ID A0A0B2UU51_TOXCA Unreviewed; 598 AA.
AC A0A0B2UU51;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Fatty-acid amide hydrolase 1 {ECO:0000313|EMBL:KHN72390.1};
GN Name=Faah {ECO:0000313|EMBL:KHN72390.1};
GN ORFNames=Tcan_04598 {ECO:0000313|EMBL:KHN72390.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN72390.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN72390.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN72390.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
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:KHN72390.1}.
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DR EMBL; JPKZ01003255; KHN72390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2UU51; -.
DR STRING; 6265.A0A0B2UU51; -.
DR OMA; LPNCEEM; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR45847; FATTY ACID AMIDE HYDROLASE; 1.
DR PANTHER; PTHR45847:SF1; MONOGLYCERIDE LIPASE FAAH-4; 1.
DR Pfam; PF01425; Amidase; 1.
DR PIRSF; PIRSF001221; Amidase_fungi; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KHN72390.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..580
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 231
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 255
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
SQ SEQUENCE 598 AA; 66498 MW; 021AFA5661284716 CRC64;
MLVRFLSESG PFTTLGVTIT ITWSLVVVYV ILKLVVEKAW GATRISRHNI AKNEQSRQKR
FKAIRERIDE NAASAQRRAT IVHMSFFELK EALQKDEVSA TEALDAYVWK AFDVHQKTNA
IIEFIDEAFE QARHLDERWR GKHDKPPLFG LPFSVKGNFF VKGYDCSIGL AKNLFEPKQS
ECTLVTHLRD QGAVPFVLTN VPQALLSFVC SNPVYGTTTH PNDSKRTPGG SSGGEAALLA
CGGCVFGTGS DLAGSLRIPA SMCGVVTLKP TEARLVVENA HGGLPGKARL GLGYGFLTKS
VDDLKFLLGN VVGSVSYWKL VPKSVPLPLA TNRIDELRKK KLRIGYFFDD GFMKPVPACE
RGVRETVDKL RKAGHELVLF HVPHPNHAAS LFYKNILPDR GEYTQQLYGN EVITPYLKRF
VMMLKIPGCV RTVGSWLLRS ISPQLSLVMR SYVSDLGDLR YTQQLTDEYV KNFTREWKIF
ELDALVCPAF AVPSVPNEYP GELPMCAFAT GLFNMLDFPA GVVPTGIVTK QDDVLLEDEK
SWPVGHNIAL RRIREAARNS VGMPIGVQVV ALPFHEEECL AVMEMVEALY NGRFVSVS
//
