ID M5J6W0_9LACO Unreviewed; 432 AA.
AC M5J6W0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=D271_03929 {ECO:0000313|EMBL:EKW99087.1};
OS Ligilactobacillus saerimneri 30a.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW99087.1, ECO:0000313|Proteomes:UP000011912};
RN [1] {ECO:0000313|EMBL:EKW99087.1, ECO:0000313|Proteomes:UP000011912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30a {ECO:0000313|EMBL:EKW99087.1,
RC ECO:0000313|Proteomes:UP000011912};
RX PubMed=23405290;
RA Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA Lolkema J.S., Lucas P.M.;
RT "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT Biogenic Amines.";
RL Genome Announc. 1:E00097-E00012(2013).
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:EKW99087.1}.
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DR EMBL; ANAG01000012; EKW99087.1; -; Genomic_DNA.
DR RefSeq; WP_009553456.1; NZ_ANAG01000012.1.
DR AlphaFoldDB; M5J6W0; -.
DR STRING; 1227363.D271_03929; -.
DR GeneID; 80986667; -.
DR PATRIC; fig|1227363.6.peg.765; -.
DR Proteomes; UP000011912; 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; cd04323; AsnRS_cyto_like_N; 1.
DR CDD; cd00776; AsxRS_core; 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:UP000011912}.
FT DOMAIN 132..432
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 432 AA; 49612 MW; 35C2C182B3608556 CRC64;
MQTITISESP KHVNETVKIG VWLTDKRSSG KIAFLQLRDG TGFFQGILLK NQVTPEVWDM
AKHELHQETS FWVTGEIHED SRSKFGYEIQ VQSIELVGES DDYPIGNKEH GVEFLMDHRH
LWLRSSKPNA MLKIRSQVKL ATMEFFAKHG FTQLDAPILT GSSPEGTTDL FHTKYFDDDA
YLSQSGQLYA EAGAMALGKV YTMGPTFRAE KSKTRRHLTE FWMIEPEMAW MHQPESLELQ
EQYIAYLVQS LIDNCARELE TVGRSVESLR PFTELPYPRI TYKKAIEMLQ EGGFDSKFGD
DFGSPEETYL ADQFQKPVFI LNYPKEIKAF YMKPDPEDDR QVVCADLLAP EGYGEIIGGS
ERATDYDYLV QKFAENHLDM ADYGWYADLR KYGTVPHSGF GMGLERFIAW ITLSDHIREG
SPFPRMLNRL RP
//
