SYH_PICTO
ID SYH_PICTO Reviewed; 423 AA.
AC Q6L1Q5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=PTO0512;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(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 -!- 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; AE017261; AAT43097.1; -; Genomic_DNA.
DR RefSeq; WP_011177313.1; NC_005877.1.
DR AlphaFoldDB; Q6L1Q5; -.
DR SMR; Q6L1Q5; -.
DR STRING; 263820.PTO0512; -.
DR EnsemblBacteria; AAT43097; AAT43097; PTO0512.
DR GeneID; 2843919; -.
DR KEGG; pto:PTO0512; -.
DR PATRIC; fig|263820.9.peg.539; -.
DR eggNOG; arCOG00404; Archaea.
DR HOGENOM; CLU_025113_3_1_2; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 47919at2157; -.
DR Proteomes; UP000000438; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..423
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136318"
SQ SEQUENCE 423 AA; 48853 MW; 5DDE971EAEC4DD63 CRC64;
MKIERLKGFR DHYPDDMEIR YDFIKKMMDT AISFGYKMID FPSLESMDLY RLKSGTELVE
QTFSFTDKGG REVTMIPEAT PSTMRMLTSR KDIKMPARWF SIPKVWRYEE PQEGRYREHI
QFNADMFGAD SPEADAEIIG LAATILDNLG LSGQYEINVN DRYLMELILR DLGSNNPVDL
FPVIDRFKKM DLTDFKKRLL KDLDDDASEK LISLLMNRID INDVERLLNG YANDVMERVK
RLKDTFALTS KYTKSKLNID LSVVRGLSYY TGIVFEAFDI SGELRAILGG GRYDNLSNLF
INESIPAVGF AIGDAVIELL LKRNNLWNYK DKRKRYYVVN ISSSPEAHIE ILNKIRGSGN
IAISEVNKRR MQTIIKYAES IKCDFLIIIG DRELSSKKMT IKNLRTQEQA EMNIDDFINN
INS