ID F0U7C3_AJEC8 Unreviewed; 994 AA.
AC F0U7C3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=HCEG_01752 {ECO:0000313|EMBL:EGC42390.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) 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; DS990636; EGC42390.1; -; Genomic_DNA.
DR AlphaFoldDB; F0U7C3; -.
DR STRING; 544711.F0U7C3; -.
DR VEuPathDB; FungiDB:I7I53_06466; -.
DR VEuPathDB; FungiDB:I7I53_06467; -.
DR HOGENOM; CLU_004553_2_5_1; -.
DR OMA; AQLFMEY; -.
DR Proteomes; UP000008142; 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:EGC42390.1};
KW Ligase {ECO:0000313|EMBL:EGC42390.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT DOMAIN 682..994
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 443..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 110552 MW; 270D4284EE35CAA5 CRC64;
MRLSTLHQPL RQSFYGCQAS SIRKQFSSSV SSQRVTPNFG FAFDIDGVLL RSSRPLPGAA
ESLQLLKRER IPFVLVTNGG GMHEKERIAQ LSQRLHVALD TDMIIQSHTP FADLVKGNEA
QEALQDKCVL VVGGGNGKCR SVAQEYGFRS VVTPGDIFQS HPEIWPFSDA FSDYYGRFAS
QLPRQIDAAD PSKSLKIDAI LVFNDPRDWA LDIQIIIDIL LSSQGIIGTY SSKNNNPDLP
NRGYQQDGQP PLYFSNPDLL WAAQYHQPRL GQGAFKASLE GVWAAMTGGA TLAKTVIGKP
CELTFRFAEK RLNQEREKLF PAENLRPLEV VYMIGDNPES DIQGANSYKS PVGTKWNSIL
LKSGVYSGGT PTWPPKVIVE GVGLRAAKFF HLVGWWRHSD SPPSAPEKGD QQPQLLPLTI
RTPNCQLPLK ALLKEIMEQN PTLPVRSKDD GDVPENSLGS QPPAGDPAPP SKSALKKAAK
EREKAEKAAK RAAQEQAAAQ ASQAADFSKH LYGPIPDSAD KVQVLNLLDL SEELCEKDVT
VVARVDNARV QSAKLAFLML RQQGKKMQAV VSASDEISRP MVKWIGGINV NSIVKVTAIV
KKAEIPVTSA TVKHLELHIR KVYMVAQASH MLPMQVKDAE RPPPESVTEE VESEAPYVTL
KTRLDNRVLD LQTEASQAIT WISSGVAQLF MEYMLKSGSR WISTPKLTAN ASEGGAGVFE
VTYFKRKAYL AQSPQLYKQM CIAGDMESVF EIGPVFRAEE SNTHRHLTEF VGLDFEKTFQ
SHYHEVLEFA EDLLVFILSE LKIRFKKEIE VIQRSYPKAG DFRLPKDGKA LRLKYMEGVA
LLKEAGVDVT EQERFENDLS TAMEKQLGRI IREKYDTDFY VLDKFPMAVR PFYTKPCPDD
PTFSNSYDFF MRGEEIMSGA QRINEAKELE AAMSAKGIDP NAEGFEDYIG AFRQGCPPHA
GGGLGLNRIV MFFLGLPNIR LATLFPRDPQ RLRP
//
