ID A0A1I2MZX2_9BACL Unreviewed; 430 AA.
AC A0A1I2MZX2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN02982927_00193 {ECO:0000313|EMBL:SFF96993.1};
OS Sporolactobacillus nakayamae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=269670 {ECO:0000313|EMBL:SFF96993.1, ECO:0000313|Proteomes:UP000198752};
RN [1] {ECO:0000313|EMBL:SFF96993.1, ECO:0000313|Proteomes:UP000198752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700379 {ECO:0000313|EMBL:SFF96993.1,
RC ECO:0000313|Proteomes:UP000198752};
RA de Groot N.N.;
RL Submitted (OCT-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; FOOY01000003; SFF96993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2MZX2; -.
DR STRING; 269670.SAMN02982927_00193; -.
DR OrthoDB; 9762036at2; -.
DR Proteomes; UP000198752; 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}.
FT DOMAIN 130..430
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 430 AA; 49196 MW; 4F2D0652A6C91910 CRC64;
MKATISKVKN HVGGEVTIGV WLANKRSSGK IQFLELRDGT GYIQGVVLKN EVSEENWAKA
KELTQESSLY VTGTVREDKR APSGFELTVT SIEIIQIAQD YPITPKEHGV EFLMDHRHLW
LRSSRQHAIL RIRNEVIKAT YDFFHDHEFI KVDPPILTGS SAEGTTDLFH TKYFDHDAYL
SQSGQLYMEA AAMAFGKVFS FGPAFRAEKS KTRRHLIEFW MIEPEMAFCD HEESLKVQEN
YVSYLVQEVL NNCKPELKAI GRDTTKLEKI KAPFPRISYD DAITFLKGKG FDDIEWGDDF
GSPHETAIAE HFDVPVFVTE YPTKVKAFYM KPNPERGEVV LCADLLAPEG YGEIIGGSQR
IDDLELMKER YEAFHLTDPS YKWYLELRQY GTVPHSGFGL GLERAVAWIC GLDHIRETIP
FPRLLNRIYP
//
