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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR418 IGR414 IGR422 IGR421 IGR413 IGR416 IGR417 IGR415 IGR419 IGR420 HD0592 datP, - HD0598 HD0595 ruvC, - HD0593 lemA, - HD0591 HD0596 ygcG, - HD0589 HD0600 aspS, - HD0599 HD0597 dksA, - HD0603 tbpA, - HD0601 pcnB, - HD0604 HD0592 datP, - HD0598 HD0595 ruvC, - HD0593 lemA, - HD0591 HD0596 ygcG, - HD0589 HD0600 aspS, - HD0599 HD0597 dksA, - HD0603 tbpA, - HD0601 pcnB, - HD0604 datP, - HD0598 HD0595 ruvC, - HD0593 lemA, - HD0591 HD0596 HD0600 aspS, - HD0599 HD0590 ygcG, - HD0589 HD0592 HD0590 HD0597 dksA, - HD0603 tbpA, - HD0601 pcnB, - HD0604 HD0602 HD0602
* Calculated from Protein Sequence

Gene ID: HD0599

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
aspS  

Definition:
aspartyl-tRNA synthetase, aspS

Gene Start:
460677

Gene Stop:
458908

Gene Length:
1770

Molecular Weight*:
66702

pI*:
5.20

Net Charge*:
-13.48

EC:
6.1.1.12  

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

Pathway: pathway table
Alanine and aspartate metabolism
Aminoacyl-tRNA biosynthesis

Secondary Evidence:
Eriani,G., Dirheimer,G. and Gangloff,J.
Aspartyl-tRNA synthetase from Escherichia coli: cloning and
characterisation of the gene, homologies of its translated amino
acid sequence with asparaginyl- and lysyl-tRNA synthetases
Nucleic Acids Res. 18 (23), 7109-7118 (1990)
Medline: 91088291

Sharples,G.J. and Lloyd,R.G.
Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12
Mutat. Res. 264 (3), 93-96 (1991)
Medline: 92049526

Eiler,S., Dock-Bregeon,A., Moulinier,L., Thierry,J.C. and Moras,D.
Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of
the second step
EMBO J. 18 (22), 6532-6541 (1999)
Medline: 20031664

Rees,B., Webster,G., Delarue,M., Boeglin,M. and Moras,D.
Aspartyl tRNA-synthetase from Escherichia coli: flexibility and
adaptability to the substrates
J. Mol. Biol. 299 (5), 1157-1164 (2000)
Medline: 20334687




Comment:


Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to aspartyl-tRNA synthetase protein; e.g. residues 1-582 are 79% similar to aspartyl-tRNA synthetase in Haemophilus influenzae strain Rd KW20 (1174503|).

Residues 2-589 are 72% similar to aspartyl-tRNA synthetase in Escherichia coli (135102|).

COGS Summary:  COGS Search
BeTs to 13 clades of COG0173
COG name: Aspartyl-tRNA synthetase
Functional Class: J
The phylogenetic pattern of COG0173 is ----yqvcebrhujgpolinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB002106 (Aminoacyl-transfer RNA synthetases class-II) with a combined E-value of 7.4e-08.
    IPB002106A    152-164
    IPB002106B    535-549


ProDom Summary:  Protein Domain Search
Residues 8-132 are 44% similar to a (SYNTHETASE LIGASE ASPARTYL-TRNA) protein domain (PD228079) which is seen in SYD_BUCAP.

Residues 2-35 are 70% similar to a (SYNTHETASE LIGASE ATP-BINDING) protein domain (PD204502) which is seen in SYD_HAEIN.

Residues 472-518 are 91% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD006889) which is seen in SYD_PASMU.

Residues 208-276 are 79% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING) protein domain (PD000871) which is seen in SYD_PASMU.

Residues 36-131 are 63% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD017062) which is seen in SYD_HAEIN.

Residues 381-467 are 48% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD190340) which is seen in Q9KDG1_BACHD.

Residues 277-369 are 40% similar to a (SYNTHETASE LIGASE ATP-BINDING) protein domain (PD291007) which is seen in SYD_BUCAI.

Residues 519-558 are 97% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA BIOSYNTHESIS) protein domain (PD000848) which is seen in SYD_HAEIN.

Residues 135-206 are 95% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD330536) which is seen in SYD_PASMU.

Residues 14-131 are 65% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD190154) which is seen in SYD_PASMU.

Residues 373-467 are 73% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD206474) which is seen in SYD_HAEIN.

Residues 277-372 are 73% similar to a (SYNTHETASE LIGASE ASPARTYL-TRNA) protein domain (PD037346) which is seen in SYD_PASMU.

Residues 17-131 are 49% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA) protein domain (PD381092) which is seen in SYD_MYCTU.



Paralogs:  Local Blast Search


HD0599 is paralogously related to HD1318 (1e-14), HD1411 (2e-09) and HD0029 (2e-06).


