HARS1_DANRE
ID HARS1_DANRE Reviewed; 513 AA.
AC E9QI36; F1Q5D5;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Histidine--tRNA ligase;
DE EC=6.1.1.21 {ECO:0000250|UniProtKB:P12081};
GN Name=hars {ECO:0000312|ZFIN:ZDB-GENE-040912-152};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RX PubMed=28934368; DOI=10.1371/journal.pone.0185317;
RA Waldron A.L., Cahan S.H., Francklyn C.S., Ebert A.M.;
RT "A single Danio rerio hars gene encodes both cytoplasmic and mitochondrial
RT histidyl-tRNA synthetases.";
RL PLoS ONE 12:E0185317-E0185317(2017).
CC -!- FUNCTION: Catalyzes the aminoacylation of histidyl-tRNA.
CC {ECO:0000250|UniProtKB:P12081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC Evidence={ECO:0000250|UniProtKB:P12081};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:28934368}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion
CC {ECO:0000269|PubMed:28934368}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Hars-002 {ECO:0000303|PubMed:28934368};
CC IsoId=E9QI36-1; Sequence=Displayed;
CC Name=2; Synonyms=Hars-001 {ECO:0000303|PubMed:28934368};
CC IsoId=E9QI36-2; Sequence=VSP_060465;
CC -!- MISCELLANEOUS: Danio rerio genome encodes a single hars gene which
CC undergoes alternative splicing to produce both a cytoplasmic and
CC mitochondrial enzyme, while humans have two separate genes.
CC {ECO:0000303|PubMed:28934368}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BX890575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001289185.1; NM_001302256.1. [E9QI36-2]
DR RefSeq; NP_001289191.1; NM_001302262.1. [E9QI36-1]
DR AlphaFoldDB; E9QI36; -.
DR SMR; E9QI36; -.
DR STRING; 7955.ENSDARP00000123163; -.
DR PeptideAtlas; E9QI36; -.
DR Ensembl; ENSDART00000141471; ENSDARP00000123163; ENSDARG00000003693. [E9QI36-2]
DR Ensembl; ENSDART00000142158; ENSDARP00000113894; ENSDARG00000003693. [E9QI36-1]
DR GeneID; 447847; -.
DR KEGG; dre:447847; -.
DR CTD; 15115; -.
DR ZFIN; ZDB-GENE-040912-152; hars.
DR eggNOG; KOG1936; Eukaryota.
DR GeneTree; ENSGT00390000005922; -.
DR HOGENOM; CLU_025113_4_2_1; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 1065556at2759; -.
DR TreeFam; TF300652; -.
DR PRO; PR:E9QI36; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000003693; Expressed in somite and 35 other tissues.
DR ExpressionAtlas; E9QI36; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:1901342; P:regulation of vasculature development; IMP:ZFIN.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:ZFIN.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00127; His_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR033656; HisRS_anticodon.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..513
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000448899"
FT DOMAIN 3..59
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT BINDING 130..132
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 157
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 173
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 177
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 326
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 330..331
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT VAR_SEQ 3..29
FT /note="DKAQLQEAIKTQGEVVRKLKSEKASKE -> ALGLVSMRLCAGLMGRRSAVR
FT LHSLRVCSGMTIS (in isoform 2)"
FT /id="VSP_060465"
FT TRANSIT E9QI36-2:1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
SQ SEQUENCE 513 AA; 57585 MW; E2EC31D3AC53C113 CRC64;
MADKAQLQEA IKTQGEVVRK LKSEKASKEQ IDEEVARLLQ LKAQLGGDEG KHVFVLKTAK
GTRDYNPKQM AIREKVFNII INCFKRHGAE TIDSPVFELK ETLTGKYGED SKLIYDLKDQ
GGELLSLRYD LTVPFARYLA MNKITNIKRY HIAKVYRRDN PAMTRGRYRE FYQCDFDIAG
QYDAMIPDAE CLKLVYEILS ELDLGDFRIK VNDRRILDGM FAICGVPDEK FRTICSTVDK
LDKLAWEEVK KEMVNEKGLS EEVADRIRDY VSMQGGKDLA ERLLQDPKLS QSKQACAGIT
DMKLLFSYLE LFQITDKVVF DLSLARGLDY YTGVIYEAIL TQANPAPAST PAEQNGAEDA
GVSVGSVAGG GRYDGLVGMF DPKGRKVPCV GVSIGIERVF SIMEQKAELS SEKVRTTETQ
VLVASAQKNL LEERLKLTAE LWNAGIKAEV LYKKNPKLLS QLQHCEDTGI PLVAILGEQE
LKDGVVKLRN VASREEVDVP RAELVDEVKK RTS
