ID A0A1C3CYY1_9GAMM Unreviewed; 404 AA.
AC A0A1C3CYY1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02007};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02007};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02007};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02007};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02007};
GN ORFNames=BBP83_14580 {ECO:0000313|EMBL:ODA13996.1};
OS Acinetobacter celticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1891224 {ECO:0000313|EMBL:ODA13996.1, ECO:0000313|Proteomes:UP000186553};
RN [1] {ECO:0000313|EMBL:ODA13996.1, ECO:0000313|Proteomes:UP000186553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4603 {ECO:0000313|EMBL:ODA13996.1,
RC ECO:0000313|Proteomes:UP000186553};
RA Radolfova-Krizova L., Nemec A.;
RT "Acinetobacter sp. ANC 4603.";
RL Submitted (JUL-2016) 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_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:0000256|ARBA:ARBA00000069, ECO:0000256|HAMAP-
CC Rule:MF_02007};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02007}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02007}.
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:ODA13996.1}.
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DR EMBL; MBDL01000005; ODA13996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3CYY1; -.
DR STRING; 1891224.BBP83_14580; -.
DR Proteomes; UP000186553; 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; 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_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 NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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_02007};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02007}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02007};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02007};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02007}; RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 342..402
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT MOTIF 45..54
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT MOTIF 229..233
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
SQ SEQUENCE 404 AA; 44765 MW; 6182E7D21D77E141 CRC64;
MSNFLPAEEQ LALIQRGTHE IISEEDLLKK LKENRPLKIK AGFDPTAPDL HLGHTVLINK
LKVFQDLGHD VTFLIGDYTA MIGDPTGKSA TRPPLSREQV LENAKTYQEQ VFKILDPKKT
KVRFNSEWFA EKTAADLIQL ASQQTVARML ERDDFTKRYN NHQPIAIHEF LYPLVQGYDS
IALEADVELG GTDQTFNLLM GRTLQGRFDQ EAQVCITVPI LEGLDGVNKM SKSLGNYIGV
FDAPGAMYQK VLSMPDSLIE RYFDLLSFKS IEEIQLLLKE VAEGCNPQDV KKILALELVE
RFHGSDAAAH AHKGAGNLIT EGELPEGTPE VTISRAEFGG ELFITSILRE AGLTKNAAQA
KDAIARGAVK VDWNTVDASF SVKENVTLIV QASKKAIAKV IFID
//
