SYH_THET8
ID SYH_THET8 Reviewed; 421 AA.
AC P56194; Q5SKD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Histidine--tRNA ligase;
DE EC=6.1.1.21;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
GN Name=hisS; OrderedLocusNames=TTHA0712;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.7
RP ANGSTROMS).
RX PubMed=9115984; DOI=10.1021/bi9618373;
RA Aaberg A., Yaremchuk A., Tukalo M., Rasmussen B., Cusack S.;
RT "Crystal structure analysis of the activation of histidine by Thermus
RT thermophilus histidyl-tRNA synthetase.";
RL Biochemistry 36:3084-3094(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD70535.1; -; Genomic_DNA.
DR RefSeq; WP_011172810.1; NC_006461.1.
DR RefSeq; YP_143978.1; NC_006461.1.
DR PDB; 1ADJ; X-ray; 2.70 A; A/B/C/D=1-421.
DR PDB; 1ADY; X-ray; 2.80 A; A/B/C/D=1-421.
DR PDBsum; 1ADJ; -.
DR PDBsum; 1ADY; -.
DR AlphaFoldDB; P56194; -.
DR SMR; P56194; -.
DR STRING; 300852.55772094; -.
DR DrugBank; DB04201; Histidyl-Adenosine Monophosphate.
DR EnsemblBacteria; BAD70535; BAD70535; BAD70535.
DR GeneID; 3168691; -.
DR KEGG; ttj:TTHA0712; -.
DR PATRIC; fig|300852.9.peg.706; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_0; -.
DR OMA; CDFDFIG; -.
DR PhylomeDB; P56194; -.
DR BRENDA; 6.1.1.21; 2305.
DR EvolutionaryTrace; P56194; -.
DR Proteomes; UP000000532; 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: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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..421
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136284"
FT REGION 1..171
FT /note="Catalytic"
FT REGION 229..320
FT /note="Catalytic"
FT CONFLICT 200
FT /note="L -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 14..33
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 98..111
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 137..153
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 231..246
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 338..351
FT /evidence="ECO:0007829|PDB:1ADJ"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:1ADJ"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:1ADJ"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:1ADJ"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:1ADJ"
SQ SEQUENCE 421 AA; 47041 MW; 9DEEE25F2C570A27 CRC64;
MTARAVRGTK DLFGKELRMH QRIVATARKV LEAAGALELV TPIFEETQVF EKGVGAATDI
VRKEMFTFQD RGGRSLTLRP EGTAAMVRAY LEHGMKVWPQ PVRLWMAGPM FRAERPQKGR
YRQFHQVNYE ALGSENPILD AEAVVLLYEC LKELGLRRLK VKLSSVGDPE DRARYNAYLR
EVLSPHREAL SEDSKERLEL NPMRILDSKS ERDQALLKEL GVRPMLDFLG EEARAHLKEV
ERHLERLSVP YELEPALVRG LDYYVRTAFE VHHEEIGAQS ALGGGGRYDG LSELLGGPRV
PGVGFAFGVE RVALALEAEG FGLPEEKGPD LYLIPLTEEA VAEAFYLAEA LRPRLRAEYA
LAPRKPAKGL EEALKRGAAF AGFLGEDELR AGEVTLKRLA TGEQVRLSRE EVPGYLLQAL
G
