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Database: UniProt
Entry: A0A0G2BIK1_9BACT
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ID   A0A0G2BIK1_9BACT        Unreviewed;       400 AA.
AC   A0A0G2BIK1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=tyrosine--tRNA ligase {ECO:0000256|ARBA:ARBA00013160};
DE            EC=6.1.1.1 {ECO:0000256|ARBA:ARBA00013160};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033323};
GN   ORFNames=UY96_C0019G0015 {ECO:0000313|EMBL:KKW45549.1};
OS   Parcubacteria group bacterium GW2011_GWB1_56_8.
OC   Bacteria.
OX   NCBI_TaxID=1618888 {ECO:0000313|EMBL:KKW45549.1, ECO:0000313|Proteomes:UP000034284};
RN   [1] {ECO:0000313|EMBL:KKW45549.1, ECO:0000313|Proteomes:UP000034284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363036}.
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:KKW45549.1}.
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DR   EMBL; LCSB01000019; KKW45549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2BIK1; -.
DR   PATRIC; fig|1618888.3.peg.709; -.
DR   Proteomes; UP000034284; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
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   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   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   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|RuleBase:RU363036};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363036};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
SQ   SEQUENCE   400 AA;  45208 MW;  3BBCB56EA326A00B CRC64;
     MARTGLKDAG KIRHLLARNV EQVIDRAHLE KTLKSGKKLR IKLGIDPTGE KIHIGRAIVL
     WKLREFQELG HQVVLIIGDF TAQIGDPSDK LSKRPMLSRE QVEKNMRDYL SQIGKILDLH
     KTETRYNSKW LDKLNFRETA ELAESFSVQQ MLHRRNFQER WKEGQDISLR EFLYPIIQGY
     DSVAIKADVE LGGTDQLFNL MAGREVQKQC GQKPQDVMTV GMLSGTDGRK MSTSWGNVIN
     IVDPADEQFG KIMSMHDKMI QDYFHMATRM PEKEIAEQDR ALARGANPRD VKLVLAKEIV
     ALYHGKPAAE KAAEKWVKMF SKKDVSGADI PTLKLKNKKI AAVDLVLKSG AATSKGEAWR
     LIAQGGLKAG EKTISNPRQE LNLKGGEVVR VGKKRFFRIN
//
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