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Ureaplasma urealyticum Search Results

Record: 1 of 1  
MiniMap tRNA-Trp-2 IGR448 IGR446 IGR449 IGR451 IGR445 IGR450 IGR447 rpL33,rpmG, - UU533 cdd, - UU531 truA,hisT, - UU536 pepP,ampP, - UU532 ABC, - UU538 UU537 manB,cpsG, - UU530 thrS,syt, - UU534 codV, - UU529 UU535 rpL33,rpmG, - UU533 cdd, - UU531 truA,hisT, - UU536 pepP,ampP, - UU532 ABC, - UU538 UU537 manB,cpsG, - UU530 thrS,syt, - UU534 codV, - UU529 UU535 Type: tandem, Name:  - 327 Type: tandem, Name:  - 324 Type: tandem, Name:  - 329 Type: tandem, Name:  - 325 Type: tandem, Name:  - 326 Type: tandem, Name:  - 328 rpL33,rpmG, - UU533 cdd, - UU531 truA,hisT, - UU536 pepP,ampP, - UU532 ABC, - UU538 UU537 manB,cpsG, - UU530 thrS,syt, - UU534 codV, - UU529 UU535
* Calculated from Protein Sequence

Gene ID: UU534

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
thrS  syt  

Definition:
threonyl-tRNA synthetase

Gene Start:
664096

Gene Stop:
662354

Gene Length:
1743

Molecular Weight*:
67743

pI*:
7.30

Net Charge*:
2.39

EC:
6.1.1.3  

Functional Class:
translation; aminoacyl-tRNA synthetases  

Pathway: pathway table
Aminoacyl-tRNA biosynthesis
Glycine, serine and threonine metabolism

Comment:
ThrS is also a translational repressor protein, it controls the
translation of its own gene by binding to its mRNA.

Reaction:
ATP + L-THREONINE + TRNA(THR) = AMP + PYROPHOSPHATE + L-THREONYL-TRNA(THR).

See Prosite PDOC00363.

From Prosite:

Aminoacyl-tRNA synthetases (EC 6.1.1.-) [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 [2 to 6] 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 [7].

[ 1] Schimmel P.
Annu. Rev. Biochem. 56:125-158(1987).
[ 2] Delarue M., Moras D.
BioEssays 15:675-687(1993).
[ 3] Schimmel P.
Trends Biochem. Sci. 16:1-3(1991).
[ 4] Nagel G.M., Doolittle R.F.
Proc. Natl. Acad. Sci. U.S.A. 88:8121-8125(1991).
[ 5] Cusack S., Haertlein M., Leberman R.
Nucleic Acids Res. 19:3489-3498(1991).
[ 6] Cusack S.
Biochimie 75:1077-1081(1993).
[ 7] Cusack S., Berthet-Colominas C., Haertlein M., Nassar N., Leberman R.
Nature 347:249-255(1990).
[ 8] Leveque F., Plateau P., Dessen P., Blanquet S.
Nucleic Acids Res. 18:305-312(1990).

The complete list of predicted and possible tRNA synthetases is: UU062, UU106, UU117, UU123, UU175, UU192, UU197, UU267, UU278, UU285, UU286, UU287, UU365, UU369, UU371, UU410, UU452, UU457, UU458, UU493, UU534, and UU599.

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to threonyl-tRNA synthetase sequences; e.g. residues 6-569 are 47% similar to SYT1_BACSU; residues 15-569 are 41% similar to SYT_MYCGE; and residues 6-573 are 39% similar to SYT_SYNY3. Also similar to: SYT_HELPY, SYT_ECOLI, SYT_HAEIN, SYT_RICPR, SYTC_YEAST, and SYTC_HUMAN.
BLAST reveals significant similarity to MG375, CT581, and TP0837, all of which are threonyl-tRNA synthetases.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0441 is ehgpcmYu.
Cog name: Threonyl-tRNA synthetase.
Functional class: J.
BeTs to -hg-cmyu.
Number of proteins in this genome belonging to this COG is 2



Blocks Summary:  Blocks Search
Residues 116-543 are in the 100th percentile of similarity to blocks PD01035A-F (SYNTHETASE LIGASE THREONYL-TRNA.)

ProDom Summary:  Protein Domain Search
Residues 180-376 are 49% similar, and residues 6-135 are 44% similar to a defined domain of SYT1_BACSU, a tRNA synthetase.
Residues 404-459 are 64% similar to a defined domain of SYT_MYCPN.

Paralogs:  Local Blast Search
No evidence of paralogs in U.u.

