ID   PYLS_METAC              Reviewed;         443 AA.
AC   Q8TUB8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   25-MAY-2022, entry version 114.
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=MA_0155;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM03608.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE010299; AAM03608.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011020213.1; NC_003552.1.
DR   AlphaFoldDB; Q8TUB8; -.
DR   SMR; Q8TUB8; -.
DR   STRING; 188937.MA_0155; -.
DR   EnsemblBacteria; AAM03608; AAM03608; MA_0155.
DR   GeneID; 1472047; -.
DR   KEGG; mac:MA_0155; -.
DR   HOGENOM; CLU_648316_0_0_2; -.
DR   OMA; RPMLAPN; -.
DR   OrthoDB; 25314at2157; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IBA:GO_Central.
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:0006421; P:asparaginyl-tRNA aminoacylation; IBA:GO_Central.
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..443
FT                   /note="Pyrrolysine--tRNA ligase"
FT                   /id="PRO_0000260451"
FT   REGION          103..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   443 AA;  49531 MW;  BC41B079AB388454 CRC64;
     MDKKPLDTLI SATGLWMSRT GMIHKIKHHE VSRSKIYIEM ACGERLVVNN SRSSRTARAL
     RHHKYRKTCR HCRVSDEDIN NFLTKTSEEK TTVKVKVVSA PRVRKAMPKS VARAPKPLEA
     TAQVPLSGSK PAPATPVSAP AQAPAPSTGS ASATSASAQR MANSAAAPAA PVPTSAPALT
     KGQLDRLEGL LSPKDEISLD SEKPFRELES ELLSRRKKDL KRIYAEEREN YLGKLEREIT
     KFFVDRGFLE IKSPILIPAE YVERMGINSD TELSKQVFRI DKNFCLRPML APNLYNYLRK
     LDRALPDPIK IFEIGPCYRK ESDGKEHLEE FTMLNFCQMG SGCTRENLEA IITEFLNHLG
     IDFEIIGDSC MVYGNTLDVM HDDLELSSAV VGPVPLDREW GIDKPWIGAG FGLERLLKVM
     HGFKNIKRAA RSESYYNGIS TNL