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Database: UniProt
Entry: L0FUL6_ECHVK
LinkDB: L0FUL6_ECHVK
Original site: L0FUL6_ECHVK 
ID   L0FUL6_ECHVK            Unreviewed;       483 AA.
AC   L0FUL6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
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   OrderedLocusNames=Echvi_0072 {ECO:0000313|EMBL:AGA76370.1};
OS   Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Echinicola.
OX   NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA76370.1, ECO:0000313|Proteomes:UP000010796};
RN   [1] {ECO:0000313|Proteomes:UP000010796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC   {ECO:0000313|Proteomes:UP000010796};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Echinicola vietnamensis DSM 17526.";
RL   Submitted (FEB-2012) 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; CP003346; AGA76370.1; -; Genomic_DNA.
DR   RefSeq; WP_015263938.1; NC_019904.1.
DR   AlphaFoldDB; L0FUL6; -.
DR   STRING; 926556.Echvi_0072; -.
DR   KEGG; evi:Echvi_0072; -.
DR   PATRIC; fig|926556.3.peg.72; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_10; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 9802326at2; -.
DR   Proteomes; UP000010796; Chromosome.
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}; 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00534};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010796}.
FT   DOMAIN          137..475
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   483 AA;  54893 MW;  EAA5E7B5556D4925 CRC64;
     MAFNKRSKIK LLLESSKIGK NTTIMGWVRT KRGNKNVSFI AVNDGSTIQN YQVVADPNVI
     SEEVLKRITT GACIKATGEV VASQGAGQDS ELIAQKIEVL GEADADKYPL QPKKHSMEFL
     RENAHLRMRT NTFGAVFRVR HALAFAVHQY FNDKGFFYIH TPIITASDAE GAGETFRVST
     LDMKNPPLTE DGAVDYTKDF FERETNLTVS GQLEGELAAM ALAEIYTFGP TFRAENSNTT
     RHLAEFWMIE PEMAFYDAED NQDLAEDFLK YIISYAMEHC KADLEFLDKR AAEENAKKPT
     NERTELGLLD RLRFVVDHDF ERISYTEAIE ILKNSKPNKK KKFSYIIDEW GADLQSEHER
     FLVEKHFKKP VILTDYPKDI KAFYMKQNDD GKTVAAMDIL FPGIGEIVGG SQREENMEKL
     TTRMDEMGIS QEELYWYLDT RRFGATPHSG FGLGFERMVQ FVTGMGNIRD VIAFPRTPGN
     AEF
//
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