UniProt: A0A0M4EE41

Database: UniProt
Entry: A0A0M4EE41_DROBS

LinkDB:  A0A0M4EE41_DROBS 
Original site:  A0A0M4EE41_DROBS

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
All databases (19)   

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ID   A0A0M4EE41_DROBS        Unreviewed;       527 AA.
AC   A0A0M4EE41;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|RuleBase:RU361234};
DE            EC=6.1.1.1 {ECO:0000256|RuleBase:RU361234};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|RuleBase:RU361234};
GN   ORFNames=Dbus_chr3Lg1150 {ECO:0000313|EMBL:ALC43984.1},
GN   Dbus_chr3Lg2008 {ECO:0000313|EMBL:ALC44842.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC43984.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC43984.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC43984.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-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:ARBA00034238};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10221;
CC         Evidence={ECO:0000256|ARBA:ARBA00034238};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU361234}.
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DR   EMBL; CP012525; ALC43984.1; -; Genomic_DNA.
DR   EMBL; CP012525; ALC44842.1; -; Genomic_DNA.
DR   RefSeq; XP_017841001.1; XM_017985512.1.
DR   RefSeq; XP_017841003.1; XM_017985514.1.
DR   AlphaFoldDB; A0A0M4EE41; -.
DR   STRING; 30019.A0A0M4EE41; -.
DR   GeneID; 108598793; -.
DR   OMA; RKIHMLA; -.
DR   OrthoDB; 1405752at2759; -.
DR   Proteomes; UP000494163; Chromosome 3l sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd02799; tRNA_bind_EMAP-II_like; 1.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 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   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11586; TRNA-AMINOACYLATION COFACTOR ARC1 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11586:SF33; TYROSINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS50886; TRBD; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU361234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00209};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW   ProRule:PRU00209}.
FT   DOMAIN          365..468
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
SQ   SEQUENCE   527 AA;  58328 MW;  E9ADD75493EFA36F CRC64;
     MVGSLSVEEK KQLITRNLQE TLGEDKLQKV LAERDLKIYW GTATTGKPHV AYFVPMSKIA
     DFLKAGCEVT ILFADLHAYL DNMKAPWSLL ELRTKYYEQV IKAMLSSIGV PLDKLKFVKG
     SDYQLSKEYT LDVYKLSSLV TIHDAKKAGA EVVKQVEYPL LSGLLYPGLQ GLDEEYLKVD
     AQFGGVDQRK IFTFSEKYLP QLGYEKRIHF MNPMVPGLAG GKMSSSEEDS KIDLLDSPAN
     VKKKLKKAFC EPGNIADNGL LSFVKHVLFS LFKEGEGFEI LRAPDNGGDV TFNNFADLEQ
     YYADNKLHPG DLKASVEKYI NRLLEPIRKT FESPELQKLT AAAYPPPAKV KAGAAPAAAA
     ADENAPHRLD IRVGKVIEVA RHPDADTLYV LKIDLAEAQP RTIISGLVKF VTVEELDQRL
     VAVLCNLKPS KMRGILSEGM VLCTSNADHT VVEPIIVPAA AKPGSRLAFD GYSGTPDEQL
     NPKKKVWEKL SEDFKTNADG IAVWKDNFLL TTEGEQLTSK LANCAIK
//

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