ID F6FFK7_MYCHI Unreviewed; 443 AA.
AC F6FFK7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:AEG72402.1};
GN OrderedLocusNames=MHF_0091 {ECO:0000313|EMBL:AEG72402.1};
OS Mycoplasma haemofelis (strain Ohio2).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=859194 {ECO:0000313|EMBL:AEG72402.1, ECO:0000313|Proteomes:UP000007952};
RN [1] {ECO:0000313|EMBL:AEG72402.1, ECO:0000313|Proteomes:UP000007952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ohio2 {ECO:0000313|EMBL:AEG72402.1,
RC ECO:0000313|Proteomes:UP000007952};
RX PubMed=21317328; DOI=10.1128/JB.00133-11;
RA Messick J.B., Santos A.P., Guimaraes A.M.;
RT "Complete genome sequences of two hemotropic Mycoplasmas, Mycoplasma
RT haemofelis strain Ohio2 and Mycoplasma suis strain Illinois.";
RL J. Bacteriol. 193:2068-2069(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ohio2;
RA Santos A.P., Guimaraes A.M.S., SanMiguel P.J., Martin S.W., Messick J.B.;
RT "The Genome of Mycoplasma haemofelis Strain Ohio2, a pathogenic hemoplasma
RT of the cat.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; CP002808; AEG72402.1; -; Genomic_DNA.
DR AlphaFoldDB; F6FFK7; -.
DR STRING; 859194.MHF_0091; -.
DR KEGG; mhf:MHF_0091; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_14; -.
DR BioCyc; MHAE859194:G1GR7-90-MONOMER; -.
DR Proteomes; UP000007952; 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: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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00534}.
FT DOMAIN 129..435
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 443 AA; 50775 MW; 90A50B0A661C4553 CRC64;
MRISHFLKNS ELNQKTRIEG WVKSFQVHGK DLVFISLNDG STCKDLQIVC KTGIDTSLLT
VGSAISASGF LQKSPKGGQD LEFVADGVEI LASADQKFPI QKKEHGFEFL REVSHQRART
RLFRIVNAIK NEVNYSIHEF FYSRGFTWIQ APILTSNNCE GGSEVFEIKN SENSFKKTTL
LSVSGQFHAE AMALGLKDVY TFGPTFRAEK SNTSQHLSEF WMIEPECSFS NLDGNINLME
DFLKFVVNRV LRNCHEELEF LADKLPNNED LIPRLENLLS EPFGRISYRE AIDMLLQEQK
KGVTFENNDI KFGIDLASEH ERYITSKFKK AVFITHYPRA IKAFYMKDCE DETVLAVDLL
VPEVGELMGG SERESDFEKL RIKAEEFGIP LDHLNWYLEL RKYGYYSSAG FGCGYERLIM
YLTGMKNIKD IINYPRSYGQ LNF
//
