SYY1_ENTFT
ID SYY1_ENTFT Reviewed; 418 AA.
AC E6ELF6; Q838D7; Q8KXD3;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Tyrosine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE Short=TyrRS 1 {ECO:0000255|HAMAP-Rule:MF_02006};
GN Name=tyrS1 {ECO:0000255|HAMAP-Rule:MF_02006}; Synonyms=tyrS;
GN ORFNames=HMPREF9496_00499;
OS Enterococcus faecalis (strain TX4000 / JH2-2).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=749493;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TX4000 / JH2-2;
RX PubMed=12089039; DOI=10.1128/aem.68.7.3537-3544.2002;
RA Connil N., Le Breton Y., Dousset X., Auffray Y., Rince A., Prevost H.;
RT "Identification of the Enterococcus faecalis tyrosine decarboxylase operon
RT involved in tyramine production.";
RL Appl. Environ. Microbiol. 68:3537-3544(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX4000 / JH2-2;
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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_02006}.
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_02006};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM46083.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EFT42488.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF354231; AAM46083.1; ALT_INIT; Genomic_DNA.
DR EMBL; AEBB01000015; EFT42488.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002355444.1; NZ_GL476258.1.
DR AlphaFoldDB; E6ELF6; -.
DR SMR; E6ELF6; -.
DR GeneID; 60892922; -.
DR PATRIC; fig|749493.3.peg.471; -.
DR HOGENOM; CLU_024003_0_3_9; -.
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_02006; Tyr_tRNA_synth_type1; 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; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
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; RNA-binding.
FT CHAIN 1..418
FT /note="Tyrosine--tRNA ligase 1"
FT /id="PRO_0000422422"
FT DOMAIN 350..416
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 39..48
FT /note="'HIGH' region"
FT MOTIF 228..232
FT /note="'KMSKS' region"
FT BINDING 34
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 166
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 170
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ SEQUENCE 418 AA; 47261 MW; 3136B3CBB783F9F8 CRC64;
MNIIDELAWR DAINQQTNEE GLRELTENTS ISLYCGVDPT GDSMHIGHLI PFMMMKRFQL
AGHHPYILIG GGTGTIGDPS GRTTERVLQT MEAVQHNVDS LSNQMKKLFG KDAEVTMVNN
YDWLSELSLL DFLRDYGKNF NVNTMLAKDI VASRLESGIS FTEFTYQILQ SIDFYTLHKK
HNIQLQIGGA DQWGNITAGL DLIRKKEGPE AKVFGLTIPL MLKADGTKFG KTAGGAIWLD
PKKTSPFEFY QFWLNQDDRD VIKYLKFFTF LDKEEIDALA EKVEKEPGKR EAQRRLAEEV
TRFVHDDAAL EEAQKISEAL FSGNIKDLTI EEIEQGLEHV PTVEITKDAK NIVDWLVDTE
IEPSKRQARE DVSGGAISIN GDRVTDLDFA VDPTQHFDGK FVVVRKGKKN YFLAKVMD
