ID A0A0K2M512_9NOST Unreviewed; 463 AA.
AC A0A0K2M512;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=AA650_23405 {ECO:0000313|EMBL:ALB43014.1};
OS Anabaena sp. WA102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB43014.1, ECO:0000313|Proteomes:UP000056652};
RN [1] {ECO:0000313|EMBL:ALB43014.1, ECO:0000313|Proteomes:UP000056652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA102 {ECO:0000313|EMBL:ALB43014.1,
RC ECO:0000313|Proteomes:UP000056652};
RA Brown N.M.;
RT "The finished genome of an anatoxin-a-producing Anabaena isolate reveals
RT extensive genome rearrangement.";
RL Submitted (MAY-2015) 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; CP011456; ALB43014.1; -; Genomic_DNA.
DR RefSeq; WP_053540852.1; NZ_CP011456.1.
DR AlphaFoldDB; A0A0K2M512; -.
DR STRING; 1647413.AA650_23405; -.
DR KEGG; awa:AA650_23405; -.
DR PATRIC; fig|1647413.5.peg.5517; -.
DR OrthoDB; 9762036at2; -.
DR Proteomes; UP000056652; 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}; 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}.
FT DOMAIN 135..453
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 463 AA; 52826 MW; 22035A78B16419EF CRC64;
MLNPRIAEIL RSGKPEQTLV VQGWVRTKRE LKGFAFLEVN DGSSLGNLQI VINQDLPDYQ
GILKQINTGG SIEVSGVLVA SQGKGQRIEL KADTVKVYGD ADPDTYPLQK KRHSFEFLRT
IAHLRPRTNS FGAVFRVRNA CAIAIHQFFQ QRGFLWVHTP IITASDCEGA GELFSVTNFN
LKNVPKTENQ EIDYSQDFFS KPAYLTVSGQ LEAEIMAMAF TNVYTFGPTF RAENSNTSRH
LAEFWMVEPE MAFCDLEGDM DVAEEFLKHI FKYVMETCPE DMEFFNERID NTVLETANNI
INNQFARLTY TEAVKLLEKA DVKFDYPVSW GADLQSEHER YLAEQLFKKP VIVTDYPAQI
KAFYMRLSDD EKTVRAMDIL APKIGEIIGG SQREERLDVL EKRVLAQGMK PEDLWWYLDL
RRYGTVPHAG FGLGFERLVQ FMTGMGNIRD VIPFPRTPQS ADF
//
