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Annotation rule MF_01278 |
General rule information
[?]
Accession |
MF_01278 |
Dates |
16-APR-2007 (Created) 19-NOV-2019 (Last updated, Version 16) |
Name |
Ser_tRNA_synth_type2 |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Protein name |
RecName:
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Full=Type-2 serine--tRNA ligase;
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EC 6.1.1.11;
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AltName:
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Full=Seryl-tRNA synthetase;
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Short=SerRS;
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AltName:
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Full=Seryl-tRNA(Ser/Sec) synthetase;
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Function |
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). |
Catalytic activity |
RHEA:12292: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser)
EC 6.1.1.11
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RHEA:42580: ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-seryl-tRNA(Sec)
EC 6.1.1.11
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case <FTGroup:1>
Cofactor |
Zn(2+) Note: Binds 1 Zn(2+) ion per subunit. This ion is coordinated with 2 cysteines, 1 glutamate and a water molecule that dissociates from the zinc ion to allow the coordination of the amino group of the serine substrate, which is essential for catalysis. |
end case
Pathway |
Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. |
Subunit |
Homodimer. |
Subcellular location |
Cytoplasm. |
Domain |
Consists of two distinct domains, a catalytic core and a N-terminal extension that is presumably involved in tRNA binding. |
Similarity |
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily. |
case <FTGroup:1>
end case
GO:0004828; Molecular function: serine-tRNA ligase activity.
GO:0005524; Molecular function: ATP binding.
case <FTGroup:1>
end case
GO:0016260; Biological process: selenocysteine biosynthetic process.
GO:0006434; Biological process: seryl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.
From: SYS2_METBF (Q46AN5) |
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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NP_BIND
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336
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338
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ATP
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R-x-E
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NP_BIND
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347
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348
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ATP
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R-V
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REGION
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353
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355
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Serine binding
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R-x-E
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METAL
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306
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306
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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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355
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355
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Zinc; catalytic
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E
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1
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METAL
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461
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461
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Zinc; catalytic
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C
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1
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BINDING
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304
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304
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Serine; via carbonyl oxygen
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A
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BINDING
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336
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336
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Serine
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R
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BINDING (Optional)
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400
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400
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Serine
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Q
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BINDING (Optional)
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432
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432
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ATP
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E
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BINDING (Optional)
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435
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435
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Serine
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N
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BINDING
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468
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468
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ATP
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R
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Additional information
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Size range |
500-527 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
There are two distinct types of seryl-tRNA synthetase, as differentiated by primary sequence analysis, three-dimensional structure and substrate recognition mechanism: type 1 (MF_00176) is found in the majority of organisms (prokaryotes, eukaryotes and archaea) whereas type 2 (MF_01278) is confined to some methanogenic archaea. METBF (Methanosarcina barkeri) possesses two seryl-tRNA synthetases, one of each type. |