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Database: UniProt
Entry: L1P9L8_9FLAO
LinkDB: L1P9L8_9FLAO
Original site: L1P9L8_9FLAO 
ID   L1P9L8_9FLAO            Unreviewed;       476 AA.
AC   L1P9L8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   08-NOV-2023, entry version 53.
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=HMPREF9075_00382 {ECO:0000313|EMBL:EKY12321.1};
OS   Capnocytophaga sp. oral taxon 332 str. F0381.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1127692 {ECO:0000313|EMBL:EKY12321.1, ECO:0000313|Proteomes:UP000010419};
RN   [1] {ECO:0000313|EMBL:EKY12321.1, ECO:0000313|Proteomes:UP000010419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0381 {ECO:0000313|EMBL:EKY12321.1,
RC   ECO:0000313|Proteomes:UP000010419};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-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}.
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:EKY12321.1}.
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DR   EMBL; AMET01000026; EKY12321.1; -; Genomic_DNA.
DR   RefSeq; WP_009416604.1; NZ_KB291341.1.
DR   AlphaFoldDB; L1P9L8; -.
DR   STRING; 1127692.HMPREF9075_00382; -.
DR   PATRIC; fig|1127692.3.peg.356; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_10; -.
DR   OrthoDB; 9762036at2; -.
DR   Proteomes; UP000010419; 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}; 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:UP000010419}.
FT   DOMAIN          130..466
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   476 AA;  54787 MW;  48D36498B9E98764 CRC64;
     MLYIKQLLQE GKTIEGEVTL QGWVRTFRSN RFIALNDGST IHNLQVVVDF ENTPEETLKR
     ITTGAAIKVK GQVVESQGKG QNVELQASEV TILGDSNPEE YPIQPKKHSL EFLRENAHLR
     VRTNAFGAIM RVRSTLAYAI HKYFQDNGFF YVNTPIITGS DAEGAGEMFR VTTLDAKKPP
     LNENGEVDYK KDFFGRETNL TVSGQLEGET FAMALGKIYT FGPTFRAENS NTSRHLAEFW
     MIEPEMAFFD LIDNMNLAED FIKSVLKYTL EVRRDDIEFL NTRFLEEEKS KPQQERSSMS
     LIEKLEFVIH NDFKRVSYTE AIDILKNCNH NKKKKFQYLI DEWGVDLQSE HERYLVEKHF
     GCPVILYDYP AKIKAFYMRL NDDGKTVRAM DILFPGIGEI VGGSQREERY EVLKQKIADL
     GMDEQTLWWY LDLRKFGTAT HSGFGLGFER LVLFATGMTN IRDVIPYPRT PQSAEF
//
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