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Database: UniProt
Entry: A0A0D2WP07_CAPO3
LinkDB: A0A0D2WP07_CAPO3
Original site: A0A0D2WP07_CAPO3 
ID   A0A0D2WP07_CAPO3        Unreviewed;       651 AA.
AC   A0A0D2WP07;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=CAOG_003878 {ECO:0000313|EMBL:KJE93015.1};
OS   Capsaspora owczarzaki (strain ATCC 30864).
OC   Eukaryota; Filasterea; Capsaspora.
OX   NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE93015.1, ECO:0000313|Proteomes:UP000008743};
RN   [1] {ECO:0000313|Proteomes:UP000008743}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL   Submitted (FEB-2011) 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; KE346364; KJE93015.1; -; Genomic_DNA.
DR   RefSeq; XP_004363606.2; XM_004363549.2.
DR   AlphaFoldDB; A0A0D2WP07; -.
DR   STRING; 595528.A0A0D2WP07; -.
DR   EnsemblProtists; KJE93015; KJE93015; CAOG_003878.
DR   GeneID; 14899301; -.
DR   eggNOG; KOG2144; Eukaryota.
DR   eggNOG; KOG2241; Eukaryota.
DR   InParanoid; A0A0D2WP07; -.
DR   OrthoDB; 1405752at2759; -.
DR   PhylomeDB; A0A0D2WP07; -.
DR   Proteomes; UP000008743; Unassembled WGS 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:UP000008743};
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          489..592
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   REGION          440..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  70746 MW;  A709ACF9D05C5F76 CRC64;
     MSLSVDERFT LINRNLQEIL GADELKKLLA ERDPVLYWGT ATTGRPHIGY FVPMTKIADF
     LKAGCQVTIL FADLHAYLDN MKAPWELLKL RTEYYEAVIK ALLESVGCNL EKLKFVRGTS
     YQLSEAYTLD VYRMSSLVTE HDAKKAGAEV VKQVDNALLS GLLYPGLQAL DEEYLKVDAQ
     FGGVDQRKIF TFAEKYMPAL GYKKRIHLMN PMVPGLQGSK MSSSEPDSKI DLLDDPKAVN
     LKLKKAFCEE GNVENNGVLS FVKMVLMPLR SLKGITTFEI TRPEKYGGNR TFNSFQELED
     AFKNREIFPT DLKNAVETEI NGLLAPIRAR FDNPDLIKLT EQAYPQEALF ALVKNYDAEI
     RKPDANVTAL HAAAVAKAEQ HAPAGPVTDS RGKRTAKGAL LDTLKEMADK PKKVINPSVL
     ARLVTDCFIT VSTVASSSDA AEGESKDAAL ASSSGEAADS GKGKKAAAAS STPKGGKAAA
     AAETEAPVDV ARIDIRVGRI VSAEKHPDAD SLYLEKIDLG EAAPRQVISG LAKFIPLDQL
     QGKLVLCVCN LKPMKMRGIE SQAMVLAASN ADHSIVELLI PPEGSKPGDR VAVEGFAGTP
     DAVLNPKKLV FETVAAEFTT TDDLVAVYRN VPFTVNGKNV VAPTLKKATI K
//
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