ID A0A139HVC0_9PEZI Unreviewed; 1011 AA.
AC A0A139HVC0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=AC578_6006 {ECO:0000313|EMBL:KXT06398.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT06398.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT06398.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT06398.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXT06398.1}.
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DR EMBL; LFZN01000006; KXT06397.1; -; Genomic_DNA.
DR EMBL; LFZN01000006; KXT06398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HVC0; -.
DR STRING; 321146.A0A139HVC0; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000070133; 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:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid 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 CDD; cd22249; UDM1_RNF168_RNF169-like; 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; IPR024320; LPG_synthase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF2; ASPARTATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09924; LPG_synthase_C; 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 Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT DOMAIN 342..645
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 113853 MW; 32BB4A436E0DCA76 CRC64;
MSLKKALHSI RPRSDSNSAA TSDNESKSQS PARGNHEGRS RTGFASLSNG IGLRRHSPDS
TRDNIGSPTS PSPSRGSKEL TRSHSPLNFL RKKIRPPSDD SHSSTEDLPL NRDGESLSRN
QQRKHERQAE KEKHRKEAEE RLEADRKRKE HMERKAAEEE TEEQKAKYGT LPINYYAGQQ
KHLNRMDIRE LTPEHIGKMV CFRARIHNMR KLSAHLMFVE LRQQTATIQG ILHEHGSVSQ
HFLYWAEHLH VETVVLVQGV VQEPKSKQGE IIGVSIHNLE VHIHEMHVEA TPSEPLAFTV
HEAEVSKADT EKEGDTRHRV SDRARQNNRV IDLRTTTSQG IFRIQSGVCQ AFRAHLHSIG
FIEIHTPKLQ GAASESGASV FKVDYFGRPA FLAQSPQLGK QMAIAADFRR VFEIGPVFRA
ENSNTHRHLT EFTGLDLEMA IDEHYHEVLR VLDSTFKAIF KYVYDNYKDD IKVVKHQFPH
DDLVWLDETP VIPFAEAIRL LNASGYRDEN GNEIPENEDM GTRDEIALGA VIKEKYKTDY
YVIDKFPTSA RPFYAMPDPY NPDVTNSFDI FLRGQEILSG GQRIHDAPTL VKKMEALKMD
PRSLEEYMTG FEWAAPPHGG GGIGMERILM LLLKLGDIRN ASLFPRDPKS LPYKPPVKQL
RHPEASTLHP PWSGQDRAAA HMDFQPIEKL IANYGDASNT SWLEPKFEHW RDPHTGAAVG
FVPHEGFAIT IGDPLCHQSQ YAKTIGGYLR YIKKDRRLKP LWLLCGSAAE EVLANKFDWR
TLSVAAEQRL DPNNNPAVQD PEIQRKCRHA EKEGVKVHDI PLGTAVPDDV KEKIDGRIQD
WLRNRKGKQV HLTDVRPWQD VEHRQYHYTT TKDGQICGLV ILAQLSPDHG WQVKFALDFP
GAPSGAIELL VLHALKAAGQ TGATSVTFGG GATAKLTPGH NLKGTRVKVL AKAYHAIATE
LKLTNKSEFR EKLGAQDDPI FVCYPPHGLG PAGVRAILSF FEDEDDTSKL G
//
