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Database: UniProt
Entry: A0A095UDI8_9GAMM
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ID   A0A095UDI8_9GAMM        Unreviewed;       424 AA.
AC   A0A095UDI8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:KGD72503.1};
GN   ORFNames=HA49_17505 {ECO:0000313|EMBL:KGD72503.1};
OS   Tatumella morbirosei.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Tatumella.
OX   NCBI_TaxID=642227 {ECO:0000313|EMBL:KGD72503.1, ECO:0000313|Proteomes:UP000029577};
RN   [1] {ECO:0000313|EMBL:KGD72503.1, ECO:0000313|Proteomes:UP000029577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 23360 {ECO:0000313|EMBL:KGD72503.1,
RC   ECO:0000313|Proteomes:UP000029577};
RA   Smits T.H., Palmer M., Venter S.N., Duffy B., Steenkamp E.T., Chan W.Y.,
RA   Coutinho T.A., Coetzee M.P., De Maayer P.;
RT   "The draft genome of the Tatumella morbirosei type strain, LMG23360T
RT   isolated from pineapple rot.";
RL   Submitted (DEC-2014) 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:KGD72503.1}.
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DR   EMBL; JPKR02000003; KGD72503.1; -; Genomic_DNA.
DR   RefSeq; WP_038022751.1; NZ_JPKR02000003.1.
DR   AlphaFoldDB; A0A095UDI8; -.
DR   STRING; 642227.HA49_17505; -.
DR   eggNOG; COG0124; Bacteria.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000029577; 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   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:UP000029577}.
FT   DOMAIN          1..325
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   424 AA;  47489 MW;  64108C13554EFE98 CRC64;
     MAKNIQAIRG MNDYLPADTA LWQRIEQVLK QVLAGYGFSE IRLPIVEQTP LFKRAIGEVT
     DVVEKEMYTF DDRNGDSLTL RPEGTAGCVR AGIEHGLLYN QEQRLWYIGP MFRYERPQKG
     RYRQFHQIGA EVFGLNGPDI DAELIMMTAR WWKALGIAEH VRLELNSIGS LEARANYRDA
     LVAFLEQHKD ALDDDCKRRM YTNPLRVLDS KNQDIQQLLN DAPQLGDYLD PESREHFAGL
     CSLLDDVGIS YTVNQRLVRG LDYYNRTVFE WVTNSLGSQG TVCAGGRYDG LVEQLGGRAT
     PAVGFAMGLE RLVLLVQAVN PEFEPTRKVD VYVIASGAGV QSAAMQLAES LRDAIPEIRL
     MTNFGGGNFK KQFARADKWG ARLALVLGED EVKNNQVVIK DLRSGDQQTV ARNDISGVLL
     SALQ
//
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