ID A0A367LGY8_9HYPO Unreviewed; 976 AA.
AC A0A367LGY8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN ORFNames=L249_7973 {ECO:0000313|EMBL:RCI13685.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI13685.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI13685.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI13685.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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:RCI13685.1}.
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DR EMBL; LKCN02000005; RCI13685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LGY8; -.
DR STRING; 1330021.A0A367LGY8; -.
DR Proteomes; UP000253664; 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:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion 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; cd11592; Agmatinase_PAH; 1.
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 Gene3D; 3.40.800.10; Ureohydrolase domain; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR NCBIfam; TIGR00457; asnS; 1.
DR PANTHER; PTHR22594:SF16; ASPARAGINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR Pfam; PF20917; AsnRS_N; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
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.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..976
FT /note="asparagine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016720105"
FT DOMAIN 671..968
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 976 AA; 106907 MW; 922DD8C411C1A5E4 CRC64;
MKSAAALAGL VAASACAAHG THDDDAGAWS KEALAELGAK WGYEWGFSGI GSFAHLDHVK
CLTDPSVDFD IAIIGAPFDT AVTFRPGARF GPRAIRQASA RQTAFRGFNP RAGFNPYQNW
AKIIDCGDIP ITPFDNQIAL EQMTQAFLEL GKRKPPPGSR ATNPKPRLVT LGGDHSLALP
ALRAIKEIYG RPVRVLHFDA HLDTWDPHSY PAAWGATQFT HGSMFWMANN EGLLTNSSSS
PSVHAGLRTR LSGDSWADND SDGAQGWVRF SADDMDDKGT AGIIEGIMKT LGTEDPVYLS
VDIDVLDPAF APGTGTPEPG GWTTRELIRV LRGIEGLNLV GADVVEVSPA YQGRGEETAL
AAAQVVYEMV TSMVKRGGIK DKAHAKDELQ TPPVQELAER TRPSGESVYV DADTGVDDAS
ADGSEAKPFK SLSFAFIQNI GRPDANYLTR ASVTGPDEDA SARLAWKAPA KSAVKKAQGA
VDAHKKKLAK QQQVQASEDA KKQQRLGNLE ASKKIVIKED PSLPKAVKMT IGDKSVALGD
GGGVKGTRVK VSGRIHRLRA QKQATFITLV DGRGHLQCVL QAGDLTKTYD ALLFAQGTSL
TLYGEMRKVP DGQTAPDGRE LHVDYYTVIG TSPGDEEAMT NKVSSAQNQW DQLMLDNRHL
VLRGDNASAV MKLRASVEWA FMTAYHDMGF VKVSPPALVQ TQVEGGATLF TVPYYDEVAY
LTQSSQLYLE TALPSLGNVY CIEKSFRAEK SLTRRHLSEY THVEAELDFI EFTDMLDHIE
EVICRVVDSV LDNAEMARLL KELNPSFVRP SRPFLRMKYV DAIDWLNKQD PPILNEEGNA
HAFGDDIAEA AERRMTDIIN RPIFLTHFPV EIKAFYMKKD PSDLRVTESV DCLMPGVGEI
VGGSMRMEGY DELLAAYEKQ GISAKDYYWY TDQRKYGTSP HGGYGLGLER FLAWMANQHT
VRTTCLYPRF MGRCKP
//
