ID   PYLS_METBF              Reviewed;         419 AA.
AC   Q46E77;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Pyrrolysyl-tRNA synthetase;
DE            EC=6.1.1.26;
DE   AltName: Full=Pyrrolysine--tRNA ligase;
DE            Short=PylRS;
GN   Name=pylS; OrderedLocusNames=Mbar_A0839;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   FUNCTION.
RX   PubMed=15314242; DOI=10.1073/pnas.0405362101;
RA   Polycarpo C., Ambrogelly A., Berube A., Winbush S.M., McCloskey J.A.,
RA   Crain P.F., Wood J.L., Soell D.;
RT   "An aminoacyl-tRNA synthetase that specifically activates
RT   pyrrolysine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12450-12454(2004).
CC   -!- FUNCTION: Catalyzes the attachment of pyrrolysine to tRNA(Pyl).
CC       Pyrrolysine is a lysine derivative encoded by the termination
CC       codon UAG.
CC   -!- CATALYTIC ACTIVITY: ATP + L-pyrrolysine + tRNA(Pyl) = AMP +
CC       diphosphate + L-pyrrolysyl-tRNA(Pyl).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000099; AAZ69815.1; -; Genomic_DNA.
DR   RefSeq; YP_304395.1; -.
DR   GeneID; 3625577; -.
DR   GenomeReviews; CP000099_GR; Mbar_A0839.
DR   KEGG; mba:Mbar_A0839; -.
DR   NMPDR; fig|269797.3.peg.315; -.
DR   HOGENOM; Q46E77; -.
DR   OMA; Q46E77; SGCTREN.
DR   BioCyc; MBAR269797:MBAR_A0839-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:HAMAP.
DR   HAMAP; MF_01573; -; 1.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR012739; PylS.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   TIGRFAMs; TIGR02367; PylS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    419       Pyrrolysyl-tRNA synthetase.
FT                                /FTId=PRO_0000260450.
SQ   SEQUENCE   419 AA;  47690 MW;  3AA51387F53F8350 CRC64;
     MDKKPLDVLI SATGLWMSRT GTLHKIKHYE VSRSKIYIEM ACGDHLVVNN SRSCRTARAF
     RHHKYRKTCK RCRVSDEDIN NFLTRSTEGK TSVKVKVVSA PKVKKAMPKS VSRAPKPLEN
     PVSAKASTDT SRSVPSPAKS TPNSPVPTSA PAPSLTRSQL DRVEALLSPE DKISLNIAKP
     FRELESELVT RRKNDFQRLY TNDREDYLGK LERDITKFFV DRDFLEIKSP ILIPAEYVER
     MGINNDTELS KQIFRVDKNL CLRPMLAPTL YNYLRKLDRI LPDPIKIFEV GPCYRKESDG
     KEHLEEFTMV NFCQMGSGCT RENLESLIKE FLDYLEIDFE IVGDSCMVYG DTLDIMHGDL
     ELSSAVVGPV PLDREWGIDK PWIGAGFGLE RLLKVMHGFK NIKRASRSES YYNGISTNL
//