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Database: UniProt
Entry: A0A0V1NZK2_9BILA
LinkDB: A0A0V1NZK2_9BILA
Original site: A0A0V1NZK2_9BILA 
ID   A0A0V1NZK2_9BILA        Unreviewed;       817 AA.
AC   A0A0V1NZK2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|ARBA:ARBA00013160, ECO:0000256|RuleBase:RU361234};
DE            EC=6.1.1.1 {ECO:0000256|ARBA:ARBA00013160, ECO:0000256|RuleBase:RU361234};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033323, ECO:0000256|RuleBase:RU361234};
GN   Name=Uba3 {ECO:0000313|EMBL:KRZ89333.1};
GN   ORFNames=T08_12987 {ECO:0000313|EMBL:KRZ89333.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ89333.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ89333.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ89333.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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:ARBA00000069,
CC         ECO:0000256|RuleBase:RU361234};
CC   -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU361234}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ89333.1}.
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DR   EMBL; JYDM01000071; KRZ89333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1NZK2; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045116; P:protein neddylation; IEA:InterPro.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR   Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014929; E2-binding.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11766:SF0; TYROSINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08825; E2_bind; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SMART; SM01181; E2_bind; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 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};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU361234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT   DOMAIN          723..810
FT                   /note="E2 binding"
FT                   /evidence="ECO:0000259|SMART:SM01181"
SQ   SEQUENCE   817 AA;  91736 MW;  011AAA88B3C8FF3D CRC64;
     MKHFWHCLRV FLKYHSSQSS TDVVEAVQCA IRRGAIKTSF PDSLLNNLES IRGVHPCIYA
     GFDPSSDSLH IGNLATSRLG DPSGRSVERD RLSLEEIQSN SQSIQFTLKS ILRNFEKIKI
     SLNSTNVLST PAVLDNTDWY HQMNVLDFFD VVGRAFRLRH MMDKQCISER IHREGMSYAE
     FSYQTLQAYD WLHLYEKFGC LLQIGGADQT GNIHSGHDLI RFFHNQSAYG LLVPLMLSST
     GEKIGKSVGS SLWLSSSRTS SFVFYQYFLQ LTDKEANSMM KLFSFCSEAD LERILDDHCQ
     QPEKRIAQRF LADQLTLLVH SESGLALAKR ITEILFDHRL HGIGDLDEND LNILCREVPG
     VQLSRQALPI SAISLALKAG CFDDVNTAER TINQGGFHVN NFKITNPTIV SMNRWHCVRK
     LLERSGPFAH PEFVPSVENI DLIGTCRVLV IGAGGLGCEL LKDLVMPFLD FETFMQKDIG
     KSKAIVAAEA IERRLPFCSV TPHFCRIEEK PLSFYESFAV IVAGLDSISA RRWINRTLVR
     LLRYDDKGEL DMASVIPLVD GGTEGFKGSV RVILPGLSPC VECLLELYPP PVQYQLCTIA
     NTPRSPEHCI EYVKRIAWSE KHPFGDMEID GDNEAHIQWI YNEAVKRAGA FGIHGVTIRL
     TKGVIKNIIP AVSSTNAVIA GRSSAMPLEN YMNFQDGEGI YMGAVLLERD ENCELCSRKP
     ITLTFNENDT LENVCNVLKT DSRFEFTSPS ITYMHGTCRA LYVPSLPGFE NLSRENLTKT
     LKELGLMNGE EIYVSDPSMK STLTFRLSIL TAAQIES
//
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