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Database: UniProt
Entry: A0A1B3LJF0_9PROT
LinkDB: A0A1B3LJF0_9PROT
Original site: A0A1B3LJF0_9PROT 
ID   A0A1B3LJF0_9PROT        Unreviewed;       433 AA.
AC   A0A1B3LJF0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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:AOF80981.1};
GN   ORFNames=BSY238_41 {ECO:0000313|EMBL:AOF80981.1};
OS   Methyloversatilis sp. RAC08.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Methyloversatilis.
OX   NCBI_TaxID=1842540 {ECO:0000313|EMBL:AOF80981.1, ECO:0000313|Proteomes:UP000094168};
RN   [1] {ECO:0000313|Proteomes:UP000094168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC08 {ECO:0000313|Proteomes:UP000094168};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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; CP016448; AOF80981.1; -; Genomic_DNA.
DR   RefSeq; WP_069037370.1; NZ_CP016448.1.
DR   AlphaFoldDB; A0A1B3LJF0; -.
DR   STRING; 1842540.BSY238_41; -.
DR   KEGG; metr:BSY238_41; -.
DR   PATRIC; fig|1842540.3.peg.40; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000094168; 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|HAMAP-Rule:MF_00127};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00127};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00127};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00127}; Reference proteome {ECO:0000313|Proteomes:UP000094168}.
FT   DOMAIN          1..327
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   433 AA;  48334 MW;  C02F60E7C727A731 CRC64;
     MSKLQAVRGM NDILPDEAER WEAFETIVRD WLRAYGYRPI RMPLLEHTPL FKRAIGEVTD
     IVEKEMYSFE DALNGENLTL RPEGTASCVR AVTEHNLLYD SPRKLWYMGP MFRHERPQKG
     RYRQFHQVGV EALGYAGPDV DAELIMMCQR LWDDLDLMGI RLEINSLGSP EERMQHRAAL
     IAYFEAHQEQ LDDDAKRRLH SNPLRILDTK NPAMQALVEA APKLSDYLGK ESIAHFTAIQ
     DTLRAANIPF RINPRLVRGL DYYNLTVFEW VTDQLGAQGT ICAGGRYDGL VSQLGGKPAP
     AAGFAMGVER LLSLWNPVQA DALIERPEAY VVHSGQGVQA EAFALAEQLR DAGFATLMHC
     GGGSFKSQMK RADASGAAVA LILGEDEVAS GDVTFKPLRG GDQMRISRDD VAEHLAMLLL
     GGDDTDEDEP LLH
//
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