ID   SYH_PORPU               Reviewed;         430 AA.
AC   P51348;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Histidine--tRNA ligase, chloroplastic;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hisS; Synonyms=syh;
OS   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U38804; AAC08234.1; -; Genomic_DNA.
DR   PIR; S73269; S73269.
DR   RefSeq; NP_053958.1; NC_000925.1.
DR   AlphaFoldDB; P51348; -.
DR   SMR; P51348; -.
DR   GeneID; 809984; -.
DR   BRENDA; 6.1.1.21; 7220.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR43707; PTHR43707; 1.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase;
KW   Nucleotide-binding; Plastid; Protein biosynthesis.
FT   CHAIN           1..430
FT                   /note="Histidine--tRNA ligase, chloroplastic"
FT                   /id="PRO_0000136331"
SQ   SEQUENCE   430 AA;  49772 MW;  2349E5B4BF1D804F CRC64;
     MAKIQAIRGT KDILPDEQLY WQFIHEKVAS LLKYANYKEI KTPIFENSDL YDRGIGENTD
     IVNKEMYRFN DRSNRDITLR PEGTAGVVRA FIENRMDVQN RLQKLWYSGP MFRYERPQSG
     RQRQFHQLGI EFIGSSDARA DAEIIHLAMN IFNDLSVNDL QLDINSIGKA EDRNHYQAKL
     QEYLEQYYDD LDTDSQNRLS SNPIRILDTK NKYTQTILND SPRISDFLSL ESEKHFDDVC
     DYLTLLNVPY KINTQLVRGL DYYNDTAFEI KILKSQGQDT LCGGGRYDSL IHQLGGNKTP
     AVGCAIGLER LLLVAKDNIL LPHMSIDCYI VSKGIKARKI GIIITQFLRN QLVKTELDIS
     SSNFGKQLKQ AHKKRAIACL ILGDNEIQQE TITIKWMYTQ EQENMSIIEF KNKISYLKKK
     IAFNKKFNSY