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Database: UniProt
Entry: A0A150VH90_9PEZI
LinkDB: A0A150VH90_9PEZI
Original site: A0A150VH90_9PEZI 
ID   A0A150VH90_9PEZI        Unreviewed;       572 AA.
AC   A0A150VH90;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE            EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
DE   AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029886};
GN   ORFNames=M433DRAFT_149584 {ECO:0000313|EMBL:KYG49831.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49831.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG49831.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG49831.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC         asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC         Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00000422};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYG49831.1}.
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DR   EMBL; JPDO01000015; KYG49831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VH90; -.
DR   STRING; 766039.A0A150VH90; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd04323; AsnRS_cyto_like_N; 1.
DR   CDD; cd00776; AsxRS_core; 1.
DR   Gene3D; 3.30.1910.20; asparaginyl-tRNA synthetase, N-terminal domain; 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; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR048952; AsnRS_N.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00457; asnS; 1.
DR   PANTHER; PTHR22594:SF16; ASPARAGINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF20917; AsnRS_N; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 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   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   DOMAIN          269..564
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          74..108
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   572 AA;  64647 MW;  FC66A6D2F75C072E CRC64;
     MPDIFIDEGQ GRDSADADGS QSSAYKSLQY AVFQHGADAE YYVKNEEKGE GQPEWKPAAK
     AAKKKAVNYA EQQRKKAAKE QEVALRQKKE QEERERALEE AKKVVVREDP SLPKAVRITL
     DETRPHIVKL GSGTRPKDLD YAAEGRGTRV RVFGRVHRER KQGAYIFLTL RDGKGYLQCI
     LSGDLARTYD ALTLAREASV MVTGEMWSVP PGNTAPGGRE LHADYFEVIG RGPGGDDAIT
     NKVQAKGDAQ TLLDQRHLVI RGENAAAVLK VRSAVDKAFR DVYERLDFKQ VSPPALVQTM
     VEGGATLFKF DYYGEPAFLT QSSQLYLETC LPSLGDVYCI EKSFRAEKSL TRRHLAEYTH
     IEAELDFISF DDLLVHLEDL ICGVLELVLS KPTVAALLRD LNPDFQMPER PFKRMRYAEA
     IDWLREHDIP NEDGQPHTFG DDIAEAAERR MTDMINRPIF LTHFPVEIKA FYMQKDAADP
     RVTESVDCLM PGVGEIVGGS MRMNDYDELM AAYARVGIDP KDYYWYTDQR KYGTSPHGGY
     GLGLERFLAW LCKQHTVRDT CLYPRYMGRC KP
//
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