ID A0A399F801_9DEIN Unreviewed; 430 AA.
AC A0A399F801;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ECO:0000313|EMBL:RIH92213.1};
GN ORFNames=Mgrana_01882 {ECO:0000313|EMBL:RIH92213.1};
OS Meiothermus granaticius NBRC 107808.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=1227551 {ECO:0000313|EMBL:RIH92213.1, ECO:0000313|Proteomes:UP000266178};
RN [1] {ECO:0000313|EMBL:RIH92213.1, ECO:0000313|Proteomes:UP000266178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF-68 {ECO:0000313|EMBL:RIH92213.1,
RC ECO:0000313|Proteomes:UP000266178};
RA Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA Egas C.;
RT "Meiothermus granaticius genome AF-68 sequencing project.";
RL Submitted (AUG-2018) 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:RIH92213.1}.
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DR EMBL; QWLB01000023; RIH92213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399F801; -.
DR OrthoDB; 9804243at2; -.
DR Proteomes; UP000266178; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000266178};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 367..428
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT MOTIF 43..52
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 430 AA; 47993 MW; 0B980F5BF59ACCF0 CRC64;
MTLSATKALE ALQVGAVDII PREELFKKLE SGRRLKVKLG LDPTRPDIHI GHAVVLRKMR
QFQELGHKVV IIIGDFTAMI GDPSGRSATR PPLTLEETRA NARSYVEQVG KILITEDPQR
FELRYNSEWL EKLGFAEIIR LTSQLTVAQM LEREDFKNRY TNGIPISIHE FLYPFAQAYD
SVPIQADVEM GGTDQKFNLL VGREVQRAYG LEEQVVFTMP LLVGGDGRKM SKSYDNYIGI
AEEPSEIYRK LMKVEDLYLQ TYFELCTDLT PEEIQGVLEK GGMVGAHRVL ARLLAGAYSQ
PRIPPRLDRS VYEGMGYRLE SAGQDALPGD SLVAEAEARY NAIAKGGIPE DIPVVPINHR
DLQGGQIPLA RLFTLAGLTA SNSEARRVAE QKGLRVNGEV VRDANQPIAL NQPLVLQRGK
DRFVRVQPGD
//
