ID   PYLS_METBU              Reviewed;         416 AA.
AC   Q12UB6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
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}; OrderedLocusNames=Mbur_2086;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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; CP000300; ABE52960.1; -; Genomic_DNA.
DR   RefSeq; WP_011500100.1; NC_007955.1.
DR   AlphaFoldDB; Q12UB6; -.
DR   SMR; Q12UB6; -.
DR   STRING; 259564.Mbur_2086; -.
DR   PRIDE; Q12UB6; -.
DR   EnsemblBacteria; ABE52960; ABE52960; Mbur_2086.
DR   GeneID; 3998168; -.
DR   KEGG; mbu:Mbur_2086; -.
DR   HOGENOM; CLU_648316_0_0_2; -.
DR   OMA; RPMLAPN; -.
DR   OrthoDB; 25314at2157; -.
DR   Proteomes; UP000001979; Chromosome.
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; Reference proteome.
FT   CHAIN           1..416
FT                   /note="Pyrrolysine--tRNA ligase"
FT                   /id="PRO_0000260452"
SQ   SEQUENCE   416 AA;  48305 MW;  8A941DAA2BC5FCAA CRC64;
     MEKQLLDVLV ELNGVWLSRS GLLHGIRNFE ITTKHIHIET DCGARFTVRN SRSSRSARSL
     RHNKYRKPCK RCRPADEQID RFVKKTFKEK RQTVSVFSSP KKHVPKKPKV AVIKSFSIST
     PSPKEASVSN SIPTPSISVV KDEVKVPEVK YTPSQIERLK TLMSPDDKIP IQDELPEFKV
     LEKELIQRRR DDLKKMYEED REDRLGKLER DITEFFVDRG FLEIKSPIMI PFEYIERMGI
     DKDDHLNKQI FRVDESMCLR PMLAPCLYNY LRKLDKVLPD PIRIFEIGPC YRKESDGSSH
     LEEFTMVNFC QMGSGCTREN MEALIDEFLE HLGIEYEIEA DNCMVYGDTI DIMHGDLELS
     SAVVGPIPLD REWGVNKPWM GAGFGLERLL KVRHNYTNIR RASRSELYYN GINTNL