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Database: UniProt
Entry: A0A090IUV9_9BACI
LinkDB: A0A090IUV9_9BACI
Original site: A0A090IUV9_9BACI 
ID   A0A090IUV9_9BACI        Unreviewed;       430 AA.
AC   A0A090IUV9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
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:CEE01846.1};
GN   Synonyms=asnC {ECO:0000313|EMBL:AWI12670.1};
GN   ORFNames=BT1A1_2024 {ECO:0000313|EMBL:CEE01846.1}, CQJ30_11215
GN   {ECO:0000313|EMBL:AWI12670.1};
OS   Caldibacillus thermoamylovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX   NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE01846.1, ECO:0000313|Proteomes:UP000040576};
RN   [1] {ECO:0000313|EMBL:CEE01846.1, ECO:0000313|Proteomes:UP000040576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg Daniel;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AWI12670.1, ECO:0000313|Proteomes:UP000244914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSBM {ECO:0000313|EMBL:AWI12670.1,
RC   ECO:0000313|Proteomes:UP000244914};
RX   PubMed=29625286; DOI=10.1016/j.biortech.2018.03.121;
RA   Cai L., Zheng S.W., Shen Y.J., Zheng G.D., Liu H.T., Wu Z.Y.;
RT   "Complete genome sequence provides insights into the biodrying-related
RT   microbial function of Bacillus thermoamylovorans isolated from sewage
RT   sludge biodrying material.";
RL   Bioresour. Technol. 260:141-149(2018).
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; CP023704; AWI12670.1; -; Genomic_DNA.
DR   EMBL; CCRF01000061; CEE01846.1; -; Genomic_DNA.
DR   RefSeq; WP_034770591.1; NZ_CP023704.1.
DR   AlphaFoldDB; A0A090IUV9; -.
DR   KEGG; bthv:CQJ30_11215; -.
DR   Proteomes; UP000040576; Unassembled WGS sequence.
DR   Proteomes; UP000244914; 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: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:UP000040576}.
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;  49616 MW;  5A2A47462FDB15C7 CRC64;
     MKTTIVEVKN YVGQEVTIGA WLANKRSSGK IAFLQLRDGS GFIQGVVVKN EVPEEVFQLA
     KSLTQESSLY VTGIVREDER SPFGYELSVT KLELIHEAHD YPITPKEHGT EFLMDHRHLW
     LRSKRQHANM KIRNEIIRAT YEFFNKEGFI KIDPPILTGS APEGTTELFH TKYFDEDAYL
     SQSGQLYMEA AAMAFGKVFS FGPTFRAEKS KTRRHLIEFW MIEPEMAFYE FEDNLKVQED
     YVSYVVQSVL KNCSLELKIL NRDTTKLEKV QAPFPRITYD DAIKFLHEQG FDDIKWGDDF
     GSPHETAIAN SFDKPVFITH YPKAIKPFYM QPDPTRDDVV LCADLIAPEG YGEIIGGSER
     IHDYDLLKQE LERHQLSLET YSWYLDLRKY GSVPHSGFGL GLERTVAWIA GCEHVRETIP
     FPRLLNRLYP
//
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