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Database: UniProt
Entry: U6MAY3_EIMMA
LinkDB: U6MAY3_EIMMA
Original site: U6MAY3_EIMMA 
ID   U6MAY3_EIMMA            Unreviewed;       213 AA.
AC   U6MAY3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
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};
DE   Flags: Fragment;
GN   ORFNames=EMWEY_00058300 {ECO:0000313|EMBL:CDJ59624.1};
OS   Eimeria maxima (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ59624.1};
RN   [1] {ECO:0000313|EMBL:CDJ59624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Weybridge {ECO:0000313|EMBL:CDJ59624.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDJ59624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Weybridge {ECO:0000313|EMBL:CDJ59624.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) 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}.
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DR   EMBL; HG720625; CDJ59624.1; -; Genomic_DNA.
DR   RefSeq; XP_013336271.1; XM_013480817.1.
DR   AlphaFoldDB; U6MAY3; -.
DR   EnsemblProtists; CDJ59624; CDJ59624; EMWEY_00058300.
DR   GeneID; 25339816; -.
DR   VEuPathDB; ToxoDB:EMWEY_00058300; -.
DR   OrthoDB; 1405752at2759; -.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR46264:SF4; TYROSINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR46264; TYROSINE-TRNA LIGASE; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363036};
KW   ATP-binding {ECO:0000256|RuleBase:RU363036};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363036}.
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         213
FT                   /evidence="ECO:0000313|EMBL:CDJ59624.1"
SQ   SEQUENCE   213 AA;  23002 MW;  1F0745EDF868E7A6 CRC64;
     MATSAAEGGA VQRSSSSSSS NSSSNSNSNN SNSSNSNGNN NSSSSSSNSS SSSSNSSKGP
     DIFSGYPPPI PSTLSLEERI ARCLSVAEEC IQEDELAKLL EKKQFPIAYD GFEPSGRMHI
     AQGLLKVKNV NKLTSAGCIF VFWVADWFAM LNNKMGGDLK KIRKVGEYFI EVWKSAGMKM
     DNVRFLWASE EIGKAPEVYW QLVMNIAKAN SIS
//
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