ID SYH_PYRFU Reviewed; 432 AA.
AC Q8U431;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 108.
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=PF0264;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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: 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; AE009950; AAL80388.1; -; Genomic_DNA.
DR RefSeq; WP_011011379.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U431; -.
DR SMR; Q8U431; -.
DR STRING; 186497.PF0264; -.
DR PaxDb; 186497-PF0264; -.
DR GeneID; 41712054; -.
DR KEGG; pfu:PF0264; -.
DR PATRIC; fig|186497.12.peg.276; -.
DR eggNOG; arCOG00404; Archaea.
DR HOGENOM; CLU_025113_3_0_2; -.
DR OrthoDB; 8659at2157; -.
DR PhylomeDB; Q8U431; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0000105; P:histidine biosynthetic process; IEA:InterPro.
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; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_00127; His_tRNA_synth; 1.
DR HAMAP; MF_00125; HisZ; 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 InterPro; IPR004517; HisZ.
DR NCBIfam; TIGR00442; hisS; 1.
DR NCBIfam; TIGR00443; hisZ_biosyn_reg; 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 Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..432
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136321"
SQ SEQUENCE 432 AA; 49183 MW; F6C8B00AD0BE150F CRC64;
MIERVKGTRD FLPEEMVKRR WVFERIRERF ETYGFKEVLT PTMEYTKLFE LRSGEEVVKQ
LYAFKDKGGR DVSLRPDMTS SVARLYVNMF QTAPKPIKWY YIANMFRYEE PQSGRYREFW
QAGVELIGSD KVEADAEVIA LFVESYLATG LREFTVNIGD RILLDEFAKM LGVKDDIGLM
RIIDKKDKLP QEDFINALKE FGLDKNGIEK VLELINIKGK PDEVLPLAEE LFTSEVAKNE
INRLYALIDL LEAYEVKDWI RIDLGIARGF DYYTSIVFEA IAPNDLGIGS IGGGGRYDNL
IEVFGGKPTP ATGFAIGIER LIPILEAKGL IPEVQIAPDV YVVPIGERMK KVAIRIATSL
RKSGIKTEIE LMGRKLKKAM DYANKVGVKK TIIVGEKDLE RGVVTVRDME SGEQNEVKID
DIVEFMKNAL KT
//
