ID A0A2C5YQ83_9HYPO Unreviewed; 982 AA.
AC A0A2C5YQ83;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN ORFNames=CDD80_6566 {ECO:0000313|EMBL:PHH69680.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH69680.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH69680.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH69680.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PHH69680.1}.
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DR EMBL; NJES01000727; PHH69680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5YQ83; -.
DR STRING; 2004952.A0A2C5YQ83; -.
DR OrthoDB; 347413at2759; -.
DR Proteomes; UP000226431; 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.
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:UP000226431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..982
FT /note="asparagine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012180338"
FT DOMAIN 677..974
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 982 AA; 108339 MW; 5E431767B05EFD63 CRC64;
MKSAVALVGL LASSVCSAHG ADDHGGPWSK EALAELEAKW GYEWGFSGIG SFAHLDHVKC
LVDPSVQFDI AVIGVPFDTA VSFRPGARFG PRAIRHSSAR QTAFRGFNPR AGINPYQDWA
KIIDCGDMPI TPFDNQIALE QMTQAFRELG KRKASKTSNP RPRLVTLGGD HSLALPALRA
LKEIYGRPVR VLHFDAHLDT WDPYSYPAAW GATQFTHGSM FWMASQEGLL SNSSSSPSVH
AGLRTRLSGT SWADNESDGS QNWVRFSADD MDEKGTSGII DGIVKTLGTE DPVYLSVDID
VLDPAFAPGT GTPEPGGWTT RELIRVLRGI EGLNLVGADV VEVSPAYQGR GEETALAAAQ
VVYEMVTSMV KRGSKGQAVV RDELTPLEPE FRYIFSEMAA VQELAERIRS DDSVYVDTDA
GVDDGTADGS QGKPFKSLAF AYIQNIDRPG VTYLTRASVT GSEEDAAARM AWKAPAKSAV
KKAQGAVDVH KKKLAKQQQV QASEDAKKQQ RLGNLEASKK IIIREDPSLP KAVKMNIGDK
TVALGDGDGV KGARVKVSGR IHRLRVQKQA TFITLVDGRG HLQCVLQAGD LTKTYDALLF
AQGTSLTLHG EMRKVPDGQT APDGRELHVD YYTVIGTSPG DEEAITNKVS STQNQWDQLM
LDNRHLVLRG DNASAVMKLR ASVEWAFIKA YHDMGFVKVS PPALVQTQVE GGATLFNVPY
YDELAYLTQS SQLYLETVLP SLGNVYCIEK SFRAEKSLTR RHLSEYTHVE AELDFIEFGE
MLEHIEEVIC RVVDSVLEDA EMARLLKELN PGFDRPSRPF LRMKYSDAID WLNKQDPPIL
NEEGNTHVFG DDIAEAAERK MTDIINRPIF LTHFPVEIKA FYMKKDPSDV RVTESVDCLM
PGVGEIVGGS MRMEGYDELL AAYEKQGIPA KDYYWYTDQR KYGTSPHGGY GLGLERFLAW
MANQHTVRTT CLYPRFMGRC KP
//
