ID