SYY_SACS2
ID SYY_SACS2 Reviewed; 366 AA.
AC P95982;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02009};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02009};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02009};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02009};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02009}; OrderedLocusNames=SSO0078;
GN ORFNames=C04_044;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA Ragan M.A., Charlebois R.L.;
RT "Organizational characteristics and information content of an archaeal
RT genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL Mol. Microbiol. 22:175-191(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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_02009}.
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_02009};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02009}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 4 subfamily. {ECO:0000255|HAMAP-Rule:MF_02009}.
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DR EMBL; Y08257; CAA69524.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40439.1; -; Genomic_DNA.
DR PIR; S75410; S75410.
DR AlphaFoldDB; P95982; -.
DR SMR; P95982; -.
DR STRING; 273057.SSO0078; -.
DR EnsemblBacteria; AAK40439; AAK40439; SSO0078.
DR KEGG; sso:SSO0078; -.
DR PATRIC; fig|273057.12.peg.78; -.
DR eggNOG; arCOG01886; Archaea.
DR HOGENOM; CLU_035267_1_1_2; -.
DR InParanoid; P95982; -.
DR OMA; YIGFEIS; -.
DR PhylomeDB; P95982; -.
DR Proteomes; UP000001974; 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_02009; Tyr_tRNA_synth_type4; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR023678; Tyr-tRNA-ligase_4.
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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..366
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000055671"
FT MOTIF 241..245
FT /note="'KMSKS' region"
FT BINDING 41
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 167
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 171
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 174
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 189
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
SQ SEQUENCE 366 AA; 41820 MW; C02CB985642A4D59 CRC64;
MGKLIMSIDQ RLQLIMRNTA EVITIDELRK KLESDEKLKG YIGFEPSGLF HIGWLIWTQK
VKDLVEAGIN MTLLRAAWHA WINDKLGGDM NLIKMAADYA VEVIKNYGVD VGKLNIVDAD
DIVKEKDYWA LVIKVAKNAS LARIKRALTI MGRRAEEAEI DASKLIYPAM QVSDIFYLDL
DIALGGTDQR KAHMLARDVA EKMGKKKIVS IHTPLLVGLQ GGQRMNITEG MEEDDIQAEI
KMSKSKPESA IFVNDSREDV ERKIMGAYCP KGVAENNPIL QILKYIIFPR YNFVKIERDI
KYGGDVEFKD YEELERTYIE GKIHPMDLKK TTARKLNEIL EPIRKSLEKK PEFEEMIQKI
SKSVTR
