SYH_GLOVI
ID SYH_GLOVI Reviewed; 467 AA.
AC Q7NHH9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Histidine--tRNA ligase {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=gll2557;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR EMBL; BA000045; BAC90498.1; -; Genomic_DNA.
DR RefSeq; NP_925503.1; NC_005125.1.
DR RefSeq; WP_011142552.1; NC_005125.1.
DR AlphaFoldDB; Q7NHH9; -.
DR SMR; Q7NHH9; -.
DR STRING; 251221.35213126; -.
DR EnsemblBacteria; BAC90498; BAC90498; BAC90498.
DR KEGG; gvi:gll2557; -.
DR PATRIC; fig|251221.4.peg.2595; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_0_3; -.
DR InParanoid; Q7NHH9; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 277998at2; -.
DR PhylomeDB; Q7NHH9; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
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 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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..467
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136168"
SQ SEQUENCE 467 AA; 51137 MW; EA8B93C9F213C0F1 CRC64;
MGELGTMGGT RDFLPDEMIR REYVIDTLKT IFRKYGFEPL ETPAIERWET LAGKYGEEGE
KLIYHVVSSG SLGTLKAGER TEHALRYDLT VPLARVVGMY GDQMVADPAD PKKQTRRLPR
PFKRYQIQPV WRGDRPGEGR YREFHQCDAD VVGSTSPLVE TELIALTVEA FKALGFADFT
VKINHRQLLK GLIEQAGIAP TKEATVLTSI DKLDKLPPEK VRLELAGKGL NADQLDALFQ
VIALEGTSEQ VLEGARSLLA GSEAAQRGIG ELTKLLHYLE ALGVDSAYYR IDLALARGLD
YYTGTIFETV SAAKVGSVGA GGRYDRLIYD LSGGKADLPA CGTSFGLDRI LAAMDQLGLF
ASLRRAGEVL VLHFGDPGVS QVCFELVRGL REAGVRAELG YHEEPFTPNG MRQQLGYANE
KGFAYAVIVG PDEMAQGQAA LRDLTTRRQE KIPLATAGQL IAGRLRS