ID A0A178BFC1_9PLEO Unreviewed; 1042 AA.
AC A0A178BFC1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=IQ06DRAFT_289281 {ECO:0000313|EMBL:OAL07578.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL07578.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL07578.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL07578.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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; KV441705; OAL07578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178BFC1; -.
DR STRING; 765868.A0A178BFC1; -.
DR InParanoid; A0A178BFC1; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000077206; 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; 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 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 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 Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:OAL07578.1};
KW Ligase {ECO:0000313|EMBL:OAL07578.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 377..680
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 117159 MW; F5DC2D8432064549 CRC64;
MSLKKALNKL KTGHSSNPAS DDESKKTPTT STTTSTNDLR SQSPGATPRS SGVFAHRPSG
DFKRGDAASP TESRSSIDQP RHSLTGLLTR RTESPNRSGS KGGNHHRSGS THSPIRAVKE
KLHIGGDNSS SDDDRPLNRD GEPMSKNQLR KAEKQAQQEE RFKQNMEKEK LLEQRRKEMD
EQANAELTPE QKAKYGAIHP NAYAGEWKHE PRMKIQDFSA RDVGKEVVFR ARIHHLRKMS
SKFVFFMFRQ QLATIQGVLM EHADISKYML YWAEHLDAET VVLVRGILQE PKAKQGEVLG
ATIHDVEVSV HALHVEAAVT ENLPFNVNEA EVSQADVDSE IAKADHKDGH NRVKISDRTR
LNNRVIDLRT TASQGIFRIQ SGICNLFRTQ LDSEGFIEIH TPKLQGGATE SGASVFKIDY
FGRGAFLAQS PQLAKQMAIS ADFGKVYEIG AVFRAENSNT YRHLTEYTGL DLEMQIDEHY
HEVLRVLDRT FKAIFKGIYE RYRPEIEIIK KHFPHEDLVW LDETPILPFA EAVRMLNDSG
WRDDNGNPLD ENEDLGTRDE VQLGRVIKQK LGTDYYILDK FPVSARPFYA MPDPNNPEVT
NSFDIFCRGQ EILSGGQRIH DSNMLLEKMR KLKVDPTTME EYIQGFQWGA PPHGGGGIGL
ERILMLMMSL GNIRHASMFP RDPKSLPEKP VIKQLRHPEA STMHPPWEGQ DRVMAKIDLQ
PVEKLIANYG DATNTSWLEP RTEIWRDDQT GAAVGFVPQD GFAITVGDPL CHPSQYLKIM
TSYLKYIKKE RNLKPLWLLV GGPVEETLAT KFNWRTFSVT GEQRVDPVHN PAEKDSDVQR
KIRHAEKEGV KITDYALGSP PPPEVKQKVD ARVEDWLKNR KGKQVHLTNI HPWQDEEHRQ
YHIAYTSDGT IAAFVAMAQL SPDHGWQVKY SLDFPGAPGG SIEYIVTHAL KMVGAAGATT
VTFGGGASSK FTPGHNVKGT RVKVLSRAYH AISTELKLTN KTEFREKLGA IDDPSYICYP
PHGLGPMAVK AILNFFSDED DN
//
