| Accession |
MF_00184 |
| Dates |
1-JUN-2001 (Created)
25-SEP-2008 (Last updated, Version 32) |
case <OC:Bacteria>
end case
case <OC:Archaea>
end case
| Protein name |
| RecName: |
Full=Threonyl-tRNA synthetase;
EC=6.1.1.3; |
| AltName: |
Full=Threonine--tRNA ligase;
Short=ThrRS; |
|
CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).
case <FT:2> and <FT:3> and <FT:4> or <FT:7> and <FT:8> and <FT:9>
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
end case
case <OC:Bacteria>
SUBUNIT: Homodimer (By similarity).
end case
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
case <FT:5>
end case
case <FT:2> and <FT:3> and <FT:4> or <FT:7> and <FT:8> and <FT:9>
end case
GO:0005524; Molecular function: ATP binding.
GO:0004829; Molecular function: threonine-tRNA ligase activity.
GO:0006435; Biological process: threonyl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.
case <OC:Bacteria>
| From: SYT_ECOLI (P0A8M3) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| REGION |
|
243 |
|
534 |
|
Catalytic |
|
|
|
|
| METAL |
|
334 |
|
334 |
|
Zinc; catalytic (By similarity) |
|
C |
|
|
| METAL |
|
385 |
|
385 |
|
Zinc; catalytic (By similarity) |
|
H |
|
|
| METAL |
|
511 |
|
511 |
|
Zinc; catalytic (By similarity) |
|
H |
|
|
end case
case <OC:Escherichia> or <OC:Shigella>
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| MOD_RES |
|
286 |
|
286 |
|
N6-acetyllysine (By similarity) |
|
K |
|
|
end case
case <OC:Archaea>
| From: SYT_ARCFU (O29703) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| REGION |
|
196 |
|
495 |
|
Catalytic |
|
|
|
|
| METAL |
|
288 |
|
288 |
|
Zinc; catalytic (By similarity) |
|
C |
|
|
| METAL |
|
340 |
|
340 |
|
Zinc; catalytic (By similarity) |
|
H |
|
|
| METAL |
|
464 |
|
464 |
|
Zinc; catalytic (By similarity) |
|
H |
|
|
end case
case <OC:Bacteria>
| Size range: |
564-702 amino acids |
end case
case <OC:Archaea>
| Size range: |
540-660 amino acids |
end case
| Related UniRules: |
None |
| Template: |
P0A8M3 (SYT_ECOLI); P56881 (SYT_THET8): [Recover all] |
| Scope: |
Bacteria
Archaea |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
in AERPE, BACSU |
| Plasmid encoded: |
None |
| Comments: |
There are two ThrRS in AERPE. The first one (APE_0809.1) is most similar to bacterial ThrRS but it lack the N-terminal domain. The second one (APE_0117.1) is most similar to archaeal ThrRS but lack the central domain |
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