SYH_THET2
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 25-MAY-2022, entry version 102.
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=TT_C0360;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; 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=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; 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 PDBsum; 1H4V; -.
DR PDBsum; 4RDX; -.
DR AlphaFoldDB; P62374; -.
DR SMR; P62374; -.
DR STRING; 262724.TT_C0360; -.
DR EnsemblBacteria; AAS80708; AAS80708; TT_C0360.
DR GeneID; 3168691; -.
DR KEGG; tth:TT_C0360; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_0; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
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; 3.30.930.10; -; 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.
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 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 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
