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Database: UniProt
Entry: D8FUV1_9CYAN
LinkDB: D8FUV1_9CYAN
Original site: D8FUV1_9CYAN 
ID   D8FUV1_9CYAN            Unreviewed;       463 AA.
AC   D8FUV1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 63.
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=asnC {ECO:0000313|EMBL:CBN54141.1};
GN   Synonyms=asnS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   ORFNames=OSCI_590016 {ECO:0000313|EMBL:CBN54141.1};
OS   Kamptonema sp. PCC 6506.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Kamptonema.
OX   NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN54141.1, ECO:0000313|Proteomes:UP000004532};
RN   [1] {ECO:0000313|Proteomes:UP000004532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX   PubMed=20675499; DOI=10.1128/JB.00704-10;
RA   Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT   "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT   reveals several gene clusters responsible for the biosynthesis of toxins
RT   and secondary metabolites.";
RL   J. Bacteriol. 192:5264-5265(2010).
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; CACA01000056; CBN54141.1; -; Genomic_DNA.
DR   RefSeq; WP_007353368.1; NZ_CACA01000056.1.
DR   AlphaFoldDB; D8FUV1; -.
DR   OrthoDB; 9762036at2; -.
DR   Proteomes; UP000004532; 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:UP000004532}.
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;  53178 MW;  FF0B1048B5F7444A CRC64;
     MTTQRIAVLL RNGQPDENVT VQGWVRTKRE LKEFTFVEVN DGSAMANLQV VINLNLPNYE
     HIVKQLNTGA SVEVTGVLVA SPAKGQRIEL KASAVTVYGD ADPQTYPLQK KRHSFEFLRT
     IAHLRSRTNT YSAVFRVRNA CAHAVHQFFQ ERGFLWVHTP IITASDCEGA GEMFSVTNFD
     LKNIPRNDRE QIDFTKDFFG KPAYLTVSGQ LEAEVMAMAF GNVYTFGPTF RAENSNTSRH
     LAEFWMIEPE MAFCDLEGDM DLAEAFLKHI FKYVLETCQE DIEFFNERID KTVLATAENI
     INNQFERITY TEAVRLLEQA DKQFEFPVKW GLDLQSEHER YLAEELFKKP TIVTDYPVEI
     KAFYMRLSDD EKTVRAMDVL APKIGEIIGG SQREERLDVL ERRIEAQGMN KEDLWWYLDL
     RRYGTVPHAG FGLGFERVVQ FMTGMGNIRD VIPFPRAPLT IDF
//
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