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SYH_THEM4
ID   SYH_THEM4               Reviewed;         419 AA.
AC   A6LL06;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=Tmel_0744;
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=391009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermosipho melanesiensis BI429.";
RL   Submitted (MAY-2007) 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         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; CP000716; ABR30607.1; -; Genomic_DNA.
DR   RefSeq; WP_012056968.1; NC_009616.1.
DR   AlphaFoldDB; A6LL06; -.
DR   SMR; A6LL06; -.
DR   STRING; 391009.Tmel_0744; -.
DR   EnsemblBacteria; ABR30607; ABR30607; Tmel_0744.
DR   KEGG; tme:Tmel_0744; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_1_1_0; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000001110; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..419
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_1000016477"
SQ   SEQUENCE   419 AA;  48182 MW;  0400DB74BFD1771F CRC64;
     MYKKIKGTDD IYGEDMKYWY FIENTAREIT RLYGYSEIRT PIFEQTELFV RSVGEETDIV
     QKEMYTFKDK GDRSITLRPE GTAPTIRAFI ENSMVATGLP KRLFYIGPMF RYERPQAGRQ
     RQFHQFGIEL IGSSSSLADA EAIVVADRFL KSLGLVDYTI KINSIGCEKC RAEYKKKLKE
     YYSDKLDKVC DDCKRRYNTN ILRLLDCKVD VEYVKDAPKI TDYLCDNCKK HYEETKNILD
     KLDINYEEDP LLVRGLDYYN GIVFEIHHGK LGAQSAIGGG GRYDNLIKEL GGQQTPSLGF
     AMGIERLIIA VKKEGIPVEE IKNNEVFVAH LGESARIEAI KISEELRDNG ISVVFNTMER
     GLSAQLKHAS RLNCRLCLIV GENELERNVV ILRNMKTGEQ IEIERDYIVG TTREWIDEQ
 
 
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