ID   A6R4Z7_AJECN            Unreviewed;       973 AA.
AC   A6R4Z7;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE            EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN   ORFNames=HCAG_04705 {ECO:0000313|EMBL:EDN08195.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN08195.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476658; EDN08195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6R4Z7; -.
DR   STRING; 339724.A6R4Z7; -.
DR   VEuPathDB; FungiDB:HCAG_04705; -.
DR   HOGENOM; CLU_004553_1_1_1; -.
DR   OMA; KYSLDFP; -.
DR   OrthoDB; 382728at2759; -.
DR   Proteomes; UP000009297; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT   DOMAIN          305..626
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   973 AA;  110556 MW;  1678FB4078D43F32 CRC64;
     MTGSSQAVPI VEQGAGKQNE RHQRSLSLNV AIKTALTRLK DTTRPNSDNE SPSSPRKSLA
     SFFLDRDVVS SSEDLPSDDS DFMSKKQQNR HERKLKRESR ARISGEISER SESLKRERDA
     QAAREETDEM KARYGDLPLM QSKQRPRQNL IKFDNITPHS IGQEVTFRAR VHHIRNMSSK
     LVFVIFRQQV TTMQGVLAEK PGMISTLMVQ WVERIRVGSI VKVRGVLSSS KVPVTGCTIH
     DVELDIQELH VVVHREDPIP FSVYEAELLN KDAKNTDGRR NHVLDRTRLS NRILDLRTDT
     SQSIFRIQSA ISNLFRASLD SQGFIEIHTP KLQSSATESG ASVFEVKYFT REAFLAQSPQ
     LAKQMAIAAD FERVYEIGAV FRAENSNTHR HLTEYTGLDI EMAIEEHYHE ALETIDSVLK
     EIFKGIYGRY RREVDIIKNQ FPHEDLVWLD ETPIIPFAEG IKLLNDSGWR QDGEELSVNE
     DLGTRDEIRL GELIKEKYHT DLLPYWDKFP KSARAHFMPW KILRTPDFTN SFDIFVRGQE
     IVSGGQRIHD EKILEQRMKE AGINPLAMEE YLEGFRWGAP PHAGAGIGLE RLLMLILKLG
     NIRLASLFHR DPKSFQDMPD TSRIIPYPES STLEPPWEKK GNQKHTGIDK NRNFQPLDEL
     IANYGDATST SWPDEKYKIW RDYTSGAAIA YVPSTHGFAI IPGNPLCDPS QYAKVSIRFL
     RWLKAETHLK PIWILCSRPV EEILGEKLGW RTLSCVGEAR IDPSRNQAAA DADISKKIRQ
     AEREGVKVHH IPSDRPLPED ITSRIDARIK EWRENRKGPQ IYLSGIKPWR SPRNYQYYYA
     ADKNGTICSF VALARLGANH MQIKYSLDFP GAPSGSIEYL ITHAIQATGR SGVKSLTFGA
     GAASNLIPGH NMSSAKGKVL QTTYDTLVKQ FGLNRKTEFR AKLGAFEEPL FIAYPRHGMG
     SKGIRAILNF FED
//