ID A0A2J7Q5J7_9NEOP Unreviewed; 542 AA.
AC A0A2J7Q5J7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Fatty-acid amide hydrolase 2 {ECO:0000313|EMBL:PNF23845.1};
GN ORFNames=B7P43_G13733 {ECO:0000313|EMBL:PNF23845.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF23845.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF23845.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF23845.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) 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:PNF23845.1}.
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DR EMBL; NEVH01017557; PNF23845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7Q5J7; -.
DR STRING; 105785.A0A2J7Q5J7; -.
DR InParanoid; A0A2J7Q5J7; -.
DR OrthoDB; 146362at2759; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
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; PTHR43372; FATTY-ACID AMIDE HYDROLASE; 1.
DR PANTHER; PTHR43372:SF1; LD38433P; 1.
DR Pfam; PF01425; Amidase; 1.
DR PIRSF; PIRSF001221; Amidase_fungi; 2.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:PNF23845.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235965}.
FT DOMAIN 88..522
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 249
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
SQ SEQUENCE 542 AA; 60556 MW; DA1AB3B1D590C678 CRC64;
MALSEIGKER RESTHRPKEG SLRPFYKCIM SLWILIHSII DCIIDVFCSF FYDDSKRTQI
PGVKESFLME SAVSLAERIR HKEVSAEEVV QGFINRIHEV NSLINSVVDE RFEAALQEAR
DVDAFLASTK LTAEELKLQK PFLGVPFTTK DSTAVQGMRQ TLGLVSRQNV KAAEDADVVI
LLKKAGGILI AVTNIPEYNL WCESRNNVYG QTLNPYNTTR TVGGSSGGEA SIIATSGSPM
GIGTDIGGSI RMPAFYCGIF GHKPTTGLIS TKGLSKRTGQ EENTMVTAGP LCRYAQDLLP
FLQVMVGNNI SKLKLNAEVS LKDIQFFYME KSGDLRSSSV CEEMRLALRR AVSHFQDISK
SPVQKVKFSD MRYSFKLWRY WMTREPFDLA KELADGKGTV SVWKELLRKL LGQSDFTFAS
IMNLVNRYVL PQENSEWAES TTERLLSEIL EKLGDNGVLL YPSHPFPAVY HYSSLLRPYN
FGYWAVFNVL KLPVTQVPMG LNKDGLPLGI QVVAAPYNDH LCIAVARELQ KAFGGWGPPF
PV
//
