ID SYY1_CLOAB Reviewed; 407 AA. AC Q97LC5; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 02-SEP-2026, entry version 119. DE RecName: Full=Tyrosine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_02006}; DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006}; DE AltName: Full=Tyrosyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_02006}; DE Short=TyrRS 1 {ECO:0000255|HAMAP-Rule:MF_02006}; GN Name=tyrS1 {ECO:0000255|HAMAP-Rule:MF_02006}; GN OrderedLocusNames=CA_C0637; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM OS 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W). OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC RC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W; RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., RA Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). 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:0000255|HAMAP- CC Rule:MF_02006}. CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Tyr) + L-tyrosine + ATP = L-tyrosyl-tRNA(Tyr) + AMP + CC diphosphate + H(+); 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:0000255|HAMAP-Rule:MF_02006}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}. 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; AE001437; AAK78614.1; -; Genomic_DNA. DR PIR; C96978; C96978. DR RefSeq; WP_010963956.1; NC_003030.1. DR AlphaFoldDB; Q97LC5; -. DR SMR; Q97LC5; -. DR STRING; 272562.CA_C0637; -. DR GeneID; 44997148; -. DR KEGG; cac:CA_C0637; -. DR PATRIC; fig|272562.8.peg.840; -. DR eggNOG; COG0162; Bacteria. DR HOGENOM; CLU_024003_0_3_9; -. DR OrthoDB; 9804243at2; -. DR Proteomes; UP000000814; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-ARBA. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. 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 FunFam; 1.10.240.10:FF:000001; Tyrosine--tRNA ligase; 1. DR FunFam; 3.40.50.620:FF:000008; Tyrosine--tRNA ligase; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1. DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1. DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR036986; S4_RNA-bd_sf. DR InterPro; IPR054608; SYY-like_C. DR InterPro; IPR002307; Tyr-tRNA-ligase. DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type. DR InterPro; IPR024107; Tyr-tRNA-ligase_bac_1. DR NCBIfam; TIGR00234; tyrS; 1. DR PANTHER; PTHR11766:SF0; TYROSINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1. DR Pfam; PF22421; SYY_C-terminal; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding. FT CHAIN 1..407 FT /note="Tyrosine--tRNA ligase 1" FT /id="PRO_0000234697" FT DOMAIN 340..406 FT /note="S4 RNA-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006" FT MOTIF 40..49 FT /note="'HIGH' region" FT MOTIF 228..232 FT /note="'KMSKS' region" FT BINDING 35 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006" FT BINDING 168 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006" FT BINDING 172 FT /ligand="L-tyrosine" FT /ligand_id="ChEBI:CHEBI:58315" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006" FT BINDING 231 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006" SQ SEQUENCE 407 AA; 46435 MW; 5F8DF6AA81772D5C CRC64; MSNVLDELIE RGYAKQFTHE EETRKLLSEE KVTFYIGFDP TGDSLHVGHF IALMLMARMQ KAGHRPIVLI GGGTAMVGDP TGKTDMRKML TREEINHNVE CLKKQMSRFI DFSDDKAIIV NNAEWLMGQN YIEFLREVGV HFSVNKMLTA ECFKQRMEKG LSFLEFNYML MQGFDFYKLN EKYDCKMELG GDDQWSNMIA GVELIRRKSN KKAYAMTSAL LTNSEGKKMG KTEKGALWLD AEKTSPYDFF QYWRNVNDAD VEKCLSMLTF LPMDEVRRLA SLKDQEINKA KEVLAYEVTK LVHGEEEAKK ALNSSKALFG GGTNMDNVPT VSIPEDMLSS SILDVLVHTK IIPSKGEGRR LVQQGGITLN DTKVEDFNYE ITKEDFNDDG FALVRRGKKK YYKIVIG //