Pfam Summary:  Pfam Search
Residues 199 to 353 (E-value = 1.1e-36) place UU534 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T) (PF00587)
Residues 483 to 575 (E-value = 7.8e-26) place UU534 in the HGTP_anticodon family which is described as Anticodon binding domain (PF03129)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
162  
189
coil-coil  
498  
531

PDB Hit:
gi|5107656|pdb|1QF6|A Chain A, Structure Of E. Coli Threonyl-Trna Synthetase Complexed With Its Cognate Trna

Gene Protein Sequence:
MYKFDQKLNHSAAHLLAMALTKFYPNLSLAIGPTIDEGFYYDFNLNDPNT
SITPLDLLKIEKEMKKITTQALTFDYEQVTYEKAKELFKHNKYKLDIIEQ
NKNNSLSIYHSGKWFDLCKGPHVQNTKEIKAIKLLNIAGSYWRGDANNDQ
LIRIYGVAFSDQDQLDAYLKDLQERKERDHRKIGKDLNLFTFNNLAGQGL
PIWLPNGTIIKNQVQKFINEVEFQFNFDTVITPILGSIDLYKTSGHWDHY
KDNIFSPVQIDNEILVLRPMTCPHHTLVYSNELRSYRSLPIRLSEHSILH
RYESSGGLTGFERVREMILEDCHVFCRFDQIEHEVINAFKMIQEAQEGLG
IKTFEIHLSLNDPNDKEKYYDDPQMWEQSQNVLRKMLKDHNIPYKEMVGE
AAFYGPKIDFQVKTVLNRIITVSTIQLDFLLPNRFNLTYINESNEQSVPV
MIHIGIIGTYERLLAILLEQTKGILPLWLSPIQVVIIPVNENLHTDYVKE
LNIKLRKHLIRSNVDLRNERLSKKIREAQIQKIPYQIVIGDEEIKNNKMV
TYRCYGSEKTTTVSITDFINMLENKIRLKK$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTATAAGTTTGATCAAAAACTAAATCACAGTGCTGCACATCTTTTAGC
AATGGCACTAACAAAATTTTATCCTAACTTAAGCCTTGCGATTGGGCCAA
CGATTGATGAGGGGTTTTATTATGATTTTAATCTAAATGATCCAAATACC
TCAATTACCCCTTTAGATTTATTAAAAATTGAAAAAGAAATGAAGAAAAT
TACTACTCAAGCTTTAACGTTTGATTATGAACAAGTTACTTATGAAAAAG
CAAAGGAATTGTTTAAACACAATAAATATAAATTAGATATTATTGAACAA
AATAAAAATAATTCACTTTCAATTTATCACTCAGGTAAATGGTTTGACTT
ATGTAAAGGCCCGCATGTACAAAACACAAAAGAGATCAAGGCAATTAAAT
TATTAAATATTGCAGGTTCATATTGACGAGGTGATGCAAATAATGATCAA
TTAATTCGTATTTATGGGGTTGCTTTTAGTGATCAAGATCAATTAGACGC
TTATTTAAAAGATTTACAAGAACGAAAAGAACGTGATCATCGTAAAATTG
GTAAAGATTTAAACTTATTTACTTTTAATAATCTAGCAGGCCAAGGATTA
CCAATTTGATTACCTAATGGAACCATTATTAAAAATCAGGTACAAAAGTT
TATTAATGAAGTTGAATTTCAATTTAATTTTGATACTGTTATTACGCCTA
TATTAGGTAGTATAGATTTATATAAAACGAGTGGACACTGAGATCATTAT
AAAGATAATATTTTTTCACCAGTACAAATTGATAATGAAATCTTAGTACT
TCGTCCAATGACATGTCCTCATCATACATTAGTTTACTCTAATGAACTTC
GTTCATATCGAAGTTTACCAATTCGTTTAAGTGAACATTCAATTTTACAT
CGTTATGAATCATCAGGTGGATTAACAGGCTTTGAGCGGGTTCGTGAGAT
GATTTTAGAAGATTGTCATGTTTTTTGTCGCTTTGATCAAATTGAACATG
AAGTTATTAATGCTTTTAAAATGATTCAAGAAGCTCAAGAAGGATTGGGT
ATTAAAACATTTGAAATTCATTTATCTTTAAATGATCCTAATGATAAAGA
AAAATATTATGATGATCCTCAAATGTGAGAACAATCACAAAATGTGTTAC
GTAAAATGTTAAAAGATCACAATATTCCTTATAAGGAGATGGTAGGAGAA
GCGGCATTTTATGGTCCAAAAATCGATTTTCAGGTTAAAACTGTTTTAAA
TCGAATTATTACAGTTTCAACTATCCAATTAGATTTTTTATTACCAAACC
GTTTTAATTTAACTTATATTAATGAAAGTAATGAACAAAGCGTACCGGTA
ATGATTCATATTGGTATTATTGGAACTTATGAACGTTTATTAGCAATTTT
ATTAGAACAAACTAAAGGTATTTTACCGCTTTGATTATCACCTATTCAAG
TAGTTATCATTCCTGTTAATGAAAATTTACATACTGATTATGTAAAGGAG
CTAAATATTAAGTTAAGAAAGCATTTAATTCGTAGTAATGTAGATTTACG
TAATGAGCGTTTATCAAAAAAAATTCGTGAAGCTCAAATTCAAAAAATCC
CTTATCAAATTGTTATTGGTGATGAAGAAATTAAAAACAACAAAATGGTT
ACTTACCGTTGCTATGGTAGTGAAAAAACGACAACAGTTTCTATTACAGA
TTTTATAAATATGTTAGAAAACAAGATTAGATTAAAAAAATAA


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