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Mycoplasma genitalium Search Results

Record: 1 of 1  
MiniMap IGR28 IGR27 IGR25 IGR26 tdk, - MG034 glpK, - MG038 polC,polC-1, - MG031 glpF, - MG033 aspS, - MG036 MG032 tdk, - MG034 glpK, - MG038 polC,polC-1, - MG031 glpF, - MG033 aspS, - MG036 MG032 tdk, - MG034 glpK, - MG038 polC,polC-1, - MG031 glpF, - MG033 aspS, - MG036 MG032 hisS, - MG035 pbeF, - MG037 hisS, - MG035 pbeF, - MG037
* Calculated from Protein Sequence

Gene ID: MG035

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
hisS  

Definition:
histidyl-tRNA synthetase

Gene Start:
40543

Gene Stop:
41784

Gene Length:
1242

Molecular Weight*:
48312

pI*:
8.88

Net Charge*:
6.23

EC:
6.1.1.21  

Functional Class:
Translation; Aminoacyl-tRNA synthetases  

Pathway: pathway table
Amino Acid Metabolism; Histidine metabolism
Metabolism of Macromolecules; Aminoacyl-tRNA biosynthesis

Comment:
In HAEIN, the his-tRNA synthetase appears to be a homodimer.

Reaction:
ATP + L-HISTIDINE + TRNA(HIS) = AMP + PYROPHOSPHATE + L-HISTIDYL-TRNA(HIS).

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 histidyl-tRNA synthetase sequences,
e.g. residues 1-413 are 60% similar to SYH_MYCPN.
MG035 is similar to T.pallidum TP0641, predicted histidyl-tRNA
synthetase.It is also similar to C.trachomatis histidyl-tRNA
synthetase sequences CT543.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0124 is ehgpcmy.
COG name: Histidyl-tRNA synthetase.
Functional Class: J
BeTs to h,g,c,m,y.

Blocks Summary:  Blocks Search
NONE.

ProDom Summary:  Protein Domain Search
Residues 24-95, 96-190, 155-393, 191-312, 313-414 constitute
defined domains of SYH_MYCGE.
Residues 187-312 are 31% similar to a hypothetical 38.0 KD protein
of YH13_LACLA.

Paralogs:  Local Blast Search
No evidence of paralogs in M.genitalium.

Pfam Summary:  Pfam Search
Residues 9 to 159 (E-value = 2.2e-40) place MG035 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T) (PF00587)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
133  
164

PDB Hit:
gi|1942448|pdb|1HTT|A Chain A, Histidyl-Trna Synthetase Complex (Trna SynthetaseHIS-Adenylate), Aminoacyl-Trna Synthase, Ligase, Synthetase Mol_id: 1; Molecule: Histidyl-Trna Synthetase; Chain: A, B, C, D; Synonym: Histidine-Trna Ligase; Ec: 6.1.1.21; Eng

Gene Protein Sequence:
MNFLQKPRGVKDWFGDELVYFNWIVKKIRSLAFNWGFSEVKTPLFENAQL
FQRSNANADIVQKELYQFFDKSQRELALRPEATTPIVRLACENKLMQEAN
FPLKLFCIGSMYRYERPQNNRFREHWQFSCEVFGFSNLFIFLDTLLFANS
LLEALGITGYVLKINNLANFETLSKWNKALKDYLTPYKLELTELSQKRLE
KNPLRILDDKIDQKKSFVKNAPKITDFLDASAKQDSELLKTQLKKHNISF
EWTDNLVRGLDYYTGFVFEYVKNQDTILAGGVYDNLVEELSSNPTPALGF
ACGIERLINCLEIDKKAFILNTKPKQMLVICLFEEALEELVWLAKLWREY
NQVTIYPKVIKVDNGIRLANRLGYTFIGIVGKTDFDKKAITIKNLVSKQQ
TIYTWNELGERNVF

Gene Nucleotide Sequence:  Sequence Viewer
ATGAACTTCTTGCAAAAACCAAGGGGAGTTAAAGATTGGTTTGGTGATGA
ATTAGTTTATTTTAATTGGATTGTTAAAAAAATAAGATCTTTAGCATTTA
ATTGGGGTTTTAGTGAAGTTAAAACTCCGTTGTTTGAAAATGCACAACTT
TTTCAAAGATCTAATGCTAATGCTGATATTGTTCAAAAAGAACTATACCA
GTTTTTTGATAAATCTCAAAGAGAATTAGCTTTAAGACCTGAAGCTACTA
CACCAATAGTAAGACTTGCTTGTGAAAACAAATTAATGCAAGAAGCAAAT
TTTCCCTTAAAGTTATTTTGCATTGGTTCAATGTATCGTTATGAACGTCC
ACAAAACAATAGGTTTCGTGAACATTGGCAATTTAGTTGCGAAGTATTTG
GTTTTTCCAACCTGTTTATCTTTTTAGATACACTTTTGTTTGCTAACTCT
TTGCTTGAAGCACTTGGAATTACTGGATATGTGCTTAAAATTAATAATCT
TGCTAACTTTGAAACACTTAGTAAGTGAAATAAAGCCCTAAAAGATTATT
TAACTCCATATAAATTAGAACTAACTGAGCTTTCTCAAAAAAGATTAGAA
AAAAATCCTTTGAGAATTTTAGATGACAAGATAGATCAAAAAAAATCATT
TGTTAAAAATGCTCCTAAAATTACTGATTTTTTAGATGCAAGTGCAAAAC
AAGATTCAGAATTGTTAAAAACACAACTAAAAAAACACAATATTAGTTTT
GAATGAACAGACAATCTAGTTAGAGGATTGGATTACTATACTGGATTTGT
GTTTGAATATGTAAAAAATCAAGACACAATTTTAGCAGGTGGAGTTTATG
ATAACTTAGTTGAAGAATTAAGTAGTAATCCAACTCCCGCATTAGGTTTT
GCTTGTGGAATTGAACGGTTAATTAACTGTTTAGAAATTGATAAAAAAGC
ATTTATTTTGAATACTAAACCAAAGCAGATGTTAGTAATTTGCTTATTTG
AAGAAGCGCTTGAAGAATTGGTTTGACTAGCTAAATTATGAAGGGAATAT
AACCAAGTAACTATTTATCCTAAGGTTATTAAAGTTGATAATGGGATTAG
ATTAGCAAATCGCTTGGGTTATACTTTCATTGGCATTGTTGGAAAAACTG
ATTTTGACAAAAAAGCTATTACAATCAAAAACTTAGTATCTAAACAACAG
ACCATTTACACTTGAAATGAACTTGGAGAACGAAATGTGTTT


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