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

Ureaplasma urealyticum Search Results

Record: 1 of 1  
MiniMap IGR93 IGR90 IGR89 IGR91 IGR92 hpt,hprT, - UU104 potC, - UU109 sys,serS, - UU106 potA, - UU107 UU103 potD, - UU110 ftsH, - UU105 hpt,hprT, - UU104 potC, - UU109 sys,serS, - UU106 potA, - UU107 UU103 potD, - UU110 ftsH, - UU105 Type: tandem, Name:  - 74 Type: tandem, Name:  - 79 Type: tandem, Name:  - 73 Type: tandem, Name:  - 77 Type: tandem, Name:  - 71 Type: tandem, Name:  - 398 Type: tandem, Name:  - 78 Type: tandem, Name:  - 76 Type: tandem, Name:  - 72 Type: tandem, Name:  - 80 Type: tandem, Name:  - 75 hpt,hprT, - UU104 potC, - UU109 sys,serS, - UU106 potA, - UU107 UU103 potD, - UU110 ftsH, - UU105 potB, - UU108 potB, - UU108
* Calculated from Protein Sequence

Gene ID: UU106

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
sys  serS  

Definition:
seryl-tRNA synthetase

Gene Start:
135132

Gene Stop:
136388

Gene Length:
1257

Molecular Weight*:
47802

pI*:
7.70

Net Charge*:
1.95

EC:
6.1.1.11  

Functional Class:
translation; aminoacyl-tRNA synthetases  

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

Comment:
From Prosite PDOC00363 : Aminoacyl-tRNA synthetases (EC 6.1.1.-) [Schimmel P. Annu. Rev. Biochem. 56:125-158(1987).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.

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
Gapped BLAST reveals a number of significant hits against other seryl-tRNA synthetases. For example residues 1-417 are 50% similar to residues 1-417 of the seryl-tRNA synthetase of Aquifex aeolicus (AE000682). Other significant hits were to the seryl-tRNA synthetases of B.subtilis (SYS_BACSU), S.aureus (SYS_STAAU) and M.genitalium (SYS_MYCGE), in addition to many others.

Within the STDPRO database, the top hits are also against the SerS proteins of MG005, CT729, and TP0647.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0172 is ehgpcmYu.
Cog name: Seryl-tRNA synthetase.
Functional class: J.
BeTs to e-g-cmyu.
Number of proteins in this genome belonging to this COG is 1



Blocks Summary:  Blocks Search
Residues 275-294 are in the 97.44th percentile of similarity to block PD01035F (SYNTHETASE LIGASE THREONYL-TRNA.)
Residues 268-279 match to the 97.11th percentile, Block PR0098E (Uridine Kinase Signature.)

ProDom Summary:  Protein Domain Search
Residues 141-380 are 56% similar, and 381-417 are 70% similar to a defined domain of SYS_BACSU.
Residues 102-138 are 59% similar to a defined domain of SYS_AQUAE.
Residues 1-102 are 30% similar to a defined domain of SYS_HALMA.

Paralogs:  Local Blast Search
This protein is paralogously related to UU452, a prolyl-tRNA synthetase. Residues 214-412 are 23% similar.

Pfam Summary:  Pfam Search
Residues 1 to 109 (E-value = 1.4e-30) place UU106 in the Seryl_tRNA_N family which is described as Seryl-tRNA synthetase N-terminal domain (PF02403)
Residues 163 to 317 (E-value = 8.4e-52) place UU106 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
coil-coil  
34  
104

PDB Hit:
gi|494615|pdb|1SRY|A Chain A, Seryl-Trna Synthetase (E.C.6.1.1.11)

Gene Protein Sequence:
MFDINLIRKDIATTKEKMLNKKVPSNLFDQIFDLDVLVRSLMQQEQNLNA
KKNQLSKEIGILAKNKDPKLQQTLDLVNNIKNELQDISLTLSNKQDELNK
LLLVIPNMPDDSVPIGNDENDNVEIKKVFKPKKFDFLPLAHWDLAVKNKL
IDFDKSTKITGSRFIIYTNFGARLYRALQQFCLDMNVKAGFSEIWAPVIV
NQESLIGSGNLPKFADDLFKLENSNYYLSPTAEVQLTNLHRNEILKASDL
PLYYTALTPCFRSEAGSAGRDVRGVIRQHQFHKVELVKLCKPEDSFKELE
SMTRQAESILEALELPYRRIVLCTGDLGFSSAKTYDLEVWLPSYNAYKEI
SSCSNCTNFQARRAKIRYKETIDATTELVHTLNGSSLAIDRLWAAIVENY
QQEDGSINIPKVLKKYIY$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTTGATATTAATTTAATACGAAAAGATATTGCAACTACTAAAGAAAA
GATGTTAAATAAAAAGGTGCCAAGCAATTTGTTTGATCAAATTTTTGATT
TAGATGTTTTAGTACGAAGTTTAATGCAACAAGAACAAAATCTTAATGCT
AAGAAAAATCAATTATCAAAAGAAATTGGTATTTTAGCTAAAAACAAAGA
TCCTAAATTACAACAAACATTAGATTTAGTTAATAATATTAAAAACGAAT
TGCAAGATATTTCATTAACATTATCAAACAAACAAGATGAATTAAATAAA
TTATTATTAGTAATTCCTAATATGCCAGATGATTCAGTGCCCATTGGCAA
TGATGAAAATGACAACGTCGAAATTAAAAAAGTTTTTAAACCAAAAAAAT
TTGATTTTTTACCCCTTGCGCATTGAGATTTAGCAGTAAAAAACAAGTTA
ATTGATTTTGATAAATCAACAAAAATTACTGGTAGTCGTTTTATTATTTA
TACTAATTTTGGTGCACGTTTATATCGTGCTTTACAACAATTTTGTTTAG
ATATGAATGTAAAAGCAGGTTTTAGTGAAATTTGAGCACCTGTTATTGTT
AATCAAGAATCTTTAATTGGTTCTGGAAACTTACCTAAATTTGCAGATGA
TTTATTCAAATTAGAAAATTCAAATTATTATTTATCACCAACTGCTGAAG
TGCAATTAACAAATTTACATCGTAATGAAATTTTAAAAGCTAGTGATTTA
CCTTTATACTATACAGCTCTAACACCTTGTTTTCGTAGTGAAGCAGGATC
TGCAGGACGCGATGTTAGAGGTGTAATTCGTCAACACCAATTCCATAAAG
TAGAATTAGTAAAATTATGTAAACCAGAAGATAGTTTTAAAGAATTAGAA
TCAATGACAAGACAGGCTGAAAGTATTTTAGAAGCTTTAGAATTACCTTA
TAGAAGAATCGTTTTATGCACAGGCGATTTAGGTTTTAGTTCAGCTAAAA
CATATGATTTAGAAGTTTGATTACCATCATATAACGCTTATAAAGAAATT
TCAAGTTGTTCAAATTGCACTAATTTCCAAGCGCGTCGTGCAAAAATTCG
TTATAAAGAAACAATTGATGCAACAACCGAATTAGTTCATACATTAAACG
GATCATCATTAGCAATTGATCGATTATGGGCTGCAATTGTTGAAAATTAT
CAACAAGAAGATGGTAGTATCAACATTCCTAAAGTATTAAAAAAATACAT
CTATTAA


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