ID C6H6Z8_AJECH Unreviewed; 1008 AA.
AC C6H6Z8;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=HCDG_02199 {ECO:0000313|EMBL:EER44169.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER44169.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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; GG692420; EER44169.1; -; Genomic_DNA.
DR AlphaFoldDB; C6H6Z8; -.
DR STRING; 544712.C6H6Z8; -.
DR VEuPathDB; FungiDB:HCDG_02199; -.
DR HOGENOM; CLU_004553_2_5_1; -.
DR OMA; AQLFMEY; -.
DR Proteomes; UP000002624; 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:EER44169.1};
KW Ligase {ECO:0000313|EMBL:EER44169.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT DOMAIN 696..1008
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 456..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 112281 MW; 7A92B8CB21297DA1 CRC64;
MRLSTLHQPL RQSFYGCQAS SIRKQFSSSV SSQRVTPNFG FAFDIDGVLL RSSRPLPGAA
ESLQLLKRER IPFVLVTNGG GMHEKERIAQ LSQRLHVALD TDMIIQSHTP FADLVKGNEA
QEALQDKCVL VVGGGNGKCR SVAQEYGFKS VVTPGDIFQS HPEIWPFSDA FSDYYGRFAS
QLPRQIDAAD PSKSLKIDAI LVFNDPRDWA LDIQIIIDIL LSSQGIIGTY SSKNNNPDLP
NRGYQQDGQP PLYFSNPDLL WAAQYHQPRL GQGAFKASLE GVWAAMTGGA TLAKTVIGKP
CELTFRFAEK RLNQEREKLF PAENLRPLEV VYMIGDNPES DIQGANSYKS PVGTKWNSIL
LKSGVYSGGT PTWPSKVIVE GVKQAVEWSL AQSQWPRLRA AKFFHLVGWW RHSDSPPSAP
EKGDQQPQLL PLTIRTPNCQ LPLKVLLKEI MEQNPTLPVR SKDDGDVPEN SLGSQPPAGD
PAPPSKSALK KAAKEREKAE KAAKRAAQEQ AAAQASQAAD FSKHLYGPIP DSADKVQVLN
LLDLSEELCE KDVTVVARVD NARVQSAKLA FLMLRQQGKK MQAVVSASDE ISRPMVKWIG
GINVNSIVKV TAIVKKAEIP VTSATVKHLE LHIRKVYMVA QASHMLPMQV KDAERPPPES
VTEEVESEAP YVTLKTRLDN RVLDLQTEAS QAITWISSGV AQLFMEYMLK SGSRWISTPK
LTANASEGGA GVFEVTYFKR KAYLAQSPQL YKQMCIAGDM ESVFEIGPVF RAEESNTHRH
LTEFVGLDFE KTFQSHYHEV LEFAEDLLVF ILSELKIRFK KEIEVIQRSY PKAGDFRLPK
DGKALRLKYM EGVALLKEAG VDVTEQERFE NDLSTAMEKQ LGRIIREKYD TDFYVLDKFP
MAVRPFYTKP CPDDPTFSNS YDFFMRGEEI MSGAQRINEA KELEAAMSAK GIDPNAEGFE
DYIGAFRQGC PPHAGGGLGL NRIVMFFLGL PNIRLATLFP RDPQRLRP
//
