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

Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR1330 IGR1323 IGR1331 IGR1326 IGR1324 IGR1332 IGR1325 IGR1327 IGR1328 IGR1329 rpL35,rpmI, - HD1800 HD1798 rpL20, - HD1799 infC, - HD1802 HD1805 purA, - HD1807 thiI, - HD1806 thrS, - HD1803 HD1795 HD1804 HD1797 rpL35,rpmI, - HD1800 HD1798 rpL20, - HD1799 infC, - HD1802 HD1805 purA, - HD1807 thiI, - HD1806 thrS, - HD1803 HD1795 HD1804 HD1797 rpL20, - HD1799 infC, - HD1802 HD1805 purA, - HD1807 thiI, - HD1806 thrS, - HD1803 rpL35,rpmI, - HD1800 HD1798 HD1804 HD1797 HD1796 HD1795 HD1796
* Calculated from Protein Sequence

Gene ID: HD1803

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
thrS  

Definition:
threonyl-tRNA synthetase (thrS)

Gene Start:
1509172

Gene Stop:
1507241

Gene Length:
1932

Molecular Weight*:
73644

pI*:
6.30

Net Charge*:
-7.87

EC:
6.1.1.3  

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

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

Secondary Evidence:
Mayaux,J.F., Fayat,G., Fromant,M., Springer,M., Grunberg-Manago,M.
and Blanquet,S.
Structural and transcriptional evidence for related thrS and infC
expression
Proc. Natl. Acad. Sci. U.S.A. 80 (20), 6152-6156 (1983)
Medline: 84016012

Springer,M., Graffe,M., Butler,J.S. and Grunberg-Manago,M.
Genetic definition of the translational operator of the
threonine-tRNA ligase gene in Escherichia coli
Proc. Natl. Acad. Sci. U.S.A. 83 (12), 4384-4388 (1986)
Medline: 86233434

Sankaranarayanan,R., Dock-Bregeon,A.C., Romby,P., Caillet,J.,
Springer,M., Rees,B., Ehresmann,C., Ehresmann,B. and Moras,D.
The structure of threonyl-tRNA synthetase-tRNA(Thr) complex
enlightens its repressor activity and reveals an essential zinc ion in the active site
Cell 97 (3), 371-381 (1999)
Medline: 99251535

Sankaranarayanan,R., Dock-Bregeon,A.C., Rees,B., Bovee,M.,
Caillet,J., Romby,P., Francklyn,C.S. and Moras,D.
Zinc ion mediated amino acid discrimination by threonyl-tRNA
synthetase
Nat. Struct. Biol. 7 (6), 461-465 (2000)
Medline: 20343005



Comment:


Blast Summary:  PSI-Blast Search
Numerous hits to threonyl-tRNA synthetases with gapped BLAST; e.g residues 1-642 are 89% similar to threonyl-tRNA synthetase (U32816) of Haemophilus influenzae, residues 1-642 are 75% similar to threonyl-tRNA synthetase (AE000267) of E. coli, residues 4-632 are 59% similar to putative threonyl-tRNA synthetase (AL162754) of Neisseria meningitidis.

COGS Summary:  COGS Search
BeTs to 17 clades of COG0441
COG name: Threonyl-tRNA synthetase
Functional Class: J
The phylogenetic pattern of COG0441 is amtkYqVceBrhujgpoLinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
No significant hits to the Blocks database.

ProDom Summary:  Protein Domain Search
Residues 508-611 are 91% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA BIOSYNTHESIS) protein domain (PD000606) which is seen in SYT_HAEIN.

Residues 260-326 are 97% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA BIOSYNTHESIS) protein domain (PD004144) which is seen in SYT_HAEIN.

Residues 73-204 are 53% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ALANYL-TRNA) protein domain (PD001534) which is seen in Q9I099_PSEAE.

Residues 127-205 are 44% similar to a (LIGASE SYNTHETASE ATP-BINDING) protein domain (PD120616) which is seen in SYT_BUCAI.

Residues 454-507 are 90% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING) protein domain (PD002782) which is seen in SYT_HAEIN.

Residues 139-205 are 71% similar to a (SYNTHETASE LIGASE ATP-BINDING BIOSYNTHESIS) protein domain (PD190155) which is seen in SYT_ECOLI.

Residues 4-68 are 87% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD006784) which is seen in SYT_HAEIN.

Residues 211-253 are 95% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD351577) which is seen in SYT_PASMU.

Residues 71-124 are 90% similar to a (SYNTHETASE LIGASE BIOSYNTHESIS) protein domain (PD379309) which is seen in SYT_HAEIN.

Residues 321-408 are 55% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD276857) which is seen in Q9VKB0_DROME.

Residues 345-436 are 93% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA BIOSYNTHESIS) protein domain (PD000380) which is seen in SYT_PASMU.



Paralogs:  Local Blast Search


HD1803 is paralogously related to HD1919 (2e-09).


Pfam Summary:  Pfam Search
Residues 1 to 61 (E-value = 6.7e-13) place HD1803 in the TGS family which is described as TGS domain (PF02824)
Residues 262 to 415 (E-value = 2.8e-59) place HD1803 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T) (PF00587)
Residues 541 to 631 (E-value = 2e-29) place HD1803 in the HGTP_anticodon family which is described as Anticodon binding domain (PF03129)

PDB Hit:
pdb|1QF6|A Chain A, Structure Of E. Coli Threonyl-Trna Syntheta... 1047 0.0
pdb|1EVK|A Chain A, Crystal Structure Of A Truncated Form Of Th... 664 0.0
pdb|1QF6|A Chain A, Structure Of E. Coli Threonyl-Trna Syntheta... 1248 0.0

