ID A0A3P6T7F8_LITSI Unreviewed; 425 AA.
AC A0A3P6T7F8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 03-MAY-2023, entry version 15.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:VDK79219.1};
GN ORFNames=NLS_LOCUS4417 {ECO:0000313|EMBL:VDK79219.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK79219.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK79219.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UYRX01000282; VDK79219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6T7F8; -.
DR STRING; 42156.A0A3P6T7F8; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-EC.
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; 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 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:UP000277928}.
FT DOMAIN 6..255
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT DOMAIN 290..397
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT MOTIF 382..386
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 384
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 377..380
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 403
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 425 AA; 48215 MW; 9F581ED7191430E6 CRC64;
MNEVRSLIAV CQLTSTNDLE ANFKVAERMM KHAKERNAKM VFFPECFDYV GENRHESATL
ALTEDGDYIG RYRNCAREYG LWLSLGGFHQ KDPAGLQKPF NTHLIIDDGG KTRGMYRKLH
LFDIDIPGKV RLIESEFSSR GDEILKPVCT PVGNVAMSIC YDLRFAELAL WYRMNGAHIL
TYPAAFTVNT GLAHWETLLR ARAVETQCYV IAAAQTGKHN DKRSSYGHSM VVDPWGTVVA
QCSETIDMCF AEIGLNYLDE IRKLQPVFDH RRSDLYSLIA VQKNEIGNKA YTFGNQSIPP
EHVFYRSTYT FCFVNRNPVL PGHVLLCPIR NVKRLAKLSH AETSDLFITA KRVQAMLEDY
HKVASSTVCV QDGPEAGQTV SHVHVHILPR KKDDFGGDAN NIYRELAEDD KITKRKFRKK
PSDNV
//