UniProt: A0A1H7L7D3

Database: UniProt
Entry: A0A1H7L7D3_9BACT

LinkDB:  A0A1H7L7D3_9BACT 
Original site:  A0A1H7L7D3_9BACT

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
All databases (17)   

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ID   A0A1H7L7D3_9BACT        Unreviewed;       478 AA.
AC   A0A1H7L7D3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Asparagine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00534};
DE            EC=6.1.1.22 {ECO:0000256|HAMAP-Rule:MF_00534};
DE   AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00534};
DE            Short=AsnRS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   Name=asnS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   ORFNames=SAMN04488505_1011194 {ECO:0000313|EMBL:SEK94922.1};
OS   Chitinophaga rupis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=573321 {ECO:0000313|EMBL:SEK94922.1, ECO:0000313|Proteomes:UP000198984};
RN   [1] {ECO:0000313|EMBL:SEK94922.1, ECO:0000313|Proteomes:UP000198984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21039 {ECO:0000313|EMBL:SEK94922.1,
RC   ECO:0000313|Proteomes:UP000198984};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC         asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC         Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00534};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00534}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00534}.
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DR   EMBL; FOBB01000001; SEK94922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7L7D3; -.
DR   STRING; 573321.SAMN04488505_1011194; -.
DR   Proteomes; UP000198984; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00776; AsxRS_core; 1.
DR   CDD; cd04318; EcAsnRS_like_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00457; asnS; 1.
DR   PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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_00534};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00534}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00534};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00534};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00534};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00534}; Reference proteome {ECO:0000313|Proteomes:UP000198984}.
FT   DOMAIN          132..468
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          272..299
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   478 AA;  54714 MW;  FB9A5CC110EDDD71 CRC64;
     MSQRVKVKQI LSDDKVQYDV TVKGWIRSFR NNQFIALNDG STNNNLQIVI EPGTDAGLLK
     RLTTGAAISV TGEIIASLGK GQKVELKARE LEVLGDCDPE KYPLQLKNRP SLEYLREIAH
     LRFRTNTFGA IFRVRHSLAF AVHQFFNERG FVYLHTPVIT ASDAEGAGEM FRVTTLDLNK
     PPRTESGDID FKEDFFGRAT NLTVSGQLEG ELGAMAFGDI YTFGPTFRAE NSNTARHLAE
     FWMIEPEMAF YDLEDNMNLA EAFIKYVIGY VLQHNREDLE FLAQRLAEEE KQKPQQERSE
     MGLLEKLEFV LNNEFMRLTY TEAIDILKNS KPNKSKKFNY LIEEWGADLQ SEHERYLVEK
     HFKKPVILTD YPAAIKAFYM KQNEDGKTVR AMDILFPGIG EIVGGSQREE NYDKLVKRMQ
     ELHLPTEELS WYLDTRRFGA CPHAGFGLGF ERLVLFVTGM GNIRDVIPFP RTPKSAEF
//

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