ID SYH_THET2 Reviewed; 421 AA. AC P62374; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 10-JUN-2026, entry version 113. 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}; GN OrderedLocusNames=TT_C0360; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(His) + L-histidine + ATP = L-histidyl-tRNA(His) + AMP + CC diphosphate + H(+); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017221; AAS80708.1; -; Genomic_DNA. DR RefSeq; WP_011172810.1; NC_005835.1. DR PDB; 1H4V; X-ray; 2.40 A; B=1-421. DR PDB; 4RDX; X-ray; 2.55 A; A=1-421. DR AlphaFoldDB; P62374; -. DR SMR; P62374; -. DR GeneID; 3168691; -. DR KEGG; tth:TT_C0360; -. DR eggNOG; COG0124; Bacteria. DR HOGENOM; CLU_025113_1_1_0; -. DR OrthoDB; 9800814at2; -. DR BRENDA; 6.1.1.21; 2305. DR EvolutionaryTrace; P62374; -. DR Proteomes; UP000000592; 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; 3.40.50.800; Anticodon-binding domain; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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 NCBIfam; TIGR00442; hisS; 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. DR PDBsum; 1H4V; -. DR PDBsum; 4RDX; -. 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_0000136283" FT HELIX 14..33 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 47..50 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 83..92 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 98..111 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 123..133 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 137..153 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 169..183 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 184..189 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 192..200 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 202..207 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 211..220 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 231..246 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 265..272 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 281..287 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 302..308 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 309..318 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 324..329 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 330..337 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 338..351 FT /evidence="ECO:0007829|PDB:1H4V" FT TURN 352..354 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 366..375 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 379..384 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 386..391 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 393..398 FT /evidence="ECO:0007829|PDB:1H4V" FT TURN 399..401 FT /evidence="ECO:0007829|PDB:1H4V" FT STRAND 404..408 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 409..411 FT /evidence="ECO:0007829|PDB:1H4V" FT HELIX 412..419 FT /evidence="ECO:0007829|PDB:1H4V" 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 //