ID M1NY06_9CORY Unreviewed; 421 AA.
AC M1NY06;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02006};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02006};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02006};
GN ORFNames=A605_06890 {ECO:0000313|EMBL:AGF72380.1};
OS Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF72380.1, ECO:0000313|Proteomes:UP000011723};
RN [1] {ECO:0000313|EMBL:AGF72380.1, ECO:0000313|Proteomes:UP000011723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF72380.1};
RX PubMed=23408721;
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA Kalinowski J.;
RT "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT type strain YIM 70093(T) (= DSM 44683(T)).";
RL Stand. Genomic Sci. 7:284-293(2012).
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_02006}.
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, ECO:0000256|HAMAP-
CC Rule:MF_02006};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000256|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; CP003697; AGF72380.1; -; Genomic_DNA.
DR RefSeq; WP_015400799.1; NZ_JIAJ01000015.1.
DR AlphaFoldDB; M1NY06; -.
DR STRING; 1121362.A605_06890; -.
DR KEGG; chn:A605_06890; -.
DR PATRIC; fig|1121362.3.peg.1391; -.
DR eggNOG; COG0162; Bacteria.
DR HOGENOM; CLU_024003_0_2_11; -.
DR OrthoDB; 9804243at2; -.
DR Proteomes; UP000011723; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 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; 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; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02006};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02006};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02006};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02006}; Reference proteome {ECO:0000313|Proteomes:UP000011723};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT MOTIF 39..48
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT MOTIF 228..232
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 34
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 168
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 172
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
SQ SEQUENCE 421 AA; 46702 MW; E8F6DDCA3E15985B CRC64;
MNIIDELSWR GLINQSTDLD ELKKATEAGP ITLYCGFDPT GPSLHAGHLV PLLMLYRFQR
AGHRPLVLAG GATGMIGDPR DVGERSMNDA GTVEDWAGRI SGQLQRFVSF EGDNAAVLVN
NNDWTKDMSV ISFLRDVGKH FSLNTMLSRD TVKRRLENDG ISYTEFSYML LQANDFVQLR
RNYDCVLQVG GGDQWGNLVA GVDLNRRIDG ATVHALTVPL VTDSEGKKFG KSTGGGSLWL
DPEMTSPYTW YQYFINAADA DVIRYLRWFT FLTQEELAEL ETEVAERPFK REAQRRLARE
MTNLVHGEEA TVAVELAAQA LFGKAELADL DERTLASAVS ETEVFEVRAG EPRTIVDLLV
GAGLVDSRGA ARRAIKEGGA YVNNVRIESE EWEPATEDLL HGTWLVLRRG KKNFAGVKIN
G
//
