SYDND_MYCS2
ID SYDND_MYCS2 Reviewed; 598 AA.
AC A0QWN3; I7G141;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044};
DE EC=6.1.1.23 {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};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044};
GN OrderedLocusNames=MSMEG_3003, MSMEI_2928;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since
CC it is able to aspartylate not only its cognate tRNA(Asp) but also
CC tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first
CC activated by ATP to form Asp-AMP and then transferred to the acceptor
CC end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710,
CC Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.23; 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; CP000480; ABK74097.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39392.1; -; Genomic_DNA.
DR RefSeq; WP_003894384.1; NZ_SIJM01000002.1.
DR RefSeq; YP_887321.1; NC_008596.1.
DR PDB; 4O2D; X-ray; 2.60 A; A/B=2-598.
DR PDB; 4RMF; X-ray; 2.40 A; A=1-598.
DR PDBsum; 4O2D; -.
DR PDBsum; 4RMF; -.
DR AlphaFoldDB; A0QWN3; -.
DR SMR; A0QWN3; -.
DR STRING; 246196.MSMEI_2928; -.
DR PRIDE; A0QWN3; -.
DR EnsemblBacteria; ABK74097; ABK74097; MSMEG_3003.
DR EnsemblBacteria; AFP39392; AFP39392; MSMEI_2928.
DR GeneID; 66734410; -.
DR KEGG; msg:MSMEI_2928; -.
DR KEGG; msm:MSMEG_3003; -.
DR PATRIC; fig|246196.19.peg.2965; -.
DR eggNOG; COG0173; Bacteria.
DR OMA; YQLDVEM; -.
DR OrthoDB; 226836at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..598
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_1000006711"
FT REGION 194..197
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT REGION 558..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 216..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 216
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 448
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 489
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 534..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 31
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 80
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 18..31
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:4RMF"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4O2D"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 131..153
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:4O2D"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 226..237
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 240..256
FT /evidence="ECO:0007829|PDB:4RMF"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:4RMF"
FT TURN 295..300
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:4RMF"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 363..367
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 388..406
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:4RMF"
FT TURN 459..464
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 493..502
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 507..520
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 535..543
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:4RMF"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:4RMF"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:4RMF"
FT TURN 563..566
FT /evidence="ECO:0007829|PDB:4RMF"
FT HELIX 573..576
FT /evidence="ECO:0007829|PDB:4RMF"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:4RMF"
SQ SEQUENCE 598 AA; 65170 MW; FB69715BC10C2FBE CRC64;
MLRTHAAGSL RPADAGQTVT LAGWVARRRD HGGVIFIDLR DASGVSQVVF REGDVLAAAH
RLRAEFCVAV TGVVEVRPEG NENPEIPTGQ IEVNATELTV LGESAPLPFQ LDEQAGEEAR
LKYRYLDLRR EGPGNALRLR SKVNAAARSV LAEHDFVEIE TPTLTRSTPE GARDFLVPAR
LQPGSFYALP QSPQLFKQLL MVAGMERYYQ IARCYRDEDF RADRQPEFTQ LDMEMSFVEA
DDVIAISEQV LKAVWATIGY DLPLPLPRIS YEEAMRRFGS DKPDLRFGIE LVECTEYFKD
TTFRVFQAPY VGAVVMPGGA SQPRRTLDGW QEFAKQRGHK GLAYVLVGED GTLGGPVAKN
LSDAERDGLV AHVGANPGDC IFFAAGPAKG ARALLGATRI EIAKRLDLID PNAWAFTWVV
DFPMFEAADE ATAAGDVAVG SGAWTAMHHA FTAPKPDSVD TFDSDPGNAL SDAYDIVCNG
NEIGGGSIRI HRRDIQERVF AMMGIDHDEA QEKFGFLLDA FSYGAPPHGG IAFGWDRITA
LLAGVDSIRE VIAFPKSGGG VDPLTDAPAP ITPQQRKESG IDAKPREDKP KEDAKSKA
