SYY2_PYRAE
ID SYY2_PYRAE Reviewed; 316 AA.
AC Q8ZW77;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Tyrosine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_02009};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02009};
DE AltName: Full=Tyrosyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_02009};
DE Short=TyrRS 2 {ECO:0000255|HAMAP-Rule:MF_02009};
GN Name=tyrS2 {ECO:0000255|HAMAP-Rule:MF_02009}; OrderedLocusNames=PAE1931;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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 {ECO:0000255|HAMAP-Rule:MF_02009}.
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; AE009441; AAL63825.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZW77; -.
DR SMR; Q8ZW77; -.
DR STRING; 178306.PAE1931; -.
DR EnsemblBacteria; AAL63825; AAL63825; PAE1931.
DR KEGG; pai:PAE1931; -.
DR PATRIC; fig|178306.9.peg.1429; -.
DR eggNOG; arCOG01886; Archaea.
DR HOGENOM; CLU_035267_1_1_2; -.
DR InParanoid; Q8ZW77; -.
DR OMA; VATWHAW; -.
DR Proteomes; UP000002439; 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 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..316
FT /note="Tyrosine--tRNA ligase 2"
FT /id="PRO_0000240267"
FT MOTIF 219..223
FT /note="'KMSKS' region"
FT BINDING 26
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 146
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 150
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 153
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 168
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
SQ SEQUENCE 316 AA; 36004 MW; D9CDE761F1F6B890 CRC64;
MERLLMNVEE VVTREEFLRL KGGSAYLGFE PLWPIHIGWL IWAYKLAELK EAGFDVIVLV
ATWHAWINDK GSIEELRAHG ERVRAVLDRI GKFKYVYGDD VAKDPKYWEL VVKIAKETSL
ARVKRATPVM GRRAEEVELD FSKLMYPLMQ VADIFYLGVD VAVGGMDQRR AHMLARDVAE
KLGLKKPIAL HTPIITSLSG TGRMEGTHRE IDEVYAMYKM SKSKPQSAIL ITDSEEDVRK
KIWAAYCPPR ETKFNPVFEI AAYLLIPYHG PLEIKGRRYE EGNALERDYR EGVVTPQELK
EAVASALVGL LSKLKL