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Q8PWY1 (PYLS_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Pyrrolysine--tRNA ligase
EC=6.1.1.26
Alternative name(s):
Pyrrolysine--tRNA(Pyl) ligase
Pyrrolysyl-tRNA synthetase
Short name=PylRS
Gene names
Name:pylS
Ordered Locus Names:MM_1445
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina ›

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG By similarity. HAMAP-Rule MF_01573

Catalytic activity

ATP + L-pyrrolysine + tRNA(Pyl) = AMP + diphosphate + L-pyrrolysyl-tRNA(Pyl). HAMAP-Rule MF_01573

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processtRNA aminoacylation for protein translation

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

aminoacyl-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Pyrrolysine--tRNA ligase HAMAP-Rule MF_01573
PRO_0000260453

Secondary structure

1 ................................................ 454
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8PWY1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: D6BE5A812B5CA96E

FASTA45450,921
        10         20         30         40         50         60 
MDKKPLNTLI SATGLWMSRT GTIHKIKHHE VSRSKIYIEM ACGDHLVVNN SRSSRTARAL 

        70         80         90        100        110        120 
RHHKYRKTCK RCRVSDEDLN KFLTKANEDQ TSVKVKVVSA PTRTKKAMPK SVARAPKPLE 

       130        140        150        160        170        180 
NTEAAQAQPS GSKFSPAIPV STQESVSVPA SVSTSISSIS TGATASALVK GNTNPITSMS 

       190        200        210        220        230        240 
APVQASAPAL TKSQTDRLEV LLNPKDEISL NSGKPFRELE SELLSRRKKD LQQIYAEERE 

       250        260        270        280        290        300 
NYLGKLEREI TRFFVDRGFL EIKSPILIPL EYIERMGIDN DTELSKQIFR VDKNFCLRPM 

       310        320        330        340        350        360 
LAPNLYNYLR KLDRALPDPI KIFEIGPCYR KESDGKEHLE EFTMLNFCQM GSGCTRENLE 

       370        380        390        400        410        420 
SIITDFLNHL GIDFKIVGDS CMVYGDTLDV MHGDLELSSA VVGPIPLDRE WGIDKPWIGA 

       430        440        450 
GFGLERLLKV KHDFKNIKRA ARSESYYNGI STNL

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE008384 Genomic DNA. Translation: AAM31141.1.
RefSeqNP_633469.1. NC_003901.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E3CX-ray2.65A185-454[»]
2Q7EX-ray1.80A185-454[»]
2Q7GX-ray1.90A185-454[»]
2Q7HX-ray2.10A185-454[»]
2ZCEX-ray1.80A185-454[»]
2ZIMX-ray2.10A185-454[»]
2ZINX-ray1.79A185-454[»]
2ZIOX-ray2.06A185-454[»]
3QTCX-ray1.75A185-454[»]
3VQVX-ray1.90A185-454[»]
ProteinModelPortalQ8PWY1.
SMRQ8PWY1. Positions 188-454.
ModBaseSearch...

Protein-protein interaction databases

STRING192952.MM_1445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM31141; AAM31141; MM_1445.
GeneID1479787.
KEGGmma:MM_1445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG11047.
HOGENOMHOG000115810.
KOK11627.
OMAFCQMGSG.
ProtClustDBPRK09537.

Family and domain databases

Gene3D1.10.287.540. 1 hit.
HAMAPMF_01573. Pyl_tRNA_synth.
InterProIPR018150. aa-tRNA-synt_II-like.
IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR012739. Pyrrolysyl-tRNA_ligase.
IPR023877. Pyrrolysyl-tRNA_ligase_C.
IPR023878. Pyrrolysyl-tRNA_ligase_N.
IPR023218. UPF0291_struct_dom.
[Graphical view]
PANTHERPTHR22594. PTHR22594. 1 hit.
PfamPF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
TIGRFAMsTIGR02367. PylS_Cterm. 1 hit.
TIGR03912. PylS_Nterm. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8PWY1.

Entry information

Entry namePYLS_METMA
AccessionPrimary (citable) accession number: Q8PWY1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 1, 2002
Last modified: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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