Reviewed,
UniProtKB/Swiss-Prot Q8TVD2 (SYS2_METKA)
Last modified
November 3, 2009.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Type-2 seryl-tRNA synthetase EC=6.1.1.11 Alternative name(s): Seryl-tRNA(Ser/Sec) synthetase Serine--tRNA ligase Short name=SerRS | ||||
| Gene names |
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| Organism | Methanopyrus kandleri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2320 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus |
Protein attributes
| Sequence length | 527 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| 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) By similarity. |
| Catalytic activity | ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_01278 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_01278 |
| Cofactor | Binds 1 Zn2+ 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 By similarity. |
| Pathway | Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_01278 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Domain | Consists of two distinct domains, a catalytic core and a N-terminal extension that is presumably involved in tRNA binding By similarity. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP seryl-tRNA aminoacylationInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 527 | 527 | Type-2 seryl-tRNA synthetase HAMAP MF_01278 | PRO_0000286169 | |||||
Regions | |||||||||
| Nucleotide binding | 349 – 351 | 3 | ATP By similarity | ||||||
| Nucleotide binding | 360 – 361 | 2 | ATP By similarity | ||||||
| Region | 366 – 368 | 3 | Serine binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 319 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 368 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 478 | 1 | Zinc; catalytic By similarity | ||||||
| Binding site | 317 | 1 | Serine; via carbonyl oxygen By similarity | ||||||
| Binding site | 349 | 1 | Serine By similarity | ||||||
| Binding site | 485 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938. |
Cross-references
Sequence databases | |
|---|---|
| AE009439 Genomic DNA. Translation: AAM02673.1. | |
| RefSeq | NP_614743.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1478055. |
| GenomeReviews | Gene locus MK1460 in contig AE009439_GR. |
| KEGG | mka:MK1460. |
| NMPDR | fig|190192.1.peg.1456. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8TVD2. |
| OMA | PAQCEPF. |
Enzyme and pathway databases | |
| BioCyc | MKAN190192:MK1460-MON. |
| BRENDA | 6.1.1.11. 7577. |
Family and domain databases | |
| HAMAP | MF_01278. [Tree] |
| InterPro | IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004503. Ser-tRNA-synth_IIa_arc. IPR018156. Ser-tRNA-synth_IIa_C. [Graphical view] |
| PANTHER | PTHR11778. tRNA-synt_ser. 1 hit. |
| Pfam | PF00587. tRNA-synt_2b. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00415. serS_MJ. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYS2_METKA | ||||||||
| Accession | Primary (citable) accession number: Q8TVD2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


