ID S5MG01_9MOLU Unreviewed; 455 AA.
AC S5MG01;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:AGR40790.1};
GN Synonyms=asnS {ECO:0000256|HAMAP-Rule:MF_00534};
GN ORFNames=STAIW_v1c01000 {ECO:0000313|EMBL:AGR40790.1};
OS Spiroplasma taiwanense CT-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276220 {ECO:0000313|EMBL:AGR40790.1, ECO:0000313|Proteomes:UP000014984};
RN [1] {ECO:0000313|EMBL:AGR40790.1, ECO:0000313|Proteomes:UP000014984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT-1 {ECO:0000313|EMBL:AGR40790.1};
RX PubMed=23873917; DOI=10.1093/gbe/evt108;
RA Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT "Comparison of metabolic capacities and inference of gene content evolution
RT in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL Genome Biol. Evol. 5:1512-1523(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}.
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DR EMBL; CP005074; AGR40790.1; -; Genomic_DNA.
DR RefSeq; WP_020833929.1; NC_021846.1.
DR AlphaFoldDB; S5MG01; -.
DR STRING; 1276220.STAIW_v1c01000; -.
DR KEGG; stai:STAIW_v1c01000; -.
DR PATRIC; fig|1276220.3.peg.101; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_14; -.
DR OrthoDB; 9762036at2; -.
DR Proteomes; UP000014984; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000014984}.
FT DOMAIN 133..445
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 455 AA; 52306 MW; E78E312BAB041745 CRC64;
MKDIKEIFES YLKLVENQIT FIGRVRSHRQ SKVVSFLVLN DGTTINDIQV VYKNDIENYD
LVSQGRVSSI FEVTGNLILT SGKPQPFEIQ ATKINLLDQS IEEYPLQKKE HSQEFLREIA
HLRARTKTFQ AIFKIRSSAA FAIHKFFQEK NFVYVNSPII TENDAEGAGE AFVVTTRTDG
KYSQDFFGKK AALTVSGQLN AEAYAQAFKN VYTFGPTFRA ENSYTSKHAA EFWMIEPEMA
FVDLSINLEV IEELIKYIVN YLFDNNIDEL KFCNDNLEAG LIEKLNILRN SNFAVNSYEQ
VIEILKDAVK NGYVFEENNI EFGLDLGTEH ERYICEVVNK KPTFVTNYPK EIKAFYMKQN
SDNRTVAAAD LLVPGIGELV GGSQREDNYE KLIKRSEEMG MNPKDLWWYN DLRKYGYYKS
SGFGLGFERL IMYVTGASNI RDVIPFPRTP KNLFF
//
