SYY_METMJ
ID SYY_METMJ Reviewed; 315 AA.
AC A3CYG9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02008};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02008};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02008};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02008};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02008}; OrderedLocusNames=Memar_2498;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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_02008}.
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:0000255|HAMAP-Rule:MF_02008};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02008}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_02008}.
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DR EMBL; CP000562; ABN58419.1; -; Genomic_DNA.
DR RefSeq; WP_011845328.1; NC_009051.1.
DR AlphaFoldDB; A3CYG9; -.
DR SMR; A3CYG9; -.
DR STRING; 368407.Memar_2498; -.
DR EnsemblBacteria; ABN58419; ABN58419; Memar_2498.
DR GeneID; 4848401; -.
DR KEGG; mem:Memar_2498; -.
DR eggNOG; arCOG01886; Archaea.
DR HOGENOM; CLU_035267_0_1_2; -.
DR OMA; YIGFEIS; -.
DR OrthoDB; 59062at2157; -.
DR Proteomes; UP000002146; Chromosome.
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_02008; Tyr_tRNA_synth_type3; 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; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR023684; Tyr-tRNA-ligase_3.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..315
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000303678"
FT MOTIF 37..45
FT /note="'HIGH' region"
FT MOTIF 208..212
FT /note="'KMSKS' region"
FT BINDING 32
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 152
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 156
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 159
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 174
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
SQ SEQUENCE 315 AA; 35082 MW; 5AA8C1CC9298B543 CRC64;
MDPYELVTRN TVEVVTDEEL RALIDRPVRR VYTGYEPSGE IHLGHMVTVN KLMDLQQAGF
EVTVLIADLH AFLNRKGTME EIRETAEYNR RCFEGLGLRG ANYVLGSDVQ LTPEYELAVL
ELSQAITLNR AKRSMDEVGR QMDNPTVSQM VYPIMQMVDI ATLGVDAAVG GIDQRKIHML
AREHLPSIGY PAPVCIHTPI INGLDGKKMS SSAGNVISVA DSEEDIKKKM KKAFCPPEVE
NNPVLEILRY HVFPRAGAVA IRRPEKFGGD REFAAYEDLE RAYAAGEIHP LDLKNAAAAH
LIDILAPVHD YVCSR