Pfam Summary:  Pfam Search
Residues 19 to 103 (E-value = 2.9e-21) place HD0599 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain (PF01336)
Residues 118 to 560 (E-value = 4.4e-16) place HD0599 in the tRNA-synt_2 family which is described as tRNA synthetases class II (D, K and N) (PF00152)
Residues 308 to 407 (E-value = 3.1e-47) place HD0599 in the GAD family which is described as GAD domain (PF02938)

PDB Hit:
pdb|1EQR|A Chain A, Crystal Structure Of Free Aspartyl-Trna Syn... 875 0.0
pdb|1C0A|A Chain A, Crystal Structure Of The E. Coli Aspartyl-T... 873 0.0
pdb|1EFW|A Chain A, Crystal Structure Of Aspartyl-Trna Syntheta... 494 2e-140

Gene Protein Sequence:
MMRSHYCGTLNRSHVGQAVTLSGWVHRIRNLGRFIFMQIRDREGIVQVFF
DEKDDTLFKVASQLRAEACVQIQGQVIARDEAQINPEMATGEIEVLVQNV
LVYNNAEVLPLDFNQNNTEEQRLKYRYLDLRRHKMAENLKTRAKITSFVR
RYMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQ
LLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEVRALME
NMIHSLWLDRLNVDLGKFPIMSWQEAMQHFGSDKPDLRNPLELVDIADIV
KNVEFNVFNEPANAIDGRVTVLRVPNGATLTRKQIDEYTQFVAIYGAKGL
AWAKINDINAGMDGIQSPVAKFLNAEIFNALIERTAAQNGDILFFGADKW
QVVTDAMGALRLKIGRDLALTDQTAWKPLWVIDFPMFERDGEGNLSAMHH
PFTAPKDLSPDQLAADPIKAVANAYDMVINGYEVGGGSVRIFDPKMQQTV
FNILGINEQDQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIR
DVIAFPKTTAAACLMTEAPSYANPQVLQELAIQTTVETE$

Gene Nucleotide Sequence:  Sequence Viewer
ATGATGCGTTCTCATTATTGCGGTACGTTAAACCGCTCTCACGTTGGACA
AGCTGTTACATTAAGCGGTTGGGTTCACCGTATCCGTAACCTTGGCCGTT
TTATTTTTATGCAAATCCGTGATCGTGAAGGAATCGTACAAGTTTTTTTT
GATGAAAAAGATGACACTCTCTTTAAAGTAGCTTCTCAATTACGCGCCGA
AGCTTGTGTCCAAATTCAAGGTCAAGTTATTGCCCGTGATGAAGCGCAAA
TCAATCCAGAAATGGCTACTGGTGAGATTGAAGTTCTAGTGCAAAATGTA
TTGGTTTATAACAATGCTGAAGTACTACCGCTCGATTTCAATCAAAATAA
TACCGAAGAACAACGCTTAAAATACCGCTATTTAGATTTACGTCGCCATA
AAATGGCAGAAAATCTCAAAACACGCGCCAAAATTACTAGTTTTGTGCGT
CGTTATATGGATGAACACGGCTTCCTAGATATTGAAACGCCCATGTTAAC
TAAAGCAACGCCTGAAGGCGCACGTGATTATTTAGTGCCGAGCCGTGTTC
ATAAAGGCAAGTTTTATGCATTACCACAATCACCGCAACTATTTAAACAA
TTACTAATGATGTCCGGTTTTGACCGCTATTATCAAATCGTCAAATGCTT
CCGTGATGAAGATCTACGCGCAGACCGCCAGCCAGAATTTACACAAATTG
ATGTAGAAACCTCTTTCTTAACCGCTGAGGAAGTCCGTGCCTTAATGGAA
AATATGATCCACAGTTTATGGTTAGATCGACTAAATGTCGATTTAGGTAA
ATTTCCGATCATGAGCTGGCAAGAAGCAATGCAACATTTTGGTTCAGATA
AACCTGATTTACGTAATCCTCTTGAATTAGTGGATATCGCCGATATCGTT
AAAAATGTTGAATTTAACGTCTTTAATGAACCCGCAAATGCCATCGATGG
ACGAGTAACGGTTTTACGCGTACCAAATGGTGCAACCTTAACGCGTAAAC
AAATTGATGAATATACACAATTTGTAGCGATTTATGGCGCTAAAGGCTTA
GCTTGGGCAAAAATTAATGATATCAACGCAGGAATGGACGGTATCCAAAG
CCCTGTGGCTAAATTCTTAAATGCAGAGATTTTCAATGCATTAATTGAAC
GCACTGCCGCCCAAAACGGCGATATCCTGTTCTTTGGCGCAGATAAATGG
CAAGTAGTGACCGATGCAATGGGCGCCTTACGCCTAAAAATTGGTCGAGA
CTTAGCATTAACTGATCAAACCGCTTGGAAACCATTATGGGTTATTGATT
TCCCAATGTTTGAGCGAGATGGTGAAGGCAATTTATCTGCAATGCATCAT
CCATTTACTGCACCCAAAGATCTTTCACCTGACCAATTAGCAGCCGATCC
AATCAAAGCGGTTGCTAATGCCTATGATATGGTTATCAACGGCTATGAAG
TCGGTGGTGGTTCAGTTCGTATTTTCGATCCTAAAATGCAACAAACTGTC
TTCAATATTTTAGGTATTAATGAACAAGATCAGCAGGAAAAATTTGGATT
CTTATTAGATGCACTTAAATTTGGTACACCTCCACATGCTGGCTTAGCTT
TTGGTTTAGACCGTTTAACGATGTTGATCACAGGTACAGAAAACATTCGT
GATGTCATTGCATTTCCAAAAACTACAGCAGCCGCATGTTTAATGACCGA
AGCACCAAGCTATGCAAATCCACAAGTATTACAAGAATTAGCTATCCAGA
CCACGGTTGAAACTGAATAA


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