ID A0A319ABP4_ASPLB Unreviewed; 950 AA.
AC A0A319ABP4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=BO96DRAFT_465191 {ECO:0000313|EMBL:PYH57569.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH57569.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH57569.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH57569.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KZ821346; PYH57569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319ABP4; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR006353; HAD-SF_hydro_IIA_CECR5.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR NCBIfam; TIGR01456; CECR5; 1.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56784; HAD-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:0000313|EMBL:PYH57569.1};
KW Ligase {ECO:0000313|EMBL:PYH57569.1}.
FT DOMAIN 638..950
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 399..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 105479 MW; 8ECE71AD3E0DD164 CRC64;
MRSQSLWRSL ALLQSASTRS FVNTGSGRRA FQTANSRVPD FAFAFDIDGV LLRSSKPIPG
AAESLALLKE QNIPFLLLTN GGGKHETERV AEISEKLKVP LEPEVIVQSH SPFAELVRGP
DEQSALENKC VLVVGGEGDR CRQVAQMYGF KNVVTPGDIY MANPSIWPFR SFKSYYEKIS
KPLPNPKDPN DPSRGLKIDA IFVFNDPRDW ALDAQIITDI LLSSEGVIGT ISEKNGRTDL
PNRGFQQDGQ PHLYFSNPDL WWAAAYHLPR LGQGGFREAL EGIWAAVTGG PAKGVELKKT
IIGKPYQETY EFAEHQLLRN RARVFGSDAQ QPLRNVYMIG DNPESDIRGA NSYRSEHGSK
WHSILVRTGV YNGGEPAWTP TTIADNVHKA VEWALKNSQW RAPEETPAAA AAPAEGAETS
KSASKNAAKK AAKEKAKAEK AAARAAQEKA QAAAAAADDT AKDLYGKLPE SEDVIAATRF
SDISDEHYEK EVTLVARVDN ARVQSAKLAF LMLRQQGQKL QAVIALAEPI SRQMIKYTGG
LNVNSIVQVT GIIKKPAVPI SSATLSNHEI HIRKVYMISE AAQMLPMQVK DAERPPPETS
EEGFEVGEDG APIVTLKTRL DNRVLDLQTE TSQAITWISS GVAELFAEYM IKSGSRWIFT
PKLVGAATEG GSNVFEVKYF KKNAYLAQSP QLYKQMCIAG DMESVFEIAP VFRAEDSNTH
RHLTEFAGLD FEKTFRGHYH EVLEFAENLL VFILSQLKER YADKIAIIQK SYPKAGDFKL
PKDGKALRLN YMDGVAMLKE AGVDVSEQER FENDFTTAME KQLGQIIRDK YDTDFYVLDK
FPMAVRPFYT KACPQDPRFS NSYDFFMRGE EIMSGAQRIN DIKELEESMV AKGLNPNQEG
FEDYLSAFRQ GCPPHAGGGL GLNRIVMFFL GLPNVRLASL FPRDPQRLRP
//
