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Database: UniProt
Entry: A0A0V1A5L2_9BILA
LinkDB: A0A0V1A5L2_9BILA
Original site: A0A0V1A5L2_9BILA 
ID   A0A0V1A5L2_9BILA        Unreviewed;       702 AA.
AC   A0A0V1A5L2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Nitrilase and fragile histidine triad fusion protein NitFhit {ECO:0000313|EMBL:KRY19772.1};
GN   Name=nft-1 {ECO:0000313|EMBL:KRY19772.1};
GN   ORFNames=T12_12492 {ECO:0000313|EMBL:KRY19772.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19772.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY19772.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19772.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRY19772.1}.
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DR   EMBL; JYDQ01000032; KRY19772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1A5L2; -.
DR   STRING; 990121.A0A0V1A5L2; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR009688; FAM210A/B-like_dom.
DR   InterPro; IPR039383; FHIT.
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; PF06916; FAM210A-B_dom; 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; PS51084; HIT_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        104..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          270..520
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   DOMAIN          557..663
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   MOTIF           648..652
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        650
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT   BINDING         583
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         639
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         652
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   SITE            668
FT                   /note="Important for induction of apoptosis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ   SEQUENCE   702 AA;  80242 MW;  2612A2D156EC72CB CRC64;
     MALLRAVTSC SRSWRGLKLN FLRNYAFNRN PLLKFEKLVP WKYGSLSLSR NSRCTFSVSC
     IQYHRSLASL ESSKSNGSQS DKKADVDESK LTTYQKFKLT FKRYWYVLVP VHLITSSVWL
     GSFYYLAVSG VDLVGILESM GFSEQILNRL KQAPRAGNIA LAYAMFKIVT PLRYTATIGV
     TAVSVKYLVR MGLIKPAPSK EQVKRFVEQK RFQLRERYKV ESSKLKGKWK NISKISSKRN
     RLGSTAVSMI RFGLIKFQSS RIFYSSMPRS TVAICQTLST DDKQHNWKQC ESLIRLAKTK
     HAQMIFLPEC FDYVAASKSK TIELAEKENG VYINQYRMLA RELKVWLSLG GFHEKSEDSD
     VRVYNTHLII DDHGNTVTKY RKVHLFDVDI PGEKSIRESS YTIAGNNLQL PVQTPIGRLF
     VSTCYDIRFP ELACLARQFG AEVLCYPSAF TVSTGMAHWE VLVRSRAIDS QCFVIAAAQC
     GKHNDKRSSY GRAMVVDPWG TVLAQCSTNT PSLAVCDLDL DFENSVRKQF PTQNNRRTDL
     YQLLSRVSPF FDIDSISEYP FAEKRIPSSC VFYRSEHCYA FVNLKPVVEG HTLVSPLRPV
     QKLSQLNSYE IADLFNCVQL VESKLAKFYK TSSSTVCIQD GPEAGQTHLH VHILPRRRGD
     FEHNDEIYSV LDRHDKEVAE KSWRSLDEMN RESATYRELF NG
//
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