ID   PYLS_METBA              Reviewed;         419 AA.
AC   Q6WRH6; Q8NKQ6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Pyrrolysine--tRNA ligase;
DE            EC=6.1.1.26;
DE   AltName: Full=Pyrrolysine--tRNA(Pyl) ligase;
DE   AltName: Full=Pyrrolysyl-tRNA synthetase;
DE            Short=PylRS;
GN   Name=pylS;
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=12029131; DOI=10.1126/science.1069588;
RA   Srinivasan G., James C.M., Krzycki J.A.;
RT   "Pyrrolysine encoded by UAG in Archaea: charging of a UAG-decoding
RT   specialized tRNA.";
RL   Science 296:1459-1462(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=14536069; DOI=10.1016/s1097-2765(03)00280-6;
RA   Polycarpo C., Ambrogelly A., Ruan B., Tumbula-Hansen D., Ataide S.F.,
RA   Ishitani R., Yokoyama S., Nureki O., Ibba M., Soell D.;
RT   "Activation of the pyrrolysine suppressor tRNA requires formation of a
RT   ternary complex with class I and class II lysyl-tRNA synthetases.";
RL   Mol. Cell 12:287-294(2003).
RN   [3]
RP   FUNCTION, AND KINETIC PARAMETERS.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=15329732; DOI=10.1038/nature02895;
RA   Blight S.K., Larue R.C., Mahapatra A., Longstaff D.G., Chang E., Zhao G.,
RA   Kang P.T., Green-Church K.B., Chan M.K., Krzycki J.A.;
RT   "Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo.";
RL   Nature 431:333-335(2004).
CC   -!- FUNCTION: Catalyzes the attachment of pyrrolysine to tRNA(Pyl).
CC       Pyrrolysine is a lysine derivative encoded by the termination codon
CC       UAG. {ECO:0000269|PubMed:15329732}.
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;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=53 uM for pyrrolysine {ECO:0000269|PubMed:15329732};
CC         KM=2 uM for ATP {ECO:0000269|PubMed:15329732};
CC         Vmax=120 nmol/min/mg enzyme {ECO:0000269|PubMed:15329732};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AY064401; AAL40867.1; -; Genomic_DNA.
DR   EMBL; AY273828; AAQ19545.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WRH6; -.
DR   SMR; Q6WRH6; -.
DR   BioCyc; MetaCyc:MON-15529; -.
DR   BRENDA; 6.1.1.26; 3250.
DR   SABIO-RK; Q6WRH6; -.
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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..419
FT                   /note="Pyrrolysine--tRNA ligase"
FT                   /id="PRO_0000260449"
FT   REGION          100..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        16
FT                   /note="W -> G (in Ref. 1; AAL40867)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="I -> V (in Ref. 1; AAL40867)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   419 AA;  47570 MW;  C22F27D611943BB5 CRC64;
     MDKKPLDVLI SATGLWMSRT GTLHKIKHHE VSRSKIYIEM ACGDHLVVNN SRSCRTARAF
     RHHKYRKTCK RCRVSDEDIN NFLTRSTESK NSVKVRVVSA PKVKKAMPKS VSRAPKPLEN
     SVSAKASTNT SRSVPSPAKS TPNSSVPASA PAPSLTRSQL DRVEALLSPE DKISLNMAKP
     FRELEPELVT RRKNDFQRLY TNDREDYLGK LERDITKFFV DRGFLEIKSP ILIPAEYVER
     MGINNDTELS KQIFRVDKNL CLRPMLAPTL YNYLRKLDRI LPGPIKIFEV GPCYRKESDG
     KEHLEEFTMV NFCQMGSGCT RENLEALIKE FLDYLEIDFE IVGDSCMVYG DTLDIMHGDL
     ELSSAVVGPV SLDREWGIDK PWIGAGFGLE RLLKVMHGFK NIKRASRSES YYNGISTNL