ID A0A0D0GKM2_9SPHI Unreviewed; 482 AA.
AC A0A0D0GKM2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=TH53_23395 {ECO:0000313|EMBL:KIO74961.1};
OS Pedobacter lusitanus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1503925 {ECO:0000313|EMBL:KIO74961.1, ECO:0000313|Proteomes:UP000032049};
RN [1] {ECO:0000313|EMBL:KIO74961.1, ECO:0000313|Proteomes:UP000032049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL19 {ECO:0000313|EMBL:KIO74961.1,
RC ECO:0000313|Proteomes:UP000032049};
RA Santos T., Caetano T., Covas C., Cruz A., Mendo S.;
RT "Draft genome sequence of Pedobacter sp. NL19 isolated from sludge of an
RT effluent treatment pond in an abandoned uranium mine.";
RL Submitted (JAN-2015) 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:KIO74961.1}.
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DR EMBL; JXRA01000121; KIO74961.1; -; Genomic_DNA.
DR RefSeq; WP_041886264.1; NZ_JXRA01000121.1.
DR AlphaFoldDB; A0A0D0GKM2; -.
DR STRING; 1503925.TH53_23395; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000032049; 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00534}.
FT DOMAIN 132..474
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 482 AA; 55335 MW; 127282707DAFBE50 CRC64;
MIKREKIKSL LETTDFNREV TVMGWVRTFR NNQFIAINDG SCMGNIQIVV DFENTAEELL
KRITTGAAIA VTGQLVESLG KGQRVDVKAT SIEILGDSDA EKFPLQPKKH SLEFLREIAH
LRFRTNTFNA VFKVRHALAF AIHQFYNERG FVYMHTPVIT ASDAEGAGEM FKVTTLDFDN
TPRTEDGNVD FSEDFFGRAT NLTVSGQLEG ELAAMAFGQI YTFGPTFRAE NSNTTRHLAE
FWMVEPEIAF ADLEDNMQLA EDMMKYIITY ALENCKEEIE FLNNRLLEDE KTKPQQERSE
LSLIEKLNFC IGNDFVRLTY TEAIAILRSS KPNQKKQFKY LINEWGADLQ SEHERFLVEK
HFKKPVILTD YPADIKAFYM RQNEPDAEGR KTVAAMDVLF PGIGEMIGGA QREERMDKLT
QRMDEMNIPQ EELWWYLDTR RFGSAPHAGF GLGFERLVLF VTGMTNIRDV IAFPRFPKNA
EF
//
