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
//