SYY_CAMJE
ID SYY_CAMJE Reviewed; 401 AA.
AC Q9PN27; Q0P8Y5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02007};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02007};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02007};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02007};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02007}; OrderedLocusNames=Cj1271c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(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_02007}.
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_02007};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02007}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02007}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007}.
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DR EMBL; AL111168; CAL35386.1; -; Genomic_DNA.
DR PIR; A81335; A81335.
DR RefSeq; WP_002858315.1; NC_002163.1.
DR RefSeq; YP_002344662.1; NC_002163.1.
DR AlphaFoldDB; Q9PN27; -.
DR SMR; Q9PN27; -.
DR IntAct; Q9PN27; 23.
DR STRING; 192222.Cj1271c; -.
DR PaxDb; Q9PN27; -.
DR PRIDE; Q9PN27; -.
DR EnsemblBacteria; CAL35386; CAL35386; Cj1271c.
DR GeneID; 905562; -.
DR KEGG; cje:Cj1271c; -.
DR PATRIC; fig|192222.6.peg.1254; -.
DR eggNOG; COG0162; Bacteria.
DR HOGENOM; CLU_024003_5_0_7; -.
DR OMA; YMMAKDS; -.
DR Proteomes; UP000000799; 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; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02007; Tyr_tRNA_synth_type2; 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; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR PANTHER; PTHR11766:SF1; PTHR11766:SF1; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..401
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000236705"
FT DOMAIN 339..399
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT MOTIF 45..54
FT /note="'HIGH' region"
FT MOTIF 230..234
FT /note="'KMSKS' region"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ SEQUENCE 401 AA; 45420 MW; 8E53115D49CCAB5D CRC64;
MDIKKILAEV KRGCAELIDE ERIENLIKNY YEKGENFFIK AGFDPTAPDL HLGHSVVLTK
MAFLQKHGAI VQFLIGDFTG QIGDPSGKSA TRKKLDKEQV LINAKTYKTQ VFKVLDKEKT
QIKFNSTWLN ELGAAGIVEL TSTFSVARML ERDDFTKRFK EQSPISICEF LYPLLQGYDS
VALKSDIEMG GTDQKFNLLM GRQLQRVYNI GKEQAVIMMP LLEGLDGVNK MSKSLNNYIG
VTEKANDMYA KILSISDELM FRYYELLSQK SLEEIAQIKK DIEQGNLHPK KAKENLALEI
TERFHSKEEA NNAKSEFDRI HSQNALPSDM AEFEIQGKIW LAKALVECGL ESSTSAARRS
ISANAVSVNS QKVSDEQMYL EQGEYILQIG KRKFAKLKVK E