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Database: UniProt
Entry: A0A1S4APY2_TOBAC
LinkDB: A0A1S4APY2_TOBAC
Original site: A0A1S4APY2_TOBAC 
ID   A0A1S4APY2_TOBAC        Unreviewed;       541 AA.
AC   A0A1S4APY2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE            EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
DE   AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033155};
GN   Name=LOC107800111 {ECO:0000313|RefSeq:XP_016478744.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016478744.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016478744.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000225};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312}.
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DR   RefSeq; XP_016478744.1; XM_016623258.1.
DR   AlphaFoldDB; A0A1S4APY2; -.
DR   SMR; A0A1S4APY2; -.
DR   STRING; 4097.A0A1S4APY2; -.
DR   PaxDb; 4097-A0A1S4APY2; -.
DR   GeneID; 107800111; -.
DR   KEGG; nta:107800111; -.
DR   OMA; TEMSFVN; -.
DR   OrthoDB; 382728at2759; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd04320; AspRS_cyto_N; 1.
DR   CDD; cd00776; AsxRS_core; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00458; aspS_nondisc; 1.
DR   PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR43450; ASPARTYL-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   Ligase {ECO:0000313|RefSeq:XP_016478744.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000084051}.
FT   DOMAIN          233..533
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  60612 MW;  3792F1993E16875E CRC64;
     MASDSEEGSN QGKKLSKKEA AKLERQRKRQ EAAAAAATTA LSAVSVDEGP DPLASNYGDV
     LLNDLQSKVL SGRQWTKVEL LAPVMRDQVV LIRGRVQTIR PVGKKIAFVV VRERGFTVQC
     VLTVKPELVS AQMVKFATSL SKESIVDVEG VVTVPEKPIT GATQQQVEVQ ISKLYCVNKA
     VPTLPINIED AARSEVEIEQ ALEKGEQLVR VNQDTRLNYR ILDMRTPANQ GIFRIQCQVE
     NIFRQFLLSE GFVGIHTPKL IGGSSEGGSA VFRLDYKGQP ACLAQSPQLH KQMAICGDFG
     RVFEIGPVFR AEDSFTHRHL CEFTGLDVEM EIKEHYSEVM DIVDRLFVTI FDSLNDKCKK
     ELEAIGRQYP FEPLRYFRGD KKTLRLTFEE GVQMLKEAGI EVDPFGDLNT ESERKLGQLV
     AKKYGTEFYI LHKYPLAVRP FYTMPCYDNP AYSNSFDVFI RGEEIISGAQ RVHVPEFLAK
     RAEECGIDVK TISTYIDSFR YGAPPHGGFG VGLERVVMLF CALNNIRKTS LFPRDPQRIA
     P
//
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