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Database: UniProt
Entry: A0A1H8IW14_9MICO
LinkDB: A0A1H8IW14_9MICO
Original site: A0A1H8IW14_9MICO 
ID   A0A1H8IW14_9MICO        Unreviewed;       422 AA.
AC   A0A1H8IW14;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE            EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030619};
GN   ORFNames=E3O10_07105 {ECO:0000313|EMBL:TFB91164.1};
OS   Cryobacterium luteum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1424661 {ECO:0000313|EMBL:TFB91164.1, ECO:0000313|Proteomes:UP000297654};
RN   [1] {ECO:0000313|EMBL:TFB91164.1, ECO:0000313|Proteomes:UP000297654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh15 {ECO:0000313|EMBL:TFB91164.1,
RC   ECO:0000313|Proteomes:UP000297654};
RA   Liu Q., Xin Y.-H.;
RT   "Genomics of glacier-inhabiting Cryobacterium strains.";
RL   Submitted (MAR-2019) 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:TFB91164.1}.
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DR   EMBL; SOFF01000026; TFB91164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8IW14; -.
DR   STRING; 1424661.SAMN05216281_11282; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000297654; 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:InterPro.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 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   Ligase {ECO:0000313|EMBL:TFB91164.1}.
FT   DOMAIN          29..361
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   422 AA;  45057 MW;  651A86DDA2E0695C CRC64;
     MAIAVTPPRG MRDFLPADKA VRERSLGIIR ESFRAHGFDE IETPVMEDSI RLHSGLGGDN
     EKLAFAVLKR GLSAADVAAA AAQDDLLSLA DLGLRFDLTV PLARFYATHR AALPTVFRSI
     QIAPVWRAER PQKGRYRQFM QCDIDIIGEA GSLAEIELIT ATAATLDQLG LTGCSIRIND
     RRILTTLLAH WGVAAALTER ALIVIDKLDK IGVNGVATEL GTLGIDAPDL ATLLTELGSG
     GWSLGSDAPD GSAPSWLDPA AFADLEALRA ALPGVDLRFD PTLVRGMGYY TGTIFEIAHP
     DLSYSLGGGG RYDGMIGRFL GTDVPACGFS IGFERIVDLL EADAASALNA VVLVHEKDAD
     PARLVALKRD LVAGGLRVRL ERRTKNLKAL LDRAGEAGYG RFAFVTPDTN AAADLDFKPL
     GV
//
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