ID A0A1S1V8U7_9FIRM Unreviewed; 462 AA.
AC A0A1S1V8U7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, 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 ECO:0000313|EMBL:OHW63018.1};
GN ORFNames=EUAN_08020 {ECO:0000313|EMBL:OHW63018.1};
OS Andreesenia angusta.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae;
OC Andreesenia.
OX NCBI_TaxID=39480 {ECO:0000313|EMBL:OHW63018.1, ECO:0000313|Proteomes:UP000180254};
RN [1] {ECO:0000313|EMBL:OHW63018.1, ECO:0000313|Proteomes:UP000180254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1989 {ECO:0000313|EMBL:OHW63018.1,
RC ECO:0000313|Proteomes:UP000180254};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Eubacterium angustum.";
RL Submitted (SEP-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}.
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:OHW63018.1}.
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DR EMBL; MKIE01000002; OHW63018.1; -; Genomic_DNA.
DR RefSeq; WP_071061916.1; NZ_MKIE01000002.1.
DR AlphaFoldDB; A0A1S1V8U7; -.
DR STRING; 39480.EUAN_08020; -.
DR OrthoDB; 9762036at2; -.
DR Proteomes; UP000180254; 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:0016740; F:transferase activity; IEA:UniProt.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000180254}.
FT DOMAIN 135..452
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 462 AA; 52886 MW; E065DEAC4FBD8712 CRC64;
MKSQSVRELY RGQDSFIDSE VFVKGWIRTL RNSKSFGFIE LNDGTFFKNI QIVFDEELGN
FEKISKLSIS SAIEVKGKLV ATPGAKQPFE IKATDIAVAA ESEGDFPLQK KRHSLEYLRT
IAHLRPRSNT FSAVFRVRSL AAYAIHKFFQ ERDFIYVHTP VITGSDAEGA GEMFRVTTMD
PINPPMADGK LDYSKDFFGK ETNLTVSGQL EGETFAMAFK NIYTFGPTFR AENSNTTRHA
AEFWMIEPEI AFADLEDDME LAEDMLKYII SYVLENAPEE MEFFNSFVDK GLLDRLNNIV
SSDFERITYT KAVEILKEAK AEFEFPVEWG CDLQTEHERY LTEEVYKKPV FVTDYPKEIK
AFYMKLNDDN KTVAAMDLLV PGIGEIIGGS QREVNLELLK ERMKESGLDE KEYWWYLDLR
KYGGADHAGF GLGFERAIMY LTGISNIRDV IPFPRTVKSA EF
//
