ID C4JW42_UNCRE Unreviewed; 938 AA.
AC C4JW42;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=UREG_06784 {ECO:0000313|EMBL:EEP81919.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP81919.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
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; CH476618; EEP81919.1; -; Genomic_DNA.
DR RefSeq; XP_002583817.1; XM_002583771.1.
DR AlphaFoldDB; C4JW42; -.
DR STRING; 336963.C4JW42; -.
DR GeneID; 8442972; -.
DR KEGG; ure:UREG_06784; -.
DR VEuPathDB; FungiDB:UREG_06784; -.
DR eggNOG; KOG0556; Eukaryota.
DR HOGENOM; CLU_004553_1_1_1; -.
DR InParanoid; C4JW42; -.
DR OMA; KYSLDFP; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000002058; 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 Reference proteome {ECO:0000313|Proteomes:UP000002058}.
FT DOMAIN 272..582
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 37..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 106997 MW; A6FEAD61F61E808E CRC64;
MSIKHALSKI KNVSLSDTEL VPPRKSISQF VHGREFVYSS DDTSDDSENM SRKELRREAR
RKAKSQSRSR LSEDSSVDLV KKKERDEQAA KEETEEMRAR YGDLPLMQSR SRTRQNLTKF
ESIRSDMDGQ EITFRARLHV VRRMGQKLVF LVFRQQVITL QGVLTEAKGE ISTLMVQWAE
HIRVGSILRV KGILRKPEVP VIGTTIHDIE LHIRELHVIV RREEPVPFSV YEAELPAADE
EKIEGRRTRV PDRTRLTNRI LDLRTDTSQS IFRIQSAISS YFRSTLDANG FIEIHTPKLQ
GSATESGASV FNVNYFSRPA FLAQSPQLAK QMAIASDFER VYEIGAVFRA ENSNTHRHLT
EYTGLDMEMV IEEHYHESLD VLDQVIKAIF TAIYDRHRRE VQIIKHQFPS EDLLWLDQTP
IITFSEGIKM LNESGWRTED GKEFSDQEDI GTRDEIRLGE LIKEKYHTDY YIMDKFPAAA
RPFYAMPDPD DSRFTNSYDI FVRGQEIVSG GQRIHDPVML EERMKKMGID PASMEEYMEG
FRWGAPPHAG AGIGLERMLM LILKLGNIRL ASLFHRDPKS FPAQDQPVLL RHPDASTLDP
PWEDDSKSEK VKETSDRKLQ DLADLIANYG DATSTSWFDD RFQVWRDAAT GAAVSYVPAH
GYAIIAGNPL CDSSQYPRIV TQFLRWLKKE TKLKPIWILC SVEVENILGE RLGWRSLSCV
AEERVDPARN QAASDGEIAR KIRQAENNGV KVTTLRFGQT VPENVQRKID ARIQDWLSNR
KGTQIHLSQI TPWRDQRHRQ YFYATDRDGK ICSFVALTQL SPRNGMQVKY SLDFPGSPSG
SIEYIVTHAI QTAAKSGVKS LTFGGGATAH LTPGHNLSSA KAKVLSTTYD AIVKQFKLNR
KTEFRAKLGA HEEPVYIAYP KRGLGTRGIR AILSFFED
//
