SYYM_DROME
ID SYYM_DROME Reviewed; 464 AA.
AC Q9W107; A8E6L8; Q8MZ26; Q95S33;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tyrosine--tRNA ligase, mitochondrial;
DE EC=6.1.1.1 {ECO:0000250|UniProtKB:Q9Y2Z4};
DE AltName: Full=Mitochondrial tyrosyl-tRNA synthetase {ECO:0000312|FlyBase:FBgn0035064};
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
DE Flags: Precursor;
GN Name=TyrRS-m {ECO:0000312|FlyBase:FBgn0035064};
GN Synonyms=Aats-tyr-m {ECO:0000312|FlyBase:FBgn0035064};
GN ORFNames=CG16912 {ECO:0000312|FlyBase:FBgn0035064};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000303|Ref.4};
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr).
CC {ECO:0000250|UniProtKB:Q9Y2Z4}.
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:0000250|UniProtKB:Q9Y2Z4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28523.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM29400.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF47271.1; -; Genomic_DNA.
DR EMBL; AY060975; AAL28523.1; ALT_INIT; mRNA.
DR EMBL; AY113395; AAM29400.1; ALT_FRAME; mRNA.
DR EMBL; BT030810; ABV82192.1; -; mRNA.
DR RefSeq; NP_611967.1; NM_138123.3.
DR AlphaFoldDB; Q9W107; -.
DR SMR; Q9W107; -.
DR BioGRID; 63535; 1.
DR STRING; 7227.FBpp0072334; -.
DR PaxDb; Q9W107; -.
DR PRIDE; Q9W107; -.
DR DNASU; 37965; -.
DR EnsemblMetazoa; FBtr0072429; FBpp0072334; FBgn0035064.
DR GeneID; 37965; -.
DR KEGG; dme:Dmel_CG16912; -.
DR UCSC; CG16912-RA; d. melanogaster.
DR CTD; 37965; -.
DR FlyBase; FBgn0035064; TyrRS-m.
DR VEuPathDB; VectorBase:FBgn0035064; -.
DR eggNOG; KOG2623; Eukaryota.
DR GeneTree; ENSGT00390000013709; -.
DR HOGENOM; CLU_024003_0_3_1; -.
DR InParanoid; Q9W107; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 914272at2759; -.
DR PhylomeDB; Q9W107; -.
DR BioGRID-ORCS; 37965; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 37965; -.
DR PRO; PR:Q9W107; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0035064; Expressed in embryonic/larval hemocyte (Drosophila) and 23 other tissues.
DR Genevisible; Q9W107; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; ISS:FlyBase.
DR GO; GO:0070184; P:mitochondrial tyrosyl-tRNA aminoacylation; ISS:FlyBase.
DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; TAS:FlyBase.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..464
FT /note="Tyrosine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035832"
FT MOTIF 66..75
FT /note="'HIGH' region"
FT MOTIF 270..274
FT /note="'KMSKS' region"
FT BINDING 61
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 105
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 209
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 213
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 216
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 235
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00959"
SQ SEQUENCE 464 AA; 52575 MW; E1FFC8F164148C73 CRC64;
MLPLRRSLLK PLQDVLRHSH RQMSQKNLLE LTDRGFFHGI FPDTAAPRMK QLFTRGQQSI
YAGFDPTADS LHVGNLLVIM GLIHCQRAGH RPIALVGGAT GLIGDPSGRK TERNQLGETV
IETNLKAIEQ QLRRVFENHE NCLWDSKKQK LPLAPLIIVN NADWYADLQL IDFVANMGRH
FRMGSMLSRS SVQSRLESED GMSFTEFTYQ IFQAYDWLHL LRRHNCCFQM GGSDQTGNLM
TGHELISRVE RKREVFGLTL PLVTTEEGDK FGKSAGNAVW LDGNKTSPFA LYQFFLRMPD
SEVEKLLKLF TFIPLPQVEQ LMREHTKEPE KRKAQTLLAE DVTLLVHGES GLKQAERVTN
ALYKGNVEGL AELNLSEIQQ TFQGATMVNL LTEPGMSILE LAMKAKCFPT ETDAVRIINA
GGFYVNQKRV QNIAEVLTTG VHILRNGISL LRVGKRNFYI VRWQ
