SYH_THEAC
ID SYH_THEAC Reviewed; 426 AA.
AC Q9HLX5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=Ta0099;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AL445063; CAC11247.1; -; Genomic_DNA.
DR RefSeq; WP_010900526.1; NC_002578.1.
DR PDB; 1WU7; X-ray; 2.40 A; A/B=1-426.
DR PDBsum; 1WU7; -.
DR AlphaFoldDB; Q9HLX5; -.
DR SMR; Q9HLX5; -.
DR STRING; 273075.Ta0099; -.
DR EnsemblBacteria; CAC11247; CAC11247; CAC11247.
DR GeneID; 1455755; -.
DR KEGG; tac:Ta0099; -.
DR eggNOG; arCOG00404; Archaea.
DR HOGENOM; CLU_025113_3_1_2; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 47919at2157; -.
DR EvolutionaryTrace; Q9HLX5; -.
DR Proteomes; UP000001024; 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 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 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..426
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136328"
FT HELIX 17..36
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:1WU7"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:1WU7"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:1WU7"
FT TURN 265..269
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:1WU7"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:1WU7"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:1WU7"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:1WU7"
FT HELIX 417..423
FT /evidence="ECO:0007829|PDB:1WU7"
SQ SEQUENCE 426 AA; 48229 MW; 45610EC7EE055B96 CRC64;
MYRLQIEKIR GFRDFYPEDM DVEKFIFKTA EEAAEAFGFR RIDFPSLEYL DLYRIKSGEE
LLQQTYSFVD KGGREVTLIP EATPSTVRMV TSRKDLQRPL RWYSFPKVWR YEEPQAGRYR
EHYQFNADIF GSDSPEADAE VIALASSILD RLGLQDIYEI RINSRKIMEE IIGGMTSSDP
FSVFSIIDRY HKISREEFVD QLRSAGIGED GVSMIADLCS GTRGIDEMAR ITGKSSEEIA
RMAAVEDLLA SYGVKNVRYD FSIVRGLSYY TGIVFEAYDR SGQFRAILGG GRYDNLASLM
SGESVPAVGF GMGDAVISLL LKRENVQIPR EKKSVYICRV GKINSSIMNE YSRKLRERGM
NVTVEIMERG LSAQLKYASA IGADFAVIFG ERDLERGVVT IRNMYTGSQE NVGLDSVVEH
LISQAT
