PYLS_METTE
ID PYLS_METTE Reviewed; 478 AA.
AC Q1L6A3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Pyrrolysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01573};
DE EC=6.1.1.26 {ECO:0000255|HAMAP-Rule:MF_01573};
DE AltName: Full=Pyrrolysine--tRNA(Pyl) ligase;
DE AltName: Full=Pyrrolysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01573};
DE Short=PylRS {ECO:0000255|HAMAP-Rule:MF_01573};
GN Name=pylS {ECO:0000255|HAMAP-Rule:MF_01573};
OS Methanosarcina thermophila.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Polycarpo C., Ambrogelly A., Herring S., Soell D.G.;
RT "The substrate specificity of pyrrolysyl-tRNA synthetase.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of pyrrolysine to tRNA(Pyl).
CC Pyrrolysine is a lysine derivative encoded by the termination codon
CC UAG. {ECO:0000255|HAMAP-Rule:MF_01573}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-pyrrolysine + tRNA(Pyl) = AMP + diphosphate + L-
CC pyrrolysyl-tRNA(Pyl); Xref=Rhea:RHEA:19277, Rhea:RHEA-COMP:9720,
CC Rhea:RHEA-COMP:9721, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58499, ChEBI:CHEBI:78442, ChEBI:CHEBI:78556,
CC ChEBI:CHEBI:456215; EC=6.1.1.26; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01573};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01573}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_01573}.
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DR EMBL; DQ017250; AAY81923.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1L6A3; -.
DR SMR; Q1L6A3; -.
DR BRENDA; 6.1.1.26; 3281.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043767; F:pyrrolysyl-tRNA synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_01573; Pyl_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR012739; Pyrrolysyl-tRNA_ligase.
DR InterPro; IPR023877; Pyrrolysyl-tRNA_ligase_C.
DR InterPro; IPR023878; Pyrrolysyl-tRNA_ligase_N.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR02367; PylS_Cterm; 1.
DR TIGRFAMs; TIGR03912; PylS_Nterm; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..478
FT /note="Pyrrolysine--tRNA ligase"
FT /id="PRO_0000260454"
FT REGION 106..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 53441 MW; 348D3824845E0278 CRC64;
MDKKPLNTLI SATGLWMSRT GKLHKIRHHE VSKRKIYIEM ECGERLVVNN SRSCRAARAL
RHHKYRKICK HCRVSDEDLN KFLTRTNEDK SNAKVTVVSA PKIRKVMPKS VARTPKPLEN
TAPVQTLPSE SQPAPTTPIS ASTTAPASTS TTAPAPASTT APAPASTTAP ASASTTISTS
AMPASTSAQG TTKFNYISGG FPRPIPVQAS APALTKSQID RLQGLLSPKD EISLDSGTPF
RKLESELLSR RRKDLKQIYA EEREHYLGKL EREITKFFVD RGFLEIKSPI LIPMEYIERM
GIDNDKELSK QIFRVDNNFC LRPMLAPNLY NYLRKLNRAL PDPIKIFEIG PCYRKESDGK
EHLEEFTMLN FCQMGSGCTR ENLEAIIKDF LDYLGIDFEI VGDSCMVYGD TLDVMHGDLE
LSSAVVGPVP MDRDWGINKP WIGAGFGLER LLKVMHNFKN IKRASRSESY YNGISTNL
