UniProt: A0A0Q6XZ47

Database: UniProt
Entry: A0A0Q6XZ47_9BURK

LinkDB:  A0A0Q6XZ47_9BURK 
Original site:  A0A0Q6XZ47_9BURK

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
All databases (17)   

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ID   A0A0Q6XZ47_9BURK        Unreviewed;       440 AA.
AC   A0A0Q6XZ47;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   ORFNames=ASC87_13170 {ECO:0000313|EMBL:KQW02649.1};
OS   Rhizobacter sp. Root1221.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQW02649.1, ECO:0000313|Proteomes:UP000051465};
RN   [1] {ECO:0000313|EMBL:KQW02649.1, ECO:0000313|Proteomes:UP000051465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1221 {ECO:0000313|EMBL:KQW02649.1,
RC   ECO:0000313|Proteomes:UP000051465};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW02649.1, ECO:0000313|Proteomes:UP000051465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1221 {ECO:0000313|EMBL:KQW02649.1,
RC   ECO:0000313|Proteomes:UP000051465};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KQW02649.1}.
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DR   EMBL; LMDI01000002; KQW02649.1; -; Genomic_DNA.
DR   RefSeq; WP_056656342.1; NZ_LMDI01000002.1.
DR   AlphaFoldDB; A0A0Q6XZ47; -.
DR   STRING; 1736433.ASC87_13170; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000051465; Unassembled WGS sequence.
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   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   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   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:UP000051465}.
FT   DOMAIN          36..364
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   440 AA;  49472 MW;  01F53D544ED4A52F CRC64;
     MSKPTSPAPY KPEPITGYTE WLPEARLVEQ QWMDHIRKVF ESYGFCNIET PAVEEIEVLS
     AKGGDTEKEI YALRRLYDSP QDAEPRVALH YDLTVPMARY VAQHYNDLVF PFKRYQMQKV
     WRGERPQEGR FREFLQCDID VIDNEDVSKS FDAELPIIVY EVLQGLGVGP FSINVNNRKI
     LQGFYQGLGI EKITEAIRIA DKFDKIGADG VRKSLVDQLQ LPEDVAAKCV ALAQIRTSDL
     GFVEQVRALG VQSELLDEGI EELRFVIDHM KDIPAGRIWA DLSIARGLDY YTGTVYEGKL
     LDYPGYPSVC SGGRYENLVG SYLRKKLPGV GMSIGLTRIF AKLLKDGKLP VGPKSTTQLL
     VAFPQGANRD DVRRVAAHFR SRGVRVEAYH EDKKTPKQLQ YASRKGIPYV LFPGADGAPH
     QVKTMATGEQ AEVPADWLPG
//

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