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Database: UniProt
Entry: A0A0A0JYR5_9MICO
LinkDB: A0A0A0JYR5_9MICO
Original site: A0A0A0JYR5_9MICO 
ID   A0A0A0JYR5_9MICO        Unreviewed;       451 AA.
AC   A0A0A0JYR5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00017399};
DE            EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030619};
GN   ORFNames=N801_02155 {ECO:0000313|EMBL:KGN41227.1};
OS   Knoellia aerolata DSM 18566.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1385519 {ECO:0000313|EMBL:KGN41227.1, ECO:0000313|Proteomes:UP000030013};
RN   [1] {ECO:0000313|EMBL:KGN41227.1, ECO:0000313|Proteomes:UP000030013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18566 {ECO:0000313|EMBL:KGN41227.1,
RC   ECO:0000313|Proteomes:UP000030013};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Knoellia aerolata.";
RL   Submitted (AUG-2013) 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};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGN41227.1}.
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DR   EMBL; AVPL01000021; KGN41227.1; -; Genomic_DNA.
DR   RefSeq; WP_035936866.1; NZ_AVPL01000021.1.
DR   AlphaFoldDB; A0A0A0JYR5; -.
DR   STRING; 1385519.N801_02155; -.
DR   eggNOG; COG0124; Bacteria.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000030013; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 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; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11476; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030013}.
FT   DOMAIN          19..348
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          404..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   451 AA;  48911 MW;  B4EFB51DDF431FF4 CRC64;
     MKVTKLSGFP EYLPAERIVE QHFLDVIRET FELHGFTSLE TRAVEPVERL LGKGGDADKE
     IYGVTRLADE GGQASSRDVA LGLHFDLTVP FARFVLENAG RLTFPYRRYQ IQKVWRGERP
     QEGRYREFTQ ADIDVVDVGE LSAHFEAEMP LVVAEVFAKL PIGRMTIQVN NRKIPEGFYK
     GIGIEDVAGT LRIVDKLDKV GPDKVAAQLR EAGRTDEQAA QCLALAAIRT EDLSFVDRVR
     ALGVEHPTLD EGLDALAAVI RTGLENAPGA MVADLKIARG LDYYTGTVYE TQLEGHESWG
     SFCSGGRYDA LASDGRTTYP GVGISIGVSR LLGLLLSQGL VTASRATPAA VLVAVVEEDS
     RRASDAVARA LRARGIPCEV APTAAKFGKQ IRYADRRGIP FVWFPGDGTG PGPGDQVKDI
     RSGDQVDADP QTWSPPAEDL RPSVGAPAPS P
//
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