ID M7T611_9ARCH Unreviewed; 346 AA. AC M7T611; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 03-AUG-2022, entry version 41. DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|ARBA:ARBA00013160}; DE EC=6.1.1.1 {ECO:0000256|ARBA:ARBA00013160}; DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033323}; GN ORFNames=MBGDN05_00758 {ECO:0000313|EMBL:EMR74284.1}; OS Thermoplasmatales archaeon SCGC AB-539-N05. OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales. OX NCBI_TaxID=1198116 {ECO:0000313|EMBL:EMR74284.1, ECO:0000313|Proteomes:UP000053781}; RN [1] {ECO:0000313|EMBL:EMR74284.1, ECO:0000313|Proteomes:UP000053781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCGC AB-539-N05 {ECO:0000313|EMBL:EMR74284.1}; RX PubMed=23535597; DOI=10.1038/nature12033; RA Lloyd K.G., Schreiber L., Petersen D.G., Kjeldsen K.U., Lever M.A., RA Steen A.D., Stepanauskas R., Richter M., Kleindienst S., Lenk S., RA Schramm A., Jorgensen B.B.; RT "Predominant archaea in marine sediments degrade detrital proteins."; RL Nature 496:215-218(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L- CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; CC Evidence={ECO:0000256|ARBA:ARBA00000069}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|RuleBase:RU363036}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EMR74284.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ALXL01000015; EMR74284.1; -; Genomic_DNA. DR EnsemblBacteria; EMR74284; EMR74284; MBGDN05_00758. DR PATRIC; fig|1198116.5.peg.117; -. DR Proteomes; UP000053781; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro. DR CDD; cd00805; TyrRS_core; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_02009; Tyr_tRNA_synth_type4; 1. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002307; Tyr-tRNA-ligase. DR InterPro; IPR023678; Tyr-tRNA-ligase_4. DR InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PIRSF; PIRSF006588; TyrRS_arch_euk; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR TIGRFAMs; TIGR00234; tyrS; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|RuleBase:RU363036}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU363036}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, KW ECO:0000256|RuleBase:RU363036}; KW Reference proteome {ECO:0000313|Proteomes:UP000053781}. SQ SEQUENCE 346 AA; 39036 MW; 3DAC4C8042DDE8BF CRC64; MNKVDQIMAN TEEIVTVEEL KVVLGKSKPK AYIGFEPSGT VHLGWKICTN KIKDFIECGF DFTVLLADWH AYINDKLGGD IDKIKLCGKY MEDCFAAMGV DTSQVRFVYA SDYVSDSAYW ELVLRTAKSM SVARVKRAMD IMGRDAEEAE KDLSKLFYPA MQVSDIFYLD LDAAYGGMDQ RRAHMLAREV SKKLGKKAPV AIHTPLLTGL QAGGRMDPVE AKMSKSKPGS MISIHDDPAS VKKKMNKAFC PERQVEGNPV LEICRYVVFP ELKDEVFLIE RPEKFGGNLK FANYKELEQA FVDGLHPLDL KNATAKYVNM ILEPVHTYFE KQPENYNKMK KAGIIQ //