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Database: UniProt
Entry: U1KA07_9GAMM
LinkDB: U1KA07_9GAMM
Original site: U1KA07_9GAMM 
ID   U1KA07_9GAMM            Unreviewed;       465 AA.
AC   U1KA07;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
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:ERG43739.1};
GN   Synonyms=asnS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   ORFNames=PRUB_17372 {ECO:0000313|EMBL:ERG43739.1};
OS   Pseudoalteromonas rubra DSM 6842.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117318 {ECO:0000313|EMBL:ERG43739.1};
RN   [1] {ECO:0000313|EMBL:ERG43739.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29570 {ECO:0000313|EMBL:ERG43739.1};
RX   PubMed=22374963; DOI=10.1128/JB.06822-11;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Zhou B.C.,
RA   Zhang Y.Z.;
RT   "Genome sequence of the cycloprodigiosin-producing bacterial strain
RT   Pseudoalteromonas rubra ATCC 29570(T).";
RL   J. Bacteriol. 194:1637-1638(2012).
RN   [2] {ECO:0000313|EMBL:ERG43739.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 29570 {ECO:0000313|EMBL:ERG43739.1};
RA   Xie B.-B., Rong J.-C., Qin Q.-L., Shu Y.-L., Zhang Y.-Z.;
RT   "Genome sequence of Pseudoalteromonas rubra.";
RL   Submitted (APR-2013) 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}.
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:ERG43739.1}.
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DR   EMBL; AHCD02000139; ERG43739.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1KA07; -.
DR   eggNOG; COG0017; Bacteria.
DR   OrthoDB; 9762036at2; -.
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          138..457
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   465 AA;  52370 MW;  4ADE405BD5170133 CRC64;
     MSHTAITELL AGTVAVDSQV TVKGWIRTRR DSKAGISFLA VHDGSCFDPI QAVVPNSLNN
     YEEVTRLTAG CSVAVTGVLV ASEGQGQAFE IQANKVEVLG WVENPDTYPM AAKRHSIEYL
     REHAHLRPRT NVIGAVTRVR NCLSQAIHRF FHERGYMWIS TPIITASDCE GAGEMFRVST
     LDMQNLPRTD KGDIDYSEDF FGKEAFLTVS GQLNGETYAS AMSKIYTFGP TFRAENSNTS
     RHLAEFWMVE PEVAFADLDD IAALAEDMLK YAFKAVLDER RDDMEFFAQR IEKQAITRLE
     SFIDKDFAQV DYTDAIEILK NCGKKFEFPV DWGVDLQSEH ERYLAEEHFN APVVIKNYPR
     DIKAFYMRQN EDGKTVAAMD VVAPGIGEII GGSQREERLD VLDQRLEEMG LDKEDYSWYR
     DLRKYGTVPH SGFGLGFERL VAYVTGMGNV RDVIAFPRTK GSATY
//
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