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Protein

Pyrrolysine--tRNA ligase

Gene

pylS

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG.UniRule annotation

Catalytic activityi

ATP + L-pyrrolysine + tRNA(Pyl) = AMP + diphosphate + L-pyrrolysyl-tRNA(Pyl).UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.26. 3270.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrrolysine--tRNA ligaseUniRule annotation (EC:6.1.1.26UniRule annotation)
Alternative name(s):
Pyrrolysine--tRNA(Pyl) ligase
Pyrrolysyl-tRNA synthetaseUniRule annotation
Short name:
PylRSUniRule annotation
Gene namesi
Name:pylSUniRule annotation
Ordered Locus Names:MM_1445
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000000595 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002604531 – 454Pyrrolysine--tRNA ligaseAdd BLAST454

Proteomic databases

PRIDEiQ8PWY1.

Interactioni

Protein-protein interaction databases

STRINGi192952.MM_1445.

Structurei

Secondary structure

1454
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi192 – 201Combined sources10
Helixi204 – 206Combined sources3
Beta strandi210 – 214Combined sources5
Helixi216 – 236Combined sources21
Helixi242 – 256Combined sources15
Beta strandi260 – 262Combined sources3
Beta strandi266 – 269Combined sources4
Helixi270 – 275Combined sources6
Helixi283 – 287Combined sources5
Turni292 – 294Combined sources3
Beta strandi295 – 297Combined sources3
Beta strandi299 – 301Combined sources3
Helixi302 – 312Combined sources11
Turni313 – 315Combined sources3
Beta strandi318 – 329Combined sources12
Beta strandi335 – 337Combined sources3
Beta strandi340 – 351Combined sources12
Helixi356 – 370Combined sources15
Beta strandi375 – 381Combined sources7
Turni382 – 384Combined sources3
Beta strandi385 – 392Combined sources8
Beta strandi395 – 403Combined sources9
Helixi406 – 411Combined sources6
Beta strandi417 – 423Combined sources7
Helixi424 – 432Combined sources9
Helixi437 – 440Combined sources4
Beta strandi444 – 447Combined sources4
Beta strandi450 – 452Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3VQWX-ray2.40A185-454[»]
3VQXX-ray2.30A/B/C/D185-454[»]
4BW9X-ray2.35A185-454[»]
4BWAX-ray2.45A185-454[»]
4CH3X-ray2.28A185-454[»]
4CH4X-ray2.16A185-454[»]
4CH5X-ray2.20A185-454[»]
4CH6X-ray2.05A185-454[»]
4CS2X-ray1.90A188-454[»]
4CS3X-ray1.50A188-454[»]
4CS4X-ray1.35A188-454[»]
4Q6GX-ray2.25A188-454[»]
4TQDX-ray2.14A185-454[»]
4TQFX-ray2.71A185-454[»]
4ZIBX-ray2.05A185-454[»]
5K1PX-ray1.50A188-454[»]
5K1XX-ray1.95A188-454[»]
ProteinModelPortaliQ8PWY1.
SMRiQ8PWY1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8PWY1.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG00413. Archaea.
ENOG410ZS8D. LUCA.
HOGENOMiHOG000115810.
KOiK11627.
OMAiNFCQMGS.

Family and domain databases

Gene3Di1.10.287.540. 1 hit.
HAMAPiMF_01573. Pyl_tRNA_synth. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR012739. Pyrrolysyl-tRNA_ligase.
IPR023877. Pyrrolysyl-tRNA_ligase_C.
IPR023878. Pyrrolysyl-tRNA_ligase_N.
IPR023218. UPF0291_struct_dom.
[Graphical view]
PfamiPF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02367. PylS_Cterm. 1 hit.
TIGR03912. PylS_Nterm. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8PWY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKKPLNTLI SATGLWMSRT GTIHKIKHHE VSRSKIYIEM ACGDHLVVNN
60 70 80 90 100
SRSSRTARAL RHHKYRKTCK RCRVSDEDLN KFLTKANEDQ TSVKVKVVSA
110 120 130 140 150
PTRTKKAMPK SVARAPKPLE NTEAAQAQPS GSKFSPAIPV STQESVSVPA
160 170 180 190 200
SVSTSISSIS TGATASALVK GNTNPITSMS APVQASAPAL TKSQTDRLEV
210 220 230 240 250
LLNPKDEISL NSGKPFRELE SELLSRRKKD LQQIYAEERE NYLGKLEREI
260 270 280 290 300
TRFFVDRGFL EIKSPILIPL EYIERMGIDN DTELSKQIFR VDKNFCLRPM
310 320 330 340 350
LAPNLYNYLR KLDRALPDPI KIFEIGPCYR KESDGKEHLE EFTMLNFCQM
360 370 380 390 400
GSGCTRENLE SIITDFLNHL GIDFKIVGDS CMVYGDTLDV MHGDLELSSA
410 420 430 440 450
VVGPIPLDRE WGIDKPWIGA GFGLERLLKV KHDFKNIKRA ARSESYYNGI

STNL
Length:454
Mass (Da):50,921
Last modified:October 1, 2002 - v1
Checksum:iD6BE5A812B5CA96E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM31141.1.
RefSeqiWP_011033391.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM31141; AAM31141; MM_1445.
GeneIDi24883267.
KEGGimma:MM_1445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM31141.1.
RefSeqiWP_011033391.1. NC_003901.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3VQWX-ray2.40A185-454[»]
3VQXX-ray2.30A/B/C/D185-454[»]
4BW9X-ray2.35A185-454[»]
4BWAX-ray2.45A185-454[»]
4CH3X-ray2.28A185-454[»]
4CH4X-ray2.16A185-454[»]
4CH5X-ray2.20A185-454[»]
4CH6X-ray2.05A185-454[»]
4CS2X-ray1.90A188-454[»]
4CS3X-ray1.50A188-454[»]
4CS4X-ray1.35A188-454[»]
4Q6GX-ray2.25A188-454[»]
4TQDX-ray2.14A185-454[»]
4TQFX-ray2.71A185-454[»]
4ZIBX-ray2.05A185-454[»]
5K1PX-ray1.50A188-454[»]
5K1XX-ray1.95A188-454[»]
ProteinModelPortaliQ8PWY1.
SMRiQ8PWY1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi192952.MM_1445.

Proteomic databases

PRIDEiQ8PWY1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM31141; AAM31141; MM_1445.
GeneIDi24883267.
KEGGimma:MM_1445.

Phylogenomic databases

eggNOGiarCOG00413. Archaea.
ENOG410ZS8D. LUCA.
HOGENOMiHOG000115810.
KOiK11627.
OMAiNFCQMGS.

Enzyme and pathway databases

BRENDAi6.1.1.26. 3270.

Miscellaneous databases

EvolutionaryTraceiQ8PWY1.

Family and domain databases

Gene3Di1.10.287.540. 1 hit.
HAMAPiMF_01573. Pyl_tRNA_synth. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR012739. Pyrrolysyl-tRNA_ligase.
IPR023877. Pyrrolysyl-tRNA_ligase_C.
IPR023878. Pyrrolysyl-tRNA_ligase_N.
IPR023218. UPF0291_struct_dom.
[Graphical view]
PfamiPF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02367. PylS_Cterm. 1 hit.
TIGR03912. PylS_Nterm. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYLS_METMA
AccessioniPrimary (citable) accession number: Q8PWY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.