ID C5CEF0_KOSOT Unreviewed; 397 AA. AC C5CEF0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 02-SEP-2026, entry version 103. DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02007}; DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02007}; DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02007}; DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02007}; GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02007}; GN OrderedLocusNames=Kole_1499 {ECO:0000313|EMBL:ACR80190.1}; OS Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1). OC Bacteria; Thermotogati; Thermotogota; Thermotogae; Kosmotogales; OC Kosmotogaceae; Kosmotoga. OX NCBI_TaxID=521045 {ECO:0000313|EMBL:ACR80190.1, ECO:0000313|Proteomes:UP000002382}; RN [1] {ECO:0000313|EMBL:ACR80190.1, ECO:0000313|Proteomes:UP000002382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1 RC {ECO:0000313|Proteomes:UP000002382}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Noll K.; RT "Complete sequence of Thermotogales bacterium TBF 19.5.1."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACR80190.1, ECO:0000313|Proteomes:UP000002382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1 RC {ECO:0000313|Proteomes:UP000002382}; RX PubMed=21914881; DOI=10.1128/JB.05828-11; RA Swithers K.S., Dipippo J.L., Bruce D.C., Detter C., Tapia R., Han S., RA Goodwin L.A., Han J., Woyke T., Pitluck S., Pennacchio L., Nolan M., RA Mikhailova N., Land M.L., Nesbo C.L., Gogarten J.P., Noll K.M.; RT "Genome Sequence of Kosmotoga olearia Strain TBF 19.5.1, a Thermophilic RT Bacterium with a Wide Growth Temperature Range, Isolated from the Troll B RT Oil Platform in the North Sea."; RL J. Bacteriol. 193:5566-5567(2011). 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_02007}. 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:0000256|ARBA:ARBA00048248, ECO:0000256|HAMAP- CC Rule:MF_02007}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_02007}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC TyrS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02007}. 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; CP001634; ACR80190.1; -; Genomic_DNA. DR RefSeq; WP_015868837.1; NC_012785.1. DR AlphaFoldDB; C5CEF0; -. DR STRING; 521045.Kole_1499; -. DR KEGG; kol:Kole_1499; -. DR eggNOG; COG0162; Bacteria. DR HOGENOM; CLU_024003_5_0_0; -. DR OrthoDB; 9804243at2; -. DR Proteomes; UP000002382; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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; cd00165; S4; 1. DR CDD; cd00805; TyrRS_core; 1. DR FunFam; 1.10.240.10:FF:000006; Tyrosine--tRNA ligase; 1. DR FunFam; 3.40.50.620:FF:000061; 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_02007; Tyr_tRNA_synth_type2; 1. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002942; S4_RNA-bd. 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; IPR024108; Tyr-tRNA-ligase_bac_2. DR NCBIfam; TIGR00234; tyrS; 1. DR PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 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 SMART; SM00363; S4; 1. DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_02007}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02007}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02007}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02007}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_02007}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_02007}; Reference proteome {ECO:0000313|Proteomes:UP000002382}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE- KW ProRule:PRU00182}. FT DOMAIN 337..396 FT /note="RNA-binding S4" FT /evidence="ECO:0000259|SMART:SM00363" FT MOTIF 42..51 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007" FT MOTIF 226..230 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007" FT BINDING 229 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007" SQ SEQUENCE 397 AA; 45748 MW; 861685EA060008F4 CRC64; MEVPEKQLQI LKRNSVSLIS EEELIERLKL GRPLRVKLGV DPSRPDLHLG HAVVLRKLRE FQDLGHHVIL IIGDFTARIG DPSGRSKTRP MLSKEEAKQN AITYSQQAFK ILDRDKTEIK FNSEWLDGMS FEDVIRLSAK YTVARMLERN DFEKRYKNNE PISIAEFLYP LAQAYDSVVV KADVEIGGDD QFFNFVVARK IQEEYGLQPQ VILTMPLIEG TDGNLKMSKS YGNYVAFEDP PEEMFGKLMS IPDTLIIKYM RLLTDIPEER ILQYERDIKS RKINPRDVKM LLAFEITRFF HGEEAAVRAR ENFIKVFRKK ELPSEIPEIK VKESELSLVD LMVKYANISS KSEARRLISQ GGVRLNNTVI KDIHAKVAVS NGDILRIGKR RFFKISC //