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Database: UniProt
Entry: A0A0F5H116_9MOLU
LinkDB: A0A0F5H116_9MOLU
Original site: A0A0F5H116_9MOLU 
ID   A0A0F5H116_9MOLU        Unreviewed;       455 AA.
AC   A0A0F5H116;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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:KKB26898.1};
GN   ORFNames=MMELEA_04760 {ECO:0000313|EMBL:KKB26898.1};
OS   Mycoplasmopsis meleagridis ATCC 25294.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=1264554 {ECO:0000313|EMBL:KKB26898.1, ECO:0000313|Proteomes:UP000033750};
RN   [1] {ECO:0000313|EMBL:KKB26898.1, ECO:0000313|Proteomes:UP000033750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25294 {ECO:0000313|EMBL:KKB26898.1,
RC   ECO:0000313|Proteomes:UP000033750};
RA   Yacoub E., Blanchard A., Sirand-Pugnet P., Mardassi B.B.A.;
RT   "Genome sequence of Mycoplasma meleagridis strain ATCC 25294.";
RL   Submitted (MAR-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|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       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:KKB26898.1}.
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DR   EMBL; JZXN01000015; KKB26898.1; -; Genomic_DNA.
DR   RefSeq; WP_046096900.1; NZ_JZXN01000015.1.
DR   AlphaFoldDB; A0A0F5H116; -.
DR   STRING; 29561.MM26B8_03450; -.
DR   PATRIC; fig|1264554.4.peg.421; -.
DR   OrthoDB; 9762036at2; -.
DR   Proteomes; UP000033750; 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:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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:UP000033750}.
FT   DOMAIN          138..445
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   455 AA;  51834 MW;  0D0C6C4C71BB4B0A CRC64;
     MKEITIKKLL QNIEAFDGQN ISLKAWVNAN RGNNKVRFIS LNDGSTVSSL QVIVKEENKN
     IDISQLDDRI VHLGAAVFVE GTVKYTPSSK QICELVANNF ILLKDAEDYP IQKKAVNLET
     LREIPHVRHR TNLLRTVFLI RSTLALEIHK YFRENDFLYF NAPIITSNDG EGAGETFVVN
     DENIESPFFG NKKATLGVTG QLHGESFALG YKKIYTFAPT FRAEHSNTKK HAAEFWMIEP
     EVAFYDLNDI INLADDLLKT VIKKTIELHP DEFKFLIENI DKNLLEKLNL FINKKLTVLD
     YKDAIKELEK VKDIFEEKDI KFGLDLATEH ERYLAEKLIG GPVAIINFPK DFKAFYMYQN
     DDGKSVAAFD LLVPGIGELI GGSQREVRED KLLERIKEIG INQEDLQWYI NLRKFGNAGS
     SGFGIGFERL VMYVTGVDNI RDVIPYPRTS GNIKM
//
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