SYY_HALSA
ID SYY_HALSA Reviewed; 327 AA.
AC Q9HN62;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=VNG_2237G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG20359.1; -; Genomic_DNA.
DR PIR; C84374; C84374.
DR RefSeq; WP_010903660.1; NC_002607.1.
DR AlphaFoldDB; Q9HN62; -.
DR SMR; Q9HN62; -.
DR STRING; 64091.VNG_2237G; -.
DR PaxDb; Q9HN62; -.
DR EnsemblBacteria; AAG20359; AAG20359; VNG_2237G.
DR GeneID; 5953300; -.
DR GeneID; 62887520; -.
DR KEGG; hal:VNG_2237G; -.
DR PATRIC; fig|64091.14.peg.1719; -.
DR HOGENOM; CLU_035267_0_1_2; -.
DR InParanoid; Q9HN62; -.
DR OMA; YIGFEIS; -.
DR OrthoDB; 59062at2157; -.
DR PhylomeDB; Q9HN62; -.
DR Proteomes; UP000000554; 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; Reference proteome.
FT CHAIN 1..327
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000240253"
FT MOTIF 38..46
FT /note="'HIGH' region"
FT MOTIF 212..216
FT /note="'KMSKS' region"
FT BINDING 33
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 154
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 158
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 161
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 176
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
SQ SEQUENCE 327 AA; 36423 MW; 571705121336E9A3 CRC64;
MNAYERITRN TAEVVTEEEV RELAEDPEGK RVYVGYEPSG VLHLGHLLTA NKLMDLQDAG
MEVVVLLADV HAYLNDKGSF EEIRATADQM KAQFLAYGLD EDQTEFVLGS SFQLDEDYEL
DLHAMQVETS LKRAQRAMAE IQSGETPKVS HVVYPLMQAL DIEYLDLDLA IGGMDQRKVH
MLAREELPSV GYEKRPVLHT PIIGDLGSGD GKMSSSEGVT ISMEDSTADI EEKVTGAFCP
QTRDPEGETV NPVLELFQYH VFPRFDEVVV QRPDEYGGDL VYESYEDLAD DLESGELHPA
DAKGALAAAL DELIEPGRQR LREIRGE
