ID A0A067JZ42_JATCU Unreviewed; 510 AA.
AC A0A067JZ42;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030619};
GN ORFNames=JCGZ_16551 {ECO:0000313|EMBL:KDP29162.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP29162.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP29162.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP29162.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
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:0000256|ARBA:ARBA00001137};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; KK914761; KDP29162.1; -; Genomic_DNA.
DR RefSeq; XP_012082424.1; XM_012227034.1.
DR AlphaFoldDB; A0A067JZ42; -.
DR STRING; 180498.A0A067JZ42; -.
DR GeneID; 105642263; -.
DR KEGG; jcu:105642263; -.
DR OrthoDB; 5476704at2759; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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 NCBIfam; TIGR00442; hisS; 1.
DR PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138}.
FT DOMAIN 98..419
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 56924 MW; 74CD1E94F38DA030 CRC64;
MPPILSSLHA VHPLISRLYA KPLFLSFTNL SHSSLSLREF SLPRQSFPVK VRTLSSIASA
AQSPSENGSG GGRSGALSAP PPVLEEAVQK IDVNPPKGTR DFPPEEMRLR NWLFHNFREV
SRLYGFEEVD FPVLESEALF IRKAGEEIRD QLYCFEDRGN RRVALRPELT PSLARLVIQK
GKSVPLPLKW FAVGQCWRYE RMTRGRRREH YQWNMDIIGV PEVTAEAELI SSIVTFFKRI
GITASDVGFK VSSRKVLQEV LKCYSISENL FGKVCIIIDK IEKIPIDEIK KELKSVGMSE
EAVEELLQVL SIKSLTKLEE ILGGAGEAVA DLKQLFSLAE NFGYSEWIQF DASVVRGLAY
YTGIVFEGFD REGKLRAICG GGRYDRLLST FGGDDLPACG FGFGDAVIVE LLKEKGLLPE
LSLQVENIVC ALDPDLQGAA STVATILREK GQTVDLVLEN KPLKWVFKRA GRINAQRLIL
VGNTEWQKGM VGVKILSSGE QYEVKLDELE
//
