ID PYLS_METTE Reviewed; 478 AA. AC Q1L6A3; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 17. DE RecName: Full=Pyrrolysyl-tRNA synthetase; DE EC=6.1.1.26; DE AltName: Full=Pyrrolysine--tRNA ligase; DE Short=PylRS; GN Name=pylS; OS Methanosarcina thermophila. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=2210; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Polycarpo C., Ambrogelly A., Herring S., Soell D.G.; RT "The substrate specificity of pyrrolysyl-tRNA synthetase."; RL Submitted (MAY-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; DQ017250; AAY81923.1; -; Genomic_DNA. DR BRENDA; 6.1.1.26; 8918. 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; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 478 Pyrrolysyl-tRNA synthetase. FT /FTId=PRO_0000260454. SQ SEQUENCE 478 AA; 53441 MW; 348D3824845E0278 CRC64; MDKKPLNTLI SATGLWMSRT GKLHKIRHHE VSKRKIYIEM ECGERLVVNN SRSCRAARAL RHHKYRKICK HCRVSDEDLN KFLTRTNEDK SNAKVTVVSA PKIRKVMPKS VARTPKPLEN TAPVQTLPSE SQPAPTTPIS ASTTAPASTS TTAPAPASTT APAPASTTAP ASASTTISTS AMPASTSAQG TTKFNYISGG FPRPIPVQAS APALTKSQID RLQGLLSPKD EISLDSGTPF RKLESELLSR RRKDLKQIYA EEREHYLGKL EREITKFFVD RGFLEIKSPI LIPMEYIERM GIDNDKELSK QIFRVDNNFC LRPMLAPNLY NYLRKLNRAL PDPIKIFEIG PCYRKESDGK EHLEEFTMLN FCQMGSGCTR ENLEAIIKDF LDYLGIDFEI VGDSCMVYGD TLDVMHGDLE LSSAVVGPVP MDRDWGINKP WIGAGFGLER LLKVMHNFKN IKRASRSESY YNGISTNL //