ID A0A494W004_9SPHN Unreviewed; 405 AA.
AC A0A494W004;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02006};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02006};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02006};
GN ORFNames=SAMIE_1015050 {ECO:0000313|EMBL:BBD98004.1};
OS Sphingobium amiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=135719 {ECO:0000313|EMBL:BBD98004.1, ECO:0000313|Proteomes:UP000279959};
RN [1] {ECO:0000313|EMBL:BBD98004.1, ECO:0000313|Proteomes:UP000279959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16289 {ECO:0000313|EMBL:BBD98004.1,
RC ECO:0000313|Proteomes:UP000279959};
RA Ootsuka M., Nishizawa T., Ohta H.;
RT "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT Sphingobium amiense DSM 16289T.";
RL Submitted (MAY-2018) 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:0000256|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:0000256|ARBA:ARBA00000069, ECO:0000256|HAMAP-
CC Rule:MF_02006};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02006}.
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DR EMBL; AP018664; BBD98004.1; -; Genomic_DNA.
DR RefSeq; WP_066697512.1; NZ_AP018664.1.
DR AlphaFoldDB; A0A494W004; -.
DR KEGG; sami:SAMIE_1015050; -.
DR Proteomes; UP000279959; 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; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1.
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 NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR11766:SF0; TYROSINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02006};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02006};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02006};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02006}; Reference proteome {ECO:0000313|Proteomes:UP000279959};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 355..393
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|Pfam:PF01479"
FT MOTIF 44..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT MOTIF 236..240
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 39
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 176
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 180
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
SQ SEQUENCE 405 AA; 44177 MW; 708D0EBA630A3260 CRC64;
MSNYQSDLLR LLDERGYIHQ LTDAAGLDAL AAKQVVPGYI GFDPTAPSLH VGSLVQIMML
RRMQQAGHKP IVLMGGGTGK IGDPSLRDEA RSLLTVEKIA ENVASIKRVF ERFLTFGDGP
TDAILVDNAD WLDALEYIPF LRDIGQHFSV NRMLSFDSVK LRLDREQSLS FLEFNYMILQ
AYDFLELSRR AGCRLQMGGS DQWGNIVNGI ELSRRVDGTP VYGLTSPLIT TADGGKMGKT
AKGAVWLNAD ALSPYDYWQF WRNTQDADVG RFMRLFTDLS LDEIARLEAL EGAEINEAKK
ILAHAATAMA HGEDAAAAAA ETARRTFEEG ASDANLPTVS LGGEALTVVQ ANTALGFATS
NKEVRRKLAE GAIRVNGEVV TEPTIILKAG DKISFGAKKH GLIVD
//
