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Q8TVD2 (SYS2_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type-2 serine--tRNA ligase
EC=6.1.1.11
Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene names
Name:serS
Ordered Locus Names:MK1460
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus ›

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_01278

Catalytic activity

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP-Rule MF_01278

ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule 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-Rule 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. HAMAP-Rule MF_01278

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Type-2 serine--tRNA ligase HAMAP-Rule MF_01278
PRO_0000286169

Regions

Nucleotide binding349 – 3513ATP By similarity
Nucleotide binding360 – 3612ATP By similarity
Region366 – 3683Serine binding By similarity

Sites

Metal binding3191Zinc; catalytic By similarity
Metal binding3681Zinc; catalytic By similarity
Metal binding4781Zinc; catalytic By similarity
Binding site3171Serine; via carbonyl oxygen By similarity
Binding site3491Serine By similarity
Binding site4851ATP By similarity

Secondary structure

1 ............................................................................................. 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8TVD2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 7526147D81EFC5CD

FASTA52761,368
        10         20         30         40         50         60 
MELKFSAEVE LTLSREVDPA EIEPTVEEFV KEANEDLLQR GVPTGKEGAK IESYRVLEDT 

        70         80         90        100        110        120 
IEMEITGTRY LRPHEAAMRV RKRLAERLGR KHRVGVRDLK IPRYEVVLRF DREVTRDDVG 

       130        140        150        160        170        180 
YVPVADDVVV EDGTVRLTFQ DVDEEMLRRH VIDRVIRLVA WAVEERSELV ERVTKVEPGT 

       190        200        210        220        230        240 
VVDESGPREI RFDGDVTEEA RRRGWVKEFP GRGQWIYTPP MAALFEVLRD FLLERVTRKL 

       250        260        270        280        290        300 
GFEPALFPKL IPLETMFRMR YLHGLPDGMY YVCPPKRDPE LFDDFKRELY VWGELNERTL 

       310        320        330        340        350        360 
GSLKEKLRDP GYVLAPAQCE PFYELLRDEV VDPERLPIKL YDCSGWTYRW EGGAAKGLER 

       370        380        390        400        410        420 
VNEFQRIEHV WIAEPEEAER IREELLEATK RVAEELELEW KVVVSDDPFY LEGRLLEDRD 

       430        440        450        460        470        480 
IELPDVPSYE FEVYLPFKGE RSSEEAWISV GSFNVHGEHF VDGFNVKEKS GRTLFTGCAG 

       490        500        510        520 
LGVTRWVVGL LAQHGFEPEE WPEPILERID EKFGGLPEVP KTLTWPE

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009439 Genomic DNA. Translation: AAM02673.1.
RefSeqNP_614743.1. NC_003551.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3W3SX-ray3.10A1-527[»]
ProteinModelPortalQ8TVD2.
ModBaseSearch...

Protein-protein interaction databases

STRING190192.MK1460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM02673; AAM02673; MK1460.
GeneID1478055.
KEGGmka:MK1460.

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHOG000254149.
KOK01875.
OMAAQCEPFY.
ProtClustDBPRK00960.

Enzyme and pathway databases

UniPathwayUPA00906; UER00895.

Family and domain databases

HAMAPMF_01278. Ser_tRNA_synth_type2.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004503. Ser-tRNA-ligase_IIa_arc.
[Graphical view]
PfamPF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
TIGRFAMsTIGR00415. serS_MJ. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS2_METKA
AccessionPrimary (citable) accession number: Q8TVD2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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