SYYC_PONAB
ID SYYC_PONAB Reviewed; 528 AA.
AC Q5R8T5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Tyrosine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
DE Contains:
DE RecName: Full=Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed;
GN Name=YARS1; Synonyms=YARS;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CR859664; CAH91825.1; -; mRNA.
DR RefSeq; NP_001126056.1; NM_001132584.1.
DR AlphaFoldDB; Q5R8T5; -.
DR SMR; Q5R8T5; -.
DR STRING; 9601.ENSPPYP00000001828; -.
DR GeneID; 100173008; -.
DR KEGG; pon:100173008; -.
DR CTD; 8565; -.
DR eggNOG; KOG2144; Eukaryota.
DR eggNOG; KOG2241; Eukaryota.
DR InParanoid; Q5R8T5; -.
DR OrthoDB; 852081at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA 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; cd00805; TyrRS_core; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..528
FT /note="Tyrosine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000423287"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT CHAIN 2..528
FT /note="Tyrosine--tRNA ligase, cytoplasmic, N-terminally
FT processed"
FT /id="PRO_0000239690"
FT DOMAIN 364..468
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT REGION 339..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000250"
FT MOTIF 222..226
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 2
FT /note="N-acetylglycine; in Tyrosine--tRNA ligase,
FT cytoplasmic, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 474
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 482
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 490
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
SQ SEQUENCE 528 AA; 59167 MW; 67A3AB8DC6755225 CRC64;
MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV AYFVPMSKIA
DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV IKAMLESIGV PLEKLTFIKG
TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
AQFGGVDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED
VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD ERWGGNKTYT AYMDLEKDFA
AEVVHPGDLK NSVDVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM AKGPAKNSEP
EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV
VVLCNLKPQK MRGVESQGML LCASIEGINR QVEPLDPPAG SAPGERVFVK GYEKGQPDEE
LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGSISCK SLKGGNIS
