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Annotation rule MF_00184 |
General rule information
[?]
Accession |
MF_00184 |
Dates |
1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 42) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Protein name |
RecName:
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Full=Threonine--tRNA ligase;
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EC 6.1.1.3;
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AltName:
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Full=Threonyl-tRNA synthetase;
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Short=ThrRS;
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case <OC:Archaea> and not <Feature:PF08915>
Function |
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). |
else
Function |
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). |
end case
Catalytic activity |
RHEA:24624: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC 6.1.1.3
|
case <FTGroup:1>
Cofactor |
Zn(2+) Note: Binds 1 zinc ion per subunit. |
end case
Subunit |
Homodimer. |
Subcellular location |
Cytoplasm. |
case <OC:Archaea> and <Feature:PF08915>
Domain |
The N-terminal domain is an archaea-specific tRNA-editing domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis of tRNA editing is performed by the charged tRNA itself. |
end case
Similarity |
Belongs to the class-II aminoacyl-tRNA synthetase family. |
case <FTTag:acet>
end case
case <FTGroup:1>
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.
From: SYT_ECOLI (P0A8M3) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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REGION
|
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243
|
|
534
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Catalytic
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|
|
|
|
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METAL
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334
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334
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Zinc; catalytic
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C
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1
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METAL
|
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385
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385
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Zinc; catalytic
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|
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H
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1
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METAL
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511
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511
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Zinc; catalytic
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H
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1
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case <OC:Escherichia> or <OC:Shigella>
MOD_RES
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286
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286
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N6-acetyllysine
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acet
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K
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|
end case
case <OC:Archaea> and <Feature:PF08915>
From: SYT_PYRAB (Q9UZ14) |
REGION
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1
|
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143
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Editing domain
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end case
Additional information
[?]
Size range |
540-702 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
In some Archaea (AERPE, METS5, Sulfolobus among others) the editing domain is found in a separate protein. |