SYD_MYCCT
ID SYD_MYCCT Reviewed; 575 AA.
AC Q48979; Q2SSF5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Aspartate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00044};
DE EC=6.1.1.12 {ECO:0000255|HAMAP-Rule:MF_00044};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; OrderedLocusNames=MCAP_0323;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-524.
RX PubMed=7476192; DOI=10.1111/j.1365-2958.1995.tb02321.x;
RA Bork P., Ouzounis C., Casari G., Schneider R., Sander C., Dolan M.,
RA Gilbert W., Gillevet P.M.;
RT "Exploring the Mycoplasma capricolum genome: a minimal cell reveals its
RT physiology.";
RL Mol. Microbiol. 16:955-967(1995).
CC -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a
CC two-step reaction: L-aspartate is first activated by ATP to form Asp-
CC AMP and then transferred to the acceptor end of tRNA(Asp).
CC {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00044};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}.
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DR EMBL; CP000123; ABC01492.1; -; Genomic_DNA.
DR EMBL; Z33048; CAA83720.1; -; Genomic_DNA.
DR PIR; S77851; S77851.
DR RefSeq; WP_011387209.1; NC_007633.1.
DR AlphaFoldDB; Q48979; -.
DR SMR; Q48979; -.
DR EnsemblBacteria; ABC01492; ABC01492; MCAP_0323.
DR GeneID; 23778721; -.
DR KEGG; mcp:MCAP_0323; -.
DR HOGENOM; CLU_014330_3_2_14; -.
DR OMA; YQLDVEM; -.
DR OrthoDB; 226836at2; -.
DR PhylomeDB; Q48979; -.
DR Proteomes; UP000001928; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-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:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR029351; GAD_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR Pfam; PF02938; GAD; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55261; SSF55261; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00459; aspS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..575
FT /note="Aspartate--tRNA ligase"
FT /id="PRO_0000110901"
FT REGION 193..196
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 169
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 215..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 215
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 438
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 479
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 524..527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT CONFLICT 523..524
FT /note="WG -> ED (in Ref. 2; CAA83720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 66695 MW; 289766FD183ED7F0 CRC64;
MKRTHTCGEL TLQNVDQKVI LQGWVKKIRK LGAMVFIDLK DRYGITQLVI EQENINLINN
LKNEYVIEIS GIVVKRKSVN KELITGEIEV IVKDLLVINK SELTPFVLEN DVNVNEDTRL
TYRYLDLRRQ VMQNNLIIRA KINHIIRNYL TDLNFLEVET PYFAKSTPEG ARHFLVPSRL
NKNKFYALPQ SPQLFKQLLM ISGIDRYYQI VRCFRDEDLR IDRQPEFTQL DLEMSFATSE
DVMQISESLI KKILKEVKNF EIKEPLLRLS YKDAIDLYGS DKPDLRYELK IHTLNDIFKN
SDIKMFLDSQ NKYIRAVCID QLLTKKQLEE LNQQAKQFHF NSIAFIKVEN NAWSGSLASQ
LTEVQKKQLI EEFNIQNKAT IILNIGKYEE ISQLMGAIRI SLAKMFNLET KDDFKLLWVV
DFPLFEFSEQ ENRYVAAHHP FTSPKEESLA DFDTNKKDAL ACAYDLVMNG FEIGGGSQRI
TNSEIQQRMF DAVELNQKQV EANFGWFMNA YKYGAPYHAG IAWGLDRISM ILTDSNSIRD
VIAFPKNSLG IDMMSNAPDL VSDKQLDELN IKTVE
