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Database: UniProt
Entry: E8N5T4_ANATU
LinkDB: E8N5T4_ANATU
Original site: E8N5T4_ANATU 
ID   E8N5T4_ANATU            Unreviewed;       426 AA.
AC   E8N5T4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Histidine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00127};
DE            EC=6.1.1.21 {ECO:0000256|HAMAP-Rule:MF_00127};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127};
DE            Short=HisRS {ECO:0000256|HAMAP-Rule:MF_00127};
GN   Name=hisS {ECO:0000256|HAMAP-Rule:MF_00127,
GN   ECO:0000313|EMBL:BAJ63798.1};
GN   OrderedLocusNames=ANT_17720 {ECO:0000313|EMBL:BAJ63798.1};
OS   Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS   UNI-1).
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Anaerolinea.
OX   NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63798.1, ECO:0000313|Proteomes:UP000008922};
RN   [1] {ECO:0000313|EMBL:BAJ63798.1, ECO:0000313|Proteomes:UP000008922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC   {ECO:0000313|Proteomes:UP000008922};
RA   Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA   Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA   Fujita N.;
RT   "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL   Submitted (DEC-2010) 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:0000256|ARBA:ARBA00001137, ECO:0000256|HAMAP-
CC         Rule:MF_00127};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_00127}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00127}.
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DR   EMBL; AP012029; BAJ63798.1; -; Genomic_DNA.
DR   RefSeq; WP_013560176.1; NC_014960.1.
DR   AlphaFoldDB; E8N5T4; -.
DR   SMR; E8N5T4; -.
DR   STRING; 926569.ANT_17720; -.
DR   GeneID; 78350151; -.
DR   KEGG; atm:ANT_17720; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_1_0; -.
DR   InParanoid; E8N5T4; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000008922; 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; 3.40.50.800; Anticodon-binding domain; 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   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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00127};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00127}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00127};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00127}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008922}.
FT   DOMAIN          1..209
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   426 AA;  48723 MW;  693F5492B36C1C34 CRC64;
     MKAIVPSVKG TRDFYPEIMA VRNWLYARIR EVSEKFGYQE YEGPFLERVD LYAAKSGEEL
     VNEQSFVFQD RGGDYIALRP ELTPTLARMV AQRQNELVYP LRWWSFGPFW RYERPQKGRT
     REFFQWNIDI IGSQAIEADA ELLAVAVEFF KSVGLTSQQV KLLVNNRRLM DVQLENLGIR
     EGQKRDVFRL IDRKEKLPLP EWRQYAFDFG LTQEQLSGLE SLLVNESLWE TSDELKRVFE
     LLEGMGIREY VEFAPQIIRG LDYYTGTVFE AKDLDGGRSI LGGGHYDNLV ANVGGEPLPG
     VGFAMGDVMI TLVLEKYGKL PALETAPAQV LVTVFDLERL PQSFALAARL REQGLKVVWY
     PEAAKLQKQL KFADRAGIRF AVIYGPDEIS AGQVALKDLH QRNQELVSVE NVGERVRQIL
     AQSERV
//
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