Gene Protein Sequence:
MPIITLPDGSQRNFDNPVSVIEVAQSIGTGLAKATIAGRVNGERRDACDI
IEQDSTLEIITAKDEDGLEIIRHSCAHLLGHAIKQLFPTVKMAIGPTIEN
GFYYDVDLDRTLTQDDLEAIEKRMLELAKTNYNVVKKPVSWQQARDTFEK
RGEPYKIAILDENIERTATPALYHHEEYIDMCRGPHVPNMRFCQHFKLQK
VAGAYWRGDSKNKMLQRIYGTAWADKKQLTEYLTRLEEAAKRDHRRIGKA
LDLYHMQEEAPGMVFWHNDGWTIFRELETFVRTKLKEYDYQEVKGPFMMD
RVLWERTGHWQNYADLMFTTQSENREYAIKPMNCPGHVQIFNQGLKSYRD
LPIRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEEQIESEVTAC
IKMVYDIYSTFGFTNIFVKLSTRPDNRIGADDMWDRAEAGLSAALSANGL
EYQIQHGEGAFYGPKIEFALRDCLGREWQCGTVQLDFALPSRLDASYVTE
DNSRHTPVMIHRAILGSIERFIGIITEEYAGFFPVWLAPIQAVVMNITDS
QADYVQQVVKQLSDAGLRVKADLRNEKVGFKVREHTLRRVPYMLVCGDKE
ITEGKVSVRTRKGEDLGTFNIEAFVEMLKAQVKTRELKLLGEA$

Gene Nucleotide Sequence:  Sequence Viewer
ATGCCTATTATAACTTTACCAGATGGTTCTCAACGCAACTTTGATAATCC
GGTTTCTGTCATAGAAGTTGCACAAAGTATTGGTACAGGCTTAGCAAAAG
CGACTATTGCGGGGCGTGTAAATGGCGAGCGCCGAGATGCTTGTGATATT
ATTGAACAGGATAGCACGCTTGAAATTATTACCGCTAAAGATGAAGATGG
TTTAGAAATTATTCGCCACTCTTGTGCTCATTTACTTGGTCACGCGATCA
AACAGTTATTTCCTACGGTAAAAATGGCGATCGGCCCAACGATCGAAAAT
GGCTTTTACTATGATGTAGATTTAGATCGTACTTTAACACAAGACGATTT
AGAAGCGATTGAAAAACGTATGTTGGAATTAGCTAAAACTAACTACAATG
TCGTGAAAAAACCAGTAAGTTGGCAACAAGCACGCGATACATTCGAAAAG
CGTGGTGAACCATATAAAATAGCTATTTTAGATGAGAATATTGAACGTAC
AGCAACGCCAGCACTTTATCATCATGAAGAATATATTGATATGTGCCGTG
GTCCACACGTACCCAATATGCGCTTTTGCCAACATTTCAAATTACAAAAA
GTAGCAGGTGCTTATTGGCGTGGCGACAGCAAAAATAAAATGTTGCAACG
TATTTATGGTACCGCTTGGGCAGATAAAAAACAATTAACGGAATATTTGA
CTCGCTTAGAAGAAGCCGCAAAACGTGATCATCGTCGGATTGGTAAAGCA
TTAGATTTATATCATATGCAGGAAGAAGCACCGGGTATGGTGTTTTGGCA
TAATGATGGTTGGACTATTTTCCGTGAGTTAGAAACATTTGTACGCACTA
AATTAAAAGAGTATGACTATCAAGAAGTTAAAGGTCCATTTATGATGGAT
CGTGTACTCTGGGAACGTACTGGACATTGGCAAAATTATGCTGATTTAAT
GTTTACTACACAGTCCGAAAACCGTGAATATGCGATTAAACCAATGAATT
GCCCAGGGCATGTGCAGATTTTCAATCAAGGGTTAAAATCATATCGAGAC
TTGCCAATTCGTATGGCAGAATTCGGTTCTTGTCACCGTAATGAGCCTTC
AGGATCGCTACATGGCTTAATGCGAGTCCGCGGTTTTACACAAGATGATG
CCCATATTTTCTGTACCGAAGAGCAAATTGAAAGTGAAGTGACCGCTTGT
ATTAAAATGGTGTATGACATTTACAGTACCTTTGGTTTTACGAATATCTT
TGTTAAGCTTTCCACGCGACCAGATAATCGTATTGGCGCAGATGATATGT
GGGATCGTGCGGAAGCGGGCCTTTCAGCGGCATTAAGTGCTAATGGTTTA
GAATATCAAATTCAGCACGGTGAAGGGGCATTTTATGGTCCAAAAATTGA
ATTTGCATTACGCGATTGTTTAGGGCGTGAATGGCAATGTGGTACTGTAC
AACTTGATTTTGCATTGCCAAGTCGTTTAGATGCTTCTTATGTTACAGAA
GATAATAGTCGCCATACACCGGTTATGATCCATCGAGCTATTTTAGGCTC
AATTGAACGCTTTATAGGTATTATTACAGAAGAATATGCGGGCTTCTTCC
CTGTGTGGTTAGCGCCAATACAAGCAGTGGTCATGAATATCACCGATAGC
CAAGCGGATTATGTGCAGCAAGTGGTTAAACAGTTGTCAGATGCGGGCTT
ACGTGTTAAAGCAGATTTACGCAATGAAAAAGTCGGCTTTAAAGTTCGTG
AACATACCTTACGGCGTGTGCCTTATATGCTAGTGTGTGGCGATAAAGAA
ATTACTGAAGGTAAAGTATCCGTACGTACGCGTAAAGGCGAGGATTTAGG
CACTTTCAATATAGAAGCGTTTGTTGAAATGCTTAAAGCACAAGTAAAAA
CACGTGAACTTAAATTATTAGGCGAAGCGTAA


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