ID   G1XR15_ARTOA            Unreviewed;       284 AA.
AC   G1XR15;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=CN hydrolase domain-containing protein {ECO:0000259|PROSITE:PS50263};
GN   ORFNames=AOL_s00193g14 {ECO:0000313|EMBL:EGX44286.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX44286.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX44286.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX44286.1}.
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DR   EMBL; ADOT01000287; EGX44286.1; -; Genomic_DNA.
DR   RefSeq; XP_011126927.1; XM_011128625.1.
DR   AlphaFoldDB; G1XR15; -.
DR   STRING; 756982.G1XR15; -.
DR   GeneID; 22897944; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   HOGENOM; CLU_030130_1_0_1; -.
DR   InParanoid; G1XR15; -.
DR   OMA; QRQKIPY; -.
DR   OrthoDB; 1365844at2759; -.
DR   Proteomes; UP000008784; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   InterPro; IPR001110; UPF0012_CS.
DR   PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR   PANTHER; PTHR23088:SF30; OMEGA-AMIDASE NIT2; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS01227; UPF0012; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT   DOMAIN          8..258
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   284 AA;  31077 MW;  ED425FABE63637D8 CRC64;
     MSILKQPLKL ALVQLATSVD KSANLARART KVIEAANSGA NIVVLPECFN SPYGTDYFPQ
     YAESLSPPGS SQTFEILSAV AKETATYLIG GSIPEIDPAT SRLYNTSLVF SPKGDLLATH
     RKVHLFDIDI PGKIKFKESE VLSPGDKITI FETEYGKIGL GICYDIRFPE LAMTAARKDC
     FVMVYPGAFN MTTGPLHWSL LARSRAVDNQ IYVALCSPAR DLGATYHAWG HSMVVDPNGS
     ILEELEASEG IAIADLDNEK VDEIRKGIPV TKQRRFDVYK NVAD
//