ID Q4A5X3_MYCS5 Unreviewed; 566 AA.
AC Q4A5X3;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Aspartate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00044};
DE EC=6.1.1.12 {ECO:0000256|HAMAP-Rule:MF_00044};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
DE Short=AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
GN Name=aspS {ECO:0000256|HAMAP-Rule:MF_00044,
GN ECO:0000313|EMBL:AAZ43848.1};
GN OrderedLocusNames=MS53_0436 {ECO:0000313|EMBL:AAZ43848.1};
OS Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=262723 {ECO:0000313|EMBL:AAZ43848.1, ECO:0000313|Proteomes:UP000000549};
RN [1] {ECO:0000313|EMBL:AAZ43848.1, ECO:0000313|Proteomes:UP000000549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=53 {ECO:0000313|EMBL:AAZ43848.1,
RC ECO:0000313|Proteomes:UP000000549};
RX PubMed=16077101; DOI=10.1128/JB.187.16.5568-5577.2005;
RA Vasconcelos A.T., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O.,
RA Pinto P.M., Almeida D.F., Almeida L.G., Almeida R., Alves-Filho L.,
RA Assuncao E.N., Azevedo V.A., Bogo M.R., Brigido M.M., Brocchi M.,
RA Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S., Carraro D.M.,
RA de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G.,
RA Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.,
RA Fiorentin L., Franco G.R., Freitas N.S., Frias D., Grangeiro T.B.,
RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA Laurino J.P., Lima L.F., Lopes M.I., Loreto E.L., Madeira H.M.,
RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R., Moreira M.A.,
RA Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.,
RA Pedrosa F.O., Pena S.D., Pereira M., Pereira-Ferrari L., Piffer I.,
RA Pinto L.S., Potrich D.P., Salim A.C., Santos F.R., Schmitt R.,
RA Schneider M.P., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA Silva D.W., Silva R., Silva S.C., Soares C.M., Souza K.R., Souza R.C.,
RA Staats C.C., Steffens M.B., Teixeira S.M., Urmenyi T.P., Vainstein M.H.,
RA Zuccherato L.W., Simpson A.J., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two strains
RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00044};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303, ECO:0000256|HAMAP-
CC Rule:MF_00044}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00044}.
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DR EMBL; AE017245; AAZ43848.1; -; Genomic_DNA.
DR RefSeq; WP_011283579.1; NC_007294.1.
DR AlphaFoldDB; Q4A5X3; -.
DR STRING; 262723.MS53_0436; -.
DR KEGG; msy:MS53_0436; -.
DR eggNOG; COG0173; Bacteria.
DR HOGENOM; CLU_014330_3_2_14; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000000549; 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 CDD; cd00777; AspRS_core; 1.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR047090; AspRS_core.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00459; aspS_bact; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 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; SSF55261; GAD domain-like; 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_00044};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00044}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00044};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00044};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00044}; Reference proteome {ECO:0000313|Proteomes:UP000000549}.
FT DOMAIN 99..536
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 188..191
FT /note="Aspartate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 165
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 210..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 210
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 429
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 470
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 515..518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ SEQUENCE 566 AA; 65581 MW; 785CEFE08678E494 CRC64;
MKFSKISNTS LDESYINKSV TLYGWVATKR KFGKISFVDL RDHSGIIQLV FSEDIKLSKE
SVIKVTGVVS KRKDINPSLK TGTIEVLVSE YELLSSSKEL PFEISEKISA SEDLRMEYRF
LDLRRESMQN AISLRSEVFF AIREFLNKEK FLEIETPILA KATPEGARDF LVPTRSQNNF
FALPQSPQLF KQLLMASGFE KYYQIARCFR DEDSRKDRQP EFTQLDMEVS FLEVSAFQKL
VENLFKYVFK KVLNVDIQTP FQRLDFDTCI KDYGTDKPDL RFDLKIQDIN NYFQEDNFEI
IKKQASKRML FINEQITKKD FKALEEIAKK NSANILFYFV LENGKVLHSN FANKAPRDVE
KLIKDHNFKN GTCFIVANNF DNASKALGAL RVELNSMFNY AKNSYNFSWI INWPMFEFNE
ESQSYQAAHH PFTMFENTVE EFKTLSKNQI KAKSYDLVLN GFELGSGSAR IYSKEVQELI
FESLGMDKKE QEEKFGFFLK AFDYGLPPHC GIGLGLDRLL MILANKSTIR DVIAFPKNAK
NKDIFTKAPS EISSKQLSEL FLELKK
//
