ID A0A091TUY7_PHALP Unreviewed; 352 AA.
AC A0A091TUY7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Arylacetamide deacetylase-like 4 {ECO:0000313|EMBL:KFQ82184.1};
DE Flags: Fragment;
GN ORFNames=N335_00832 {ECO:0000313|EMBL:KFQ82184.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ82184.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ82184.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ82184.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00010515}.
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DR EMBL; KK466581; KFQ82184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091TUY7; -.
DR ESTHER; aptfo-a0a087ql14; Arylacetamide_deacetylase.
DR PhylomeDB; A0A091TUY7; -.
DR Proteomes; UP000053638; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR017157; Arylacetamide_deacetylase.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF32; ALPHA_BETA HYDROLASE FOLD-3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053638}.
FT DOMAIN 60..207
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 248..325
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT ACT_SITE 322
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ82184.1"
FT NON_TER 352
FT /evidence="ECO:0000313|EMBL:KFQ82184.1"
SQ SEQUENCE 352 AA; 40036 MW; BF6406053DC6202D CRC64;
QGKILEKTGL CSQITFGRYV RQGRKLGVDP KLFIQDLQFN KVSVRVYQPK ATSDGRRRGI
IFFHGGGWVF GSLDTYEKVC RYISRESESV VVSVQYRLAP EHKYPAAYED CLNATIHFMK
NTEHYGVDPD NVIVCGDSAG GNLAAAVSQT LAGRSDLPRL RAQILIYPGL QALDFNLPSY
HQNRGVPLLF RERAAFFALQ YLNGDALHMQ EVLEGSHIPP DMKLKYRKWV SPDNIPEKFK
VRGVKPLRRT DFIAEVYETV KRFCEPNLCP LLAEDAIVHQ LPESFILTCE YDVLRDDGLL
YKKRLEDNGV RVTWYHLEDG FHGVISLYDY CGFSFPAGKR GLDSVVNFLK SL
//
