SYH_GRATL
ID SYH_GRATL Reviewed; 420 AA.
AC Q6B910;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Histidine--tRNA ligase, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=Grc000044;
OS Gracilaria tenuistipitata var. liui (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX NCBI_TaxID=285951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT "Comparative analysis of the complete plastid genome sequence of the red
RT alga Gracilaria tenuistipitata var. liui provides insights into the
RT evolution of rhodoplasts and their relationship to other plastids.";
RL J. Mol. Evol. 59:464-477(2004).
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:0000255|HAMAP-Rule:MF_00127};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR EMBL; AY673996; AAT79625.1; -; Genomic_DNA.
DR RefSeq; YP_063550.1; NC_006137.1.
DR AlphaFoldDB; Q6B910; -.
DR SMR; Q6B910; -.
DR GeneID; 2944168; -.
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 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 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..420
FT /note="Histidine--tRNA ligase, chloroplastic"
FT /id="PRO_0000136330"
SQ SEQUENCE 420 AA; 48859 MW; 42E419C7243E4D14 CRC64;
MKSYFMQPLR GTKDILPNEI NYWHHIHDKA LTILSLHNYS EIRTPIIEST SLFKRSIGET
SDIINKEMYT FTDQGDRSIT LRPEATASIA RAFISNKLYH SNIQRLWYLG PMFRYERPQS
GRQRQFHQLG IECIGSINPM ADTEVIHLAN QLLKELQVKN YILEINSIGT LEERQSYKLD
LVEYLSQYQQ DLDQDSKNRM YSNPLRILDS KNLKTQEILD GAPKLKKYLN KRSTEHFYLV
CTYLNNLNIT YKINYKLVRG LDYYNQTAFE IKTNSKNSQN TICGGGRYDT LIEQLGGPKT
PAVGWAIGIE RLLKIIEDKL ILPKQKINVY IATQGLAAQK KIWEIIQALE KKNIKFELDL
SNTSFHKQIK KAGKLGAKFC IILGDQEIMD NCVTIKRLDE YVQYTAQYSN FLQEIHKLQH