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 16-JUN-2009, entry version 18. 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=Mbur_2086; OS Methanococcoides burtonii (strain DSM 6242). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., RA Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., RA Richardson P.; RT "Complete sequence of Methanococcoides burtonii DSM 6242."; RL Submitted (MAR-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 CC codon UAG (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-pyrrolysine + tRNA(Pyl) = AMP + CC diphosphate + L-pyrrolysyl-tRNA(Pyl). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000300; ABE52960.1; -; Genomic_DNA. DR RefSeq; YP_566710.1; -. DR GeneID; 3998168; -. DR GenomeReviews; CP000300_GR; Mbur_2086. DR KEGG; mbu:Mbur_2086; -. DR NMPDR; fig|259564.8.peg.1993; -. DR HOGENOM; Q12UB6; -. DR OMA; Q12UB6; SGCTREN. DR BioCyc; MBUR259564:MBUR_2086-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 1 416 Pyrrolysyl-tRNA synthetase. FT /FTId=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 //