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
//