ID A0A1P9X3Y2_9BACT Unreviewed; 495 AA.
AC A0A1P9X3Y2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AWR27_06450 {ECO:0000313|EMBL:AQG82356.1};
OS Spirosoma montaniterrae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1178516 {ECO:0000313|EMBL:AQG82356.1, ECO:0000313|Proteomes:UP000187941};
RN [1] {ECO:0000313|EMBL:AQG82356.1, ECO:0000313|Proteomes:UP000187941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY10 {ECO:0000313|EMBL:AQG82356.1,
RC ECO:0000313|Proteomes:UP000187941};
RA Oliw E.H.;
RL Submitted (JAN-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; CP014263; AQG82356.1; -; Genomic_DNA.
DR RefSeq; WP_077133839.1; NZ_CP014263.1.
DR AlphaFoldDB; A0A1P9X3Y2; -.
DR STRING; 1178516.AWR27_06450; -.
DR KEGG; smon:AWR27_06450; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000187941; 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}; 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:UP000187941}.
FT DOMAIN 140..485
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 287..315
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 495 AA; 55668 MW; 5DF2D4C40BEDAC0F CRC64;
MSYLPIQQLL KTTPGPHVTV TVKGWVRNKR ESKNALFITL NDGSTINNIQ AVAERGPAEA
GQLSDDVLKL VTTGACVAVT GTLVESQGAG QAVEVKINNI HVYGPADPDK YPLQPKRHSL
EFLREIAHLR PRTNTFSAIL RVRHALAFAV HKYFNDNGFY YLNTPIITAS DAEGAGEMFR
VTTLDPVNPP RTEDGKVDYS QDFFGRETNL TVSGQLEGEL GALALGKIYT FGPTFRAENS
NTTRHLAEFW MIEPEMAFYE LPENMALAED FVKTVIRYAL QHCPDDLAFL DNRLKEEEKM
KKKEEQSELG LLEKLQFVIS NEFERLTYTE AIDILIQSKP AKKGQFQYEV KWGVDLQSEH
ERYLVEKHFK KPVILTNYPR EIKAFYMKQD DAPAVGARGE VFGPTVRAMD VLFPGIGEII
GGSQREDDLD KLTARMAEVG VEADAIWWYL DTRRFGSAPH AGFGLGFERL VQFVTGMGNI
RDVIPFPRAP KQAEF
//
