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Database: UniProt
Entry: A0A1T4NDZ8_9ACTN
LinkDB: A0A1T4NDZ8_9ACTN
Original site: A0A1T4NDZ8_9ACTN 
ID   A0A1T4NDZ8_9ACTN        Unreviewed;       467 AA.
AC   A0A1T4NDZ8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   08-NOV-2023, entry version 26.
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=SAMN06298223_1381 {ECO:0000313|EMBL:SJZ76998.1};
OS   Olsenella sp. KH1P3.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=1945884 {ECO:0000313|EMBL:SJZ76998.1, ECO:0000313|Proteomes:UP000190585};
RN   [1] {ECO:0000313|Proteomes:UP000190585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1P3 {ECO:0000313|Proteomes:UP000190585};
RA   Varghese N., Submissions S.;
RL   Submitted (FEB-2017) 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; FUWQ01000004; SJZ76998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4NDZ8; -.
DR   OrthoDB; 9802326at2; -.
DR   Proteomes; UP000190585; 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:UP000190585}.
FT   DOMAIN          145..457
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   467 AA;  53058 MW;  BC69C358FAD711F0 CRC64;
     MDLTKIAQLY AQMDQYGDAT VTVAGWVRSI RDMKNFGFVM LNDGSCFKDL QVVMNRESLN
     NYEDVAALTV GSALVITGRL ALTPDRPQPF ELQAETIVIE GAAQPDYPMQ KKRQSREFLR
     TQQHLRSRTN LFRAVFRVRS VAAFAIHQFF QERGYVYVNT PIITASDAEG AGEMFRVTTI
     DPANPPLTED GKVDYSKDFF GKATNLTVSG QLQGENFAMS FGDIYTFGPT FRAEDSNTRR
     HAAEFWMVEP EMAFCDLEGE MNVSEDMLKF VISRVMERCP DEIDMFNSFV DKGLRERLQH
     VATSDFARVS YTDAIKILQD AQAAGHVFEY PVEWGVDLQT EHERFLTEEH FKKPTFVTDY
     PAAIKAFYMR MNDDGKTVAA ADCLVPGIGE IIGGSQREER LDVLQKRIED LGMDAEQYKY
     YLDLRRYGTC HHAGFGLGFE RLVMYLTGMD NIRDVLPHPR TVGNADF
//
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