGIELTNIELSTDKIKALRKIAKDHDVSLEVHNKNNSTLKTS
IKCDEKNTLLLVANKSKKKAWTALGAIRNELKYHLDIVKPNQYSFCWVVD
FPLYDFDEKTNQWISNHNIFSKPKQEWIDNFESNKNEALSEQFDLVLNGF
EIGSGSIRINDPIVQKRLMNSLNIDPNKFAFLLEAYQYGAPVHGGMGLGI
DRLMMILNQTDNIREVIAFPKNNHGIEVHTNAPDKIDKEEVKWWIKELVK


Gene Nucleotide Sequence:  Sequence Viewer
ATGTGTTTTAACCAACGAATTTTAATTGGCTCAATTTCAACTGAACAACT
CAATAAAACAATAGTTATTATTGGGTGAATTAAACGGATTAAAAAGTTAG
GTGAAATTAACTTTATTATCGTTGGTGATAAATCAGGAACTATCCAAGTA
ACTTGCAAAGATAAAGAACAGATTCAACAACTTACAAGAGAAGACATAGT
TATTGTTAAAGCCAAATTACAACGCTTAGATAGTGTTAGATTTGAACTGA
TAAATCCAACTATTAAACTTTTTTCAAAGTCAAAAACTCCTCCTTTAATT
ATTGAAGATGAAACTGATGCTTTAGAAGAAGTTAGGTTAAAATACCGTTA
CCTTGATCTGAGAAGACGTTTGATGCAAAAACGATTGTTATTGCGTCATC
AATTTATATTAGCAATTCGTAACTGATTTAACCAGCAGGGTTTTATTGAA
ATAGAAACACCTACCTTATCCAAATCAACTCCTGAGGGAGCACAAGACTT
TTTAGTTCCTGCAAGAATTAGAAAAGATTGTTTTTATGCTTTAGTTCAAA
GTCCACAAATCTATAAGCAGCTCTTAATGATTGCAGGAGTTGAAAAATAT
TTTCAAATTGCAAGGGTCTATCGTGATGAAGATAGCAGAAAAGATCGTCA
ACCAGAACACACACAAATTGATTTCGAGATCTCTTTTTGTAACCAAAAAA
TGATTATGAATCTAGTTGAAAAACTCTTTTTTAGTGTTTTCTTAGATGTT
TTTCAAATCAAAATAAAAAAGACTTTTCCTGTTTTTAAATTTTCAGAACT
TTTTGAAAGATTTGGTAGCGATAAACCAGATTTACGTTATGGTTTTGAAA
TAAAAGATTTCACCTCGCTTTTTCAAGATCATCAGAATCAGTTCACTAAA
TTAATTGAAGCAAAAGGCATTATTGGTGGTATTGAACTTACTAATATTGA
GTTAAGTACAGACAAAATTAAAGCATTAAGAAAAATTGCTAAGGACCATG
ATGTGAGTTTAGAAGTTCATAATAAAAATAATTCAACATTAAAAACTTCA
ATTAAATGTGATGAAAAAAACACTCTTCTGTTAGTAGCAAATAAATCTAA
AAAGAAGGCATGAACTGCTTTAGGAGCAATTAGAAATGAGTTGAAATACC
ACTTGGATATTGTCAAACCTAACCAATACAGCTTTTGTTGAGTTGTTGAT
TTCCCTCTCTATGATTTTGATGAGAAAACAAATCAGTGAATATCAAATCA
CAACATCTTTTCAAAACCTAAACAAGAATGAATTGATAATTTTGAATCAA
ATAAAAACGAAGCATTAAGCGAACAGTTTGATCTTGTTTTAAATGGTTTT
GAAATTGGTAGTGGTTCAATAAGAATTAATGATCCAATTGTTCAAAAAAG
ACTAATGAATTCTTTGAACATTGACCCAAATAAGTTTGCTTTTCTTCTAG
AAGCTTATCAATATGGTGCTCCTGTTCATGGTGGAATGGGACTAGGTATT
GATCGTTTAATGATGATTCTTAATCAAACTGATAACATCAGAGAAGTAAT
CGCTTTTCCTAAGAATAATCATGGTATTGAAGTCCATACAAACGCTCCTG
ATAAAATTGACAAAGAGGAGGTTAAATGATGGATAAAAGAACTAGTGAAA



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