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Database: UniProt
Entry: M1WCX9_CLAP2
LinkDB: M1WCX9_CLAP2
Original site: M1WCX9_CLAP2 
ID   M1WCX9_CLAP2            Unreviewed;       553 AA.
AC   M1WCX9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE            EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN   ORFNames=CPUR_05733 {ECO:0000313|EMBL:CCE31878.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE31878.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE31878.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE31878.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE31878.1}.
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DR   EMBL; CAGA01000035; CCE31878.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1WCX9; -.
DR   STRING; 1111077.M1WCX9; -.
DR   VEuPathDB; FungiDB:CPUR_05733; -.
DR   eggNOG; KOG0554; Eukaryota.
DR   HOGENOM; CLU_004553_2_0_1; -.
DR   OrthoDB; 2786597at2759; -.
DR   PhylomeDB; M1WCX9; -.
DR   Proteomes; UP000016801; 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; cd00776; AsxRS_core; 1.
DR   CDD; cd04318; EcAsnRS_like_N; 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; 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:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 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   ECO:0000313|EMBL:CCE31878.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801}.
FT   DOMAIN          203..543
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          109..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  62144 MW;  834891555CB5D6DD CRC64;
     MARPTLVSHA VPTLRLPRAA GQYKRTYSVR INGQQPPSQA IRTVADLKAW RPATNVPDVE
     VCGWVRSVRK SPGVRFVDIT DGSCMRPMQA VVDKALATDI RPGAAVRVKG TWHSTADRQK
     DAADESPVSG HSHSHQQATH EYSGMSLDAL GSQTLRELRV EAVDILGSSD HQSNPIQNKY
     QTPESLRLVS HLRCRTPLNS TLLRLRSDAI ASLTNFFFKE GFQQTHPPII TSSDCEGAGE
     AFTVKTGSKE EFFKQTKYLT VSSQLHLEAL AQSLGNVWTL SPTFRAEKSD TSRHLSEFYM
     LEAEMEFVKD MDEVMDLVQK MLMSLATSLK ELRAANELEK NRLDARDPAE KGAFADLVER
     QELQRRWAGL SSPNRWPKIT YSDAMERLQP IADQFEHKPV WGSGLQSEHE KYLAKEIGYD
     KATDAYVPVF VTQYPRKIKA FYMHRSASPP PQGETVDCFD LLVPDLGELA GGSMREHRLS
     ELEHNMTLHG LEVPTKKQDR GNGLGWYLDL RRWGCPPHGG FGLGFDRLLS YLSGVPNIRD
     VVPFPRHHQR CQC
//
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