GenomeNet

Database: UniProt
Entry: W0SCV9_9PROT
LinkDB: W0SCV9_9PROT
Original site: W0SCV9_9PROT 
ID   W0SCV9_9PROT            Unreviewed;       435 AA.
AC   W0SCV9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
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:BAO28861.1};
GN   ORFNames=SUTH_01060 {ECO:0000313|EMBL:BAO28861.1};
OS   Sulfuritalea hydrogenivorans sk43H.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Sulfuritalea.
OX   NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO28861.1, ECO:0000313|Proteomes:UP000031637};
RN   [1] {ECO:0000313|EMBL:BAO28861.1, ECO:0000313|Proteomes:UP000031637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM22779 {ECO:0000313|EMBL:BAO28861.1};
RX   PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA   Watanabe T., Kojima H., Fukui M.;
RT   "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT   skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT   sulfur oxidation pathway of betaproteobacteria.";
RL   Syst. Appl. Microbiol. 37:387-395(2014).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP012547; BAO28861.1; -; Genomic_DNA.
DR   RefSeq; WP_041097617.1; NZ_AP012547.1.
DR   AlphaFoldDB; W0SCV9; -.
DR   STRING; 1223802.SUTH_01060; -.
DR   KEGG; shd:SUTH_01060; -.
DR   HOGENOM; CLU_025113_1_1_4; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000031637; 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};
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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00127};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00127}; Reference proteome {ECO:0000313|Proteomes:UP000031637}.
FT   DOMAIN          1..326
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   435 AA;  48481 MW;  F047BAF809E044CB CRC64;
     MSQTLQAVRG MNDILPVEAE LWEQFEESVR DWLGAYGYRP IRMPMVEPTP LFARAIGEVT
     DIVEKEMYSF EDALNGESLT LRPEGTASCV RAVLQHNLLY DGPKRLWYMG PMFRHERPQK
     GRYRQFHQVG VEALGFSGPD IDAEQIAMCA RLWDDLGLEG IRLEINSLGQ SEERARHRAA
     LLAYLEQHHE QLDADAQRRL HSNPLRILDT KNPAMQALVE AAPKLIDYLG EESIRHFEGV
     QQLLKDAAIP YRINPRLVRG LDYYNLTVFE WVTDQLGAQG TVCAGGRYDG LVAQLGGKPA
     PACGFAMGIE RLLALWQDQG HRHEAPVPDA YFVHQGEAAG RFAFRVAEAL RSAGFSIHLH
     CGGGSFKSQM KKADASGAPI ALIVGDDETA ANQVSVKHLR SGFDQPAEQV RVSFDELADH
     LGDILFPLED DNGNL
//
DBGET integrated database retrieval system