ID A0A0J6YPH0_9BACT Unreviewed; 404 AA.
AC A0A0J6YPH0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=UR09_05940 {ECO:0000313|EMBL:KMP10526.1};
OS Candidatus Nitromaritima sp. SCGC AAA799-A02.
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Candidatus Nitromaritima.
OX NCBI_TaxID=1628278 {ECO:0000313|EMBL:KMP10526.1, ECO:0000313|Proteomes:UP000035948};
RN [1] {ECO:0000313|EMBL:KMP10526.1, ECO:0000313|Proteomes:UP000035948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC_AAA799_A02 {ECO:0000313|EMBL:KMP10526.1};
RA Ngugi D.K., Blom J., Stepanauskas R., Stingl U.;
RT "Diversification and niche adaptations of Nitrospina-like bacteria in the
RT poly-extreme interfaces of the Atlantis II Deep brine from the Red Sea.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KMP10526.1}.
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DR EMBL; JZKI01000062; KMP10526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6YPH0; -.
DR PATRIC; fig|1628278.3.peg.1228; -.
DR Proteomes; UP000035948; 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 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|RuleBase:RU363036,
KW ECO:0000313|EMBL:KMP10526.1}; ATP-binding {ECO:0000256|RuleBase:RU363036};
KW Ligase {ECO:0000256|RuleBase:RU363036};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363036};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363036};
KW Reference proteome {ECO:0000313|Proteomes:UP000035948};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
SQ SEQUENCE 404 AA; 46727 MW; C827896C25B06A90 CRC64;
MASSESNKQL LDSFARTTAE LFSLKEFEEL LESGKQIRIK YGVDVTSPYL HIGHAVNLWM
MRELQDMGHK VIFLIGDFTT QIGDPTGRSN TRPIIPREEI DKNAEEFIRQ AKMVLRFDDP
NLLEIRRNSE WFSGYALSEF LKLMAMVTHA RLISRDMFQN RIESQEDIYM HEMIYPILQG
YDSYVLESDL TIIGTDQLFN EMLGRFYQQK FGQKPQVIIT TKITPGIDGK AKQSKSLDNY
IGLGHSARDK FGRCMKVPDE LIVDYLKVYT KVPMEAVAEI DKEVSSDPMK WKKYLAGEIL
KRYHDEASAK REQEWFENTF SKKITPDDIP LLNLEESQWI AFDLVKKYFD DSKSNSEVRR
LFQQGAVSLN SRKISSFDEK VEVASDDVVK VGKRTWFKIR VGGG
//