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Database: UniProt
Entry: A0A1F8EWJ1_9BACT
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ID   A0A1F8EWJ1_9BACT        Unreviewed;       393 AA.
AC   A0A1F8EWJ1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=A2746_01050 {ECO:0000313|EMBL:OGN05232.1};
OS   Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_01_FULL_44_22.
OC   Bacteria; Candidatus Yanofskybacteria.
OX   NCBI_TaxID=1802669 {ECO:0000313|EMBL:OGN05232.1, ECO:0000313|Proteomes:UP000177419};
RN   [1] {ECO:0000313|EMBL:OGN05232.1, ECO:0000313|Proteomes:UP000177419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGN05232.1}.
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DR   EMBL; MGJJ01000015; OGN05232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8EWJ1; -.
DR   STRING; 1802669.A2746_01050; -.
DR   Proteomes; UP000177419; 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; cd00165; S4; 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; 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   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 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|RuleBase:RU363036};
KW   ATP-binding {ECO:0000256|RuleBase:RU363036};
KW   Ligase {ECO:0000256|RuleBase:RU363036, ECO:0000313|EMBL:OGN05232.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363036};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          345..381
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|Pfam:PF01479"
SQ   SEQUENCE   393 AA;  44743 MW;  8F5EA152EF0AD88F CRC64;
     MFWNKINTDS GKIENLLSWG VEEIFEADSL RKKLLSGEKL RVKFGVDPTM NTLHLGHSLP
     LKKLQQFLDL GHQVVLLIGD FTATIGDPSG RLRERPVLSR QEVERNMKEY VRQAGKILDT
     RKAEIRHNSE WYEKKDARFF MELASQFTYA RLMDRAEFKE RIRSGGNVTM AELFYPLLQG
     YDSVELGADV EIGGTEQKFN LLMGRKVQKR FGLPEQDIMT VPLLVGTDGE KKMSKSYGNF
     IALDDKSNIM FAKIMSIPDS LVWQYFSLLT DEQPERTEER RKTAGTDIFN HKKDLSQLIV
     ARFYGEKSAQ AARDEFAKVF SQKGLPSEIE GVEGAGKLII ETGPGLNVSK SEIKRLIDEG
     AVSVNGKIIK DWHYQLQSDD LLKIGSHKFV KIK
//
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