ID A0A0C3NLN5_PISTI Unreviewed; 415 AA.
AC A0A0C3NLN5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|ARBA:ARBA00013160, ECO:0000256|RuleBase:RU361234};
DE EC=6.1.1.1 {ECO:0000256|ARBA:ARBA00013160, ECO:0000256|RuleBase:RU361234};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033323, ECO:0000256|RuleBase:RU361234};
GN ORFNames=M404DRAFT_163839 {ECO:0000313|EMBL:KIN96218.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIN96218.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIN96218.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIN96218.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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 ECO:0000256|RuleBase:RU361234};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU361234}.
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DR EMBL; KN832051; KIN96218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3NLN5; -.
DR STRING; 870435.A0A0C3NLN5; -.
DR HOGENOM; CLU_024003_0_0_1; -.
DR InParanoid; A0A0C3NLN5; -.
DR OrthoDB; 6875at2759; -.
DR Proteomes; UP000054217; 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 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; IPR001412; aa-tRNA-synth_I_CS.
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:SF0; TYROSINE--TRNA LIGASE, MITOCHONDRIAL; 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; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU361234};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361234};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361234};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361234};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU361234};
KW Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 356..391
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|Pfam:PF01479"
SQ SEQUENCE 415 AA; 46005 MW; E51715FDFF99CBFA CRC64;
MVYAGIDPTA ESLHAGHLIP LLCLLHFQLR GNNIITLIGG ATGLVGDPSG RSTERELSDA
AQVELNASKL TYAISRFFSR ASVYAASRGF TQQSVIPEVQ VLNNINWLKD LNLLDFLRST
GPHFRINQMI ARDSVRTRMN AQQGINFTEF TYQLLQAYDF YELYRTKGCT VQIGGSDQWG
NILSGLELIN KAQFSRATVA EQSSEKGFAL TTPLLTTSSG EKFGKSAGNA IWLDESLSSH
LDFYQFFLRT ADADVVKYLK MFTLLPVEEI ESIAKNHESH PEHRIAQRIL AEEVMLLVHG
EDGLSAAKVA TKVLFGTDYS SLRADQIIRS LRNDPRLVFC SQDEMFAELL PNLTAIHGLL
PSKSAARQLV LAGGLYVNNV PVRDPRLRLT REGLLDGRVA VVRAGKDKHL VLVLK
//