ID   G0NRK6_CAEBE            Unreviewed;       440 AA.
AC   G0NRK6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=CBN-NFT-1 protein {ECO:0000313|EMBL:EGT36222.1};
GN   Name=Cbn-nft-1 {ECO:0000313|EMBL:EGT36222.1};
GN   ORFNames=CAEBREN_19061 {ECO:0000313|EMBL:EGT36222.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL379932; EGT36222.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0NRK6; -.
DR   STRING; 135651.G0NRK6; -.
DR   EnsemblMetazoa; CBN19061.1; CBN19061.1; WBGene00157786.
DR   eggNOG; KOG0807; Eukaryota.
DR   eggNOG; KOG3379; Eukaryota.
DR   HOGENOM; CLU_030130_12_1_1; -.
DR   InParanoid; G0NRK6; -.
DR   OMA; GWHNKKR; -.
DR   Proteomes; UP000008068; 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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd01275; FHIT; 1.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR   Gene3D; 3.30.428.10; HIT-like; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR039383; FHIT.
DR   InterPro; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR001310; Histidine_triad_HIT.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   PANTHER; PTHR23088:SF27; DEAMINATED GLUTATHIONE AMIDASE; 1.
DR   PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF01230; HIT; 1.
DR   PRINTS; PR00332; HISTRIAD.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT   DOMAIN          14..264
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   DOMAIN          297..405
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   MOTIF           390..394
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601310-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        392
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601310-1"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         385..388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   SITE            409
FT                   /note="Important for induction of apoptosis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ   SEQUENCE   440 AA;  50003 MW;  961ABE6941BD6839 CRC64;
     MLTTVFRRTM ATGRHFIAVC QMTSDNDLEK NFQTAKNMIE RAGEKKCEMV FLPECFDFIG
     INKNEQVDLA MTADCEYMQR YRDLAKKHNV WLSLGGLHHK DPNDLAHPWN THLIIDSEGE
     TRTEYNKLHL FDLEIPGKVR LMESEFSKAG KGMIPPVDTP VGRLGLSICY DVRFAELSLW
     NRKRGAQLLS FPSAFTLNTG LAHWETLLRA RAIETQCYVI AAAQTGAHNP KRQSYGHAMV
     VDPWGAVVAQ CSERVDMCFA EIDLSYVDSL REMQPVFSHR RSDLYTLHVN ERTSETTDLK
     FAEFNVPVSH VFYSTPHSFA FVNLKPVTDG HVLICPKRVV QHLTDLTDSE TADLFIVAKK
     VQAMLENHHN VKASTICVQD GKEAGQTVPH VHVHILARRS GDFGDNEIYQ KLASHDKEPE
     RKPRSSEQMA EEAAVYRKLM
//