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
//