ID A0A261Q1S9_9BACT Unreviewed; 429 AA.
AC A0A261Q1S9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=BWI93_18280 {ECO:0000313|EMBL:OZI06769.1};
OS Siphonobacter sp. BAB-5385.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Siphonobacter.
OX NCBI_TaxID=1864822 {ECO:0000313|EMBL:OZI06769.1, ECO:0000313|Proteomes:UP000215802};
RN [1] {ECO:0000313|EMBL:OZI06769.1, ECO:0000313|Proteomes:UP000215802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-5385 {ECO:0000313|EMBL:OZI06769.1,
RC ECO:0000313|Proteomes:UP000215802};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Draft genome of Siphonobacter sp. BAB-5385.";
RL Submitted (JUN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZI06769.1}.
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DR EMBL; NMPS01000186; OZI06769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261Q1S9; -.
DR OrthoDB; 9804243at2; -.
DR Proteomes; UP000215802; Unassembled WGS sequence.
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; 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; 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; 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:UP000215802};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT MOTIF 37..46
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT MOTIF 234..238
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 32
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 167
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 171
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
SQ SEQUENCE 429 AA; 48253 MW; 0060E5E7F758934C CRC64;
MDFIEELRWR GMLQDMMPGT EEQLQKEMTS AYIGFDPTAS SLHIGNLATI MLLVHLQRAG
HKPFALVGGA TGMIGDPSFK AAERSFLSEE TLRFNQDGIR KQLEKFLDFN SGENSAEIVN
NYDWFKDFSF LGFLREAGKF LSVNYMMSKD SVKKRLETGI SFTEFSYQLL QGYDFYHLYK
TQGVKLQMGG SDQWGNITTG TEIIRRKEGG NEEETERRAF ALTTPLVTKA DGTKFGKSES
GNVWLDAEKT SPFQFYQFWL NAADADCPRL IRVFTLLSKE EIEELERQHA EAPHLRILQK
AIAQDVTTRV HSAEAYETAV RASEVLYGKG TLETLQSLDE MTFVQIFDGV PATEISLADY
EAAPNVTDLL ATAQVYPSKG EIRRAIQGNA VSVNKTKVND PNQPADFQLL QGKYLLVAKG
KKNHLVKVV
//
