ID F7XLV4_METZD Unreviewed; 427 AA.
AC F7XLV4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Pyrrolysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01573};
DE EC=6.1.1.26 {ECO:0000256|HAMAP-Rule:MF_01573};
DE AltName: Full=Pyrrolysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01573};
DE Short=PylRS {ECO:0000256|HAMAP-Rule:MF_01573};
GN Name=pylS {ECO:0000256|HAMAP-Rule:MF_01573};
GN OrderedLocusNames=Mzhil_1025 {ECO:0000313|EMBL:AEH60882.1};
OS Methanosalsum zhilinae (strain DSM 4017 / NBRC 107636 / OCM 62 / WeN5)
OS (Methanohalophilus zhilinae).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosalsum.
OX NCBI_TaxID=679901 {ECO:0000313|EMBL:AEH60882.1, ECO:0000313|Proteomes:UP000006622};
RN [1] {ECO:0000313|EMBL:AEH60882.1, ECO:0000313|Proteomes:UP000006622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4017 / NBRC 107636 / OCM 62 / WeN5
RC {ECO:0000313|Proteomes:UP000006622};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Spring S., Schueler E., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanosalsum zhilinae DSM 4017.";
RL Submitted (JUL-2010) 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 codon
CC UAG. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01573};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01573}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_01573}.
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DR EMBL; CP002101; AEH60882.1; -; Genomic_DNA.
DR RefSeq; WP_013898320.1; NC_015676.1.
DR AlphaFoldDB; F7XLV4; -.
DR STRING; 679901.Mzhil_1025; -.
DR GeneID; 10822650; -.
DR KEGG; mzh:Mzhil_1025; -.
DR HOGENOM; CLU_648316_0_0_2; -.
DR OrthoDB; 52632at2157; -.
DR Proteomes; UP000006622; Chromosome.
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; 1.10.287.540; Helix hairpin bin; 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 NCBIfam; TIGR02367; PylS_Cterm; 1.
DR NCBIfam; TIGR03912; PylS_Nterm; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01573,
KW ECO:0000313|EMBL:AEH60882.1};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01573};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01573};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01573, ECO:0000313|EMBL:AEH60882.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01573};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01573};
KW Reference proteome {ECO:0000313|Proteomes:UP000006622}.
FT DOMAIN 218..427
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 99..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 49020 MW; 651EB8436752BF72 CRC64;
MTRRSLESLV SEKEVWLSRK GLLHEIKDYS VTQRYINIYT TCGESFSVRN SRRGRASRVL
RNNKYRKICK HCKVPDEKIS KFLQKASVDS TAKVKVVSST KPSQSKKAVP KAVKAKKKGT
ENSNGSLIQS KVKDQGSVNA ISSGQPRSKI QPTEERNNIP AFTPSQKKRL EALLMPEEVI
PDPSENLNFQ ELESSLVNRR KKDIVKIYED DRENQLGKIE RIITKFFVDR GFLEIKSPIL
IPIEYIERMG ITEDKELFEQ VFKVDKNMCL RPMLAPGLYN HLRKFDKVLP DPIRIFEIGP
CYRKESDGSQ HLEEFTMLNF CQMGSMCTRK TLENLIDELL EFMDIEYEIV SDNCHVYGAT
IDVLHKDMEL ASAVVGPIPK DADWGITKPW IGAGFGLERL LKVMHNYKNI RRASRSESYY
NGITTNL
//
