ID M7T611_9EURY Unreviewed; 346 AA. AC M7T611; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 11-DEC-2019, entry version 34. DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02009}; DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02009}; DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02009}; DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02009}; GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02009}; GN ORFNames=MBGDN05_00758 {ECO:0000313|EMBL:EMR74284.1}; OS Thermoplasmatales archaeon SCGC AB-539-N05. OC Archaea; Euryarchaeota; Diaforarchaea group; Thermoplasmata; OC 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 -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and CC then transferred to the acceptor end of tRNA(Tyr). {ECO:0000256|HAMAP- CC Rule:MF_02009}. 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|HAMAP-Rule:MF_02009, CC ECO:0000256|SAAS:SAAS01118004}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02009}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02009}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC TyrS type 4 subfamily. {ECO:0000256|HAMAP-Rule:MF_02009}. 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-UniRule. DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00805; TyrRS_core; 1. DR Gene3D; 3.40.50.620; -; 1. 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|HAMAP-Rule:MF_02009, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00421485, KW ECO:0000313|EMBL:EMR74284.1}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02009, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00421484}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02009}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02009, ECO:0000256|RuleBase:RU363036, KW ECO:0000256|SAAS:SAAS00421486, ECO:0000313|EMBL:EMR74284.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02009, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00421490}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02009, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00421487}; KW Reference proteome {ECO:0000313|Proteomes:UP000053781}. FT COILED 132..152 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 222..226 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02009" FT BINDING 32 FT /note="Tyrosine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02009" FT BINDING 158 FT /note="Tyrosine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02009" FT BINDING 162 FT /note="Tyrosine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02009" FT BINDING 165 FT /note="Tyrosine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02009" FT BINDING 180 FT /note="Tyrosine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02009" FT BINDING 225 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02009" 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 //