SYH_CAEEL
ID SYH_CAEEL Reviewed; 521 AA.
AC P34183; Q22408; Q26342; Q86DB0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Histidine--tRNA ligase;
DE EC=6.1.1.21;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
GN Name=hars-1 {ECO:0000312|WormBase:T11G6.1b};
GN Synonyms=hrs-1 {ECO:0000312|WormBase:T11G6.1b},
GN syh-1 {ECO:0000303|PubMed:8414990};
GN ORFNames=T11G6.1 {ECO:0000312|WormBase:T11G6.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=8414990; DOI=10.1093/nar/21.18.4344;
RA Amaar Y.G., Baillie D.L.;
RT "Cloning and characterization of the C. elegans histidyl-tRNA synthetase
RT gene.";
RL Nucleic Acids Res. 21:4344-4347(1993).
RN [2]
RP ERRATUM OF PUBMED:8414990.
RX PubMed=8290371;
RA Amaar Y.G., Baillie D.L.;
RL Nucleic Acids Res. 21:6050-6051(1993).
RN [3]
RP SEQUENCE REVISION.
RA Amaar Y.G., Baillie D.L.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21464306; DOI=10.1073/pnas.1103471108;
RA Pierce S.B., Chisholm K.M., Lynch E.D., Lee M.K., Walsh T., Opitz J.M.,
RA Li W., Klevit R.E., King M.C.;
RT "Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian
RT dysgenesis and sensorineural hearing loss of Perrault syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6543-6548(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23076791; DOI=10.1152/ajpcell.00294.2012;
RA Lee E.C., Strange K.;
RT "GCN-2 dependent inhibition of protein synthesis activates osmosensitive
RT gene transcription via WNK and Ste20 kinase signaling.";
RL Am. J. Physiol. 303:C1269-1277(2012).
CC -!- FUNCTION: Involved in protein synthesis (PubMed:23076791). Catalyzes
CC the specific attachment of an amino acid to its cognate tRNA in a 2
CC step reaction: the amino acid (AA) is first activated by ATP to form
CC AA-AMP and then transferred to the acceptor end of the tRNA (Probable).
CC Required for germ cell development (PubMed:21464306).
CC {ECO:0000269|PubMed:21464306, ECO:0000269|PubMed:23076791,
CC ECO:0000305}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:T11G6.1b};
CC IsoId=P34183-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:T11G6.1a};
CC IsoId=P34183-2; Sequence=VSP_011853;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in gonadal
CC defects including smaller, narrower gonads and reduced fertility with
CC either no oocytes or no fertilized eggs in the majority of animals
CC (PubMed:21464306). RNAi-mediated knockdown results in an increase in
CC the expression of gpdh-1 independent of hypertonic stress
CC (PubMed:23076791). {ECO:0000269|PubMed:21464306,
CC ECO:0000269|PubMed:23076791}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB38116.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAB38116.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD14008.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L13152; AAB38116.1; ALT_FRAME; Genomic_DNA.
DR EMBL; S68230; AAD14008.1; ALT_FRAME; mRNA.
DR EMBL; Z69384; CAA93416.2; -; Genomic_DNA.
DR EMBL; Z69384; CAD89746.1; -; Genomic_DNA.
DR PIR; S41763; S41763.
DR PIR; T24848; T24848.
DR RefSeq; NP_001023373.2; NM_001028202.4. [P34183-2]
DR RefSeq; NP_001023374.1; NM_001028203.4. [P34183-1]
DR AlphaFoldDB; P34183; -.
DR SMR; P34183; -.
DR BioGRID; 43079; 2.
DR DIP; DIP-25741N; -.
DR STRING; 6239.T11G6.1a.1; -.
DR EPD; P34183; -.
DR PaxDb; P34183; -.
DR PeptideAtlas; P34183; -.
DR EnsemblMetazoa; T11G6.1a.1; T11G6.1a.1; WBGene00002001. [P34183-2]
DR EnsemblMetazoa; T11G6.1b.1; T11G6.1b.1; WBGene00002001. [P34183-1]
DR GeneID; 177978; -.
DR KEGG; cel:CELE_T11G6.1; -.
DR UCSC; T11G6.1a.1; c. elegans. [P34183-1]
DR CTD; 177978; -.
DR WormBase; T11G6.1a; CE47289; WBGene00002001; hars-1. [P34183-2]
DR WormBase; T11G6.1b; CE33829; WBGene00002001; hars-1. [P34183-1]
DR eggNOG; KOG1936; Eukaryota.
DR GeneTree; ENSGT00390000005922; -.
DR HOGENOM; CLU_025113_4_2_1; -.
DR InParanoid; P34183; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 1065556at2759; -.
DR PhylomeDB; P34183; -.
DR BRENDA; 6.1.1.21; 1045.
DR PRO; PR:P34183; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002001; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; ISS:WormBase.
DR GO; GO:0042802; F:identical protein binding; ISS:WormBase.
DR GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; ISS:WormBase.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0006412; P:translation; IMP:UniProtKB.
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 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 Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..521
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136338"
FT BINDING 137..139
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 164
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 180
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 184
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 338
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 342..343
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT VAR_SEQ 1..33
FT /note="MFRTITSRLAFSVRQAEETVKPRIAYAQRSGRR -> MSSKMTAERKAILMQ
FT EAQALGDEIRQLKLDKADQAI (in isoform a)"
FT /evidence="ECO:0000303|PubMed:8414990"
FT /id="VSP_011853"
FT CONFLICT 218..220
FT /note="LNH -> V (in Ref. 1; AAB38116/AAD14008)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..455
FT /note="IKTE -> TQGLK (in Ref. 1; AAB38116/AAD14008)"
FT /evidence="ECO:0000305"
FT CONFLICT 467..497
FT /note="QFQYAEERRIPLAIVIGEQELKDGVVKLRNV -> SIPVCLRKDRIPSCYCY
FT YESRAKMSVSAKC (in Ref. 1; AAB38116/AAD14008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 58559 MW; A47A14DCD02BA4C7 CRC64;
MFRTITSRLA FSVRQAEETV KPRIAYAQRS GRRIKEKVAL MQAKRKEAGE TGAPEKPGKF
VLKTGKGTRD YGPAQSALRN SVLQTVTETF NRYGAETIDT PVFELRDVLM GKYGEEGGKL
VYDLQDQGGE LLSLRYDLTV PFARYLAMNK ITNITRYQIA KVYRRDQPVM SRGRYREFYQ
CDFDIAGQYD LMLPEAECLG IVDELLTKLE IGEFFINLNH RLILEGMFAV SGIPAKDFKT
ICSSVDKLDK TPWEDVEQEM INEKFLTKEQ TGKLGELVRF RELNSDLNNL ELLEKMSQLP
DLGQNDKFKK GAEELKVLIE YLNVDGVTTV RYEPSLARGL DYYTGAIYEA VAPKALEGTA
VENSEDTAGQ PVGVGSVAAG GRYDGLVKMF DSKANVPCCG VSFGIERLFA IMEARQKVAI
RTTQTEVYVA SAQKNLVRDR KKLVKMLRSA GIKTEMALKA NPKLLTQFQY AEERRIPLAI
VIGEQELKDG VVKLRNVVTR DEQTIKLDQL ITAVRDTLAA L
