ID K8ZLH1_9ENTE Unreviewed; 432 AA.
AC K8ZLH1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=C683_0739 {ECO:0000313|EMBL:EKU27408.1};
OS Catellicoccus marimammalium M35/04/3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Catellicoccus.
OX NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU27408.1, ECO:0000313|Proteomes:UP000016057};
RN [1] {ECO:0000313|EMBL:EKU27408.1, ECO:0000313|Proteomes:UP000016057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU27408.1,
RC ECO:0000313|Proteomes:UP000016057};
RX PubMed=23405330;
RA Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T., Santo Domingo J.W.;
RT "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species
RT Commonly Found in Gull Feces.";
RL Genome Announc. 1:E00019-12(2013).
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:EKU27408.1}.
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DR EMBL; AMYT01000017; EKU27408.1; -; Genomic_DNA.
DR RefSeq; WP_009490145.1; NZ_AMYT01000017.1.
DR AlphaFoldDB; K8ZLH1; -.
DR STRING; 1234409.C683_0739; -.
DR PATRIC; fig|1234409.3.peg.690; -.
DR eggNOG; COG0017; Bacteria.
DR OrthoDB; 9762036at2; -.
DR Proteomes; UP000016057; 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}; Reference proteome {ECO:0000313|Proteomes:UP000016057}.
FT DOMAIN 133..432
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 432 AA; 49410 MW; E0F73B0B04566B67 CRC64;
MEKISIIDSK NHVNEVVEIN GWIANKRSSG KIAFLTLRDG SAYFQGIVLK ETVGEEAFAQ
IKNLPQETAV KIIGEIHEDK RSKFGYEIEI SQLEVIGTSG DYPITPKEHG TDFLMDHRHL
WLRSSKQHAI MQIRNEIIRA TYEFFNDRGF IKIDPPILTG SAPEGTTELF ETDYFGQSAY
LSQSGQLYAE AAAMAFGKVF TFGPTFRAEK SKTRRHLTEF WMIEPEMAFT HQDESLKVQE
DYVAFLVRNV LDHCEYALDV LGRDRDVLER YTQTPYPRIS YDEAIELLKE NGFDDIEWGD
DFGSPHETFI ANSFEKPVFI MNYPAKIKPF YMPLAPGRDD VVICADLIAP EGYGEIIGGS
EREVDYDVLA ENIEKFGLSE EEYGWYLDLR KYGSVPHSGF GLGLERTVTW ISGIEHIREA
SPFPRLLHRL RP
//
