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-NOV-2015, entry version 14. DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02009, ECO:0000256|SAAS:SAAS00011232}; DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02009, ECO:0000256|SAAS:SAAS00011232}; DE AltName: Full=Tyrosyl-tRNA synthetase {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; Thermoplasmata; Thermoplasmatales. OX NCBI_TaxID=1198116 {ECO:0000313|EMBL:EMR74284.1}; RN [1] {ECO:0000313|EMBL:EMR74284.1} RP NUCLEOTIDE SEQUENCE. 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). RN [2] {ECO:0000313|EMBL:EMR74284.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCGC AB-539-N05 {ECO:0000313|EMBL:EMR74284.1}; RA Lloyd K., Schreiber L., Petersen D., Kjeldsen K., Lever M., RA Steen A.D., Stepanauskas R., Richter M., Kleindienst S., Lenk S., RA Schramm A., Jorgensen B.B.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a CC two-step reaction: tyrosine is first activated by ATP to form Tyr- CC AMP and then transferred to the acceptor end of tRNA(Tyr). CC {ECO:0000256|HAMAP-Rule:MF_02009}. CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP + CC diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000256|HAMAP- CC Rule:MF_02009, ECO:0000256|SAAS:SAAS00011233}. 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 CC family. TyrS type 4 subfamily. {ECO:0000256|HAMAP-Rule:MF_02009}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. 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|SAAS:SAAS00011234}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02009, KW ECO:0000256|SAAS:SAAS00011243}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02009}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02009, KW ECO:0000256|SAAS:SAAS00011245}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02009, KW ECO:0000256|SAAS:SAAS00011248}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02009, KW ECO:0000256|SAAS:SAAS00011244}. FT COILED 132 152 {ECO:0000256|SAM:Coils}. FT MOTIF 222 226 "KMSKS" region. {ECO:0000256|HAMAP-Rule: FT MF_02009}. FT BINDING 32 32 Tyrosine. {ECO:0000256|HAMAP-Rule: FT MF_02009}. FT BINDING 158 158 Tyrosine. {ECO:0000256|HAMAP-Rule: FT MF_02009}. FT BINDING 162 162 Tyrosine. {ECO:0000256|HAMAP-Rule: FT MF_02009}. FT BINDING 165 165 Tyrosine. {ECO:0000256|HAMAP-Rule: FT MF_02009}. FT BINDING 180 180 Tyrosine. {ECO:0000256|HAMAP-Rule: FT MF_02009}. FT BINDING 225 225 ATP. {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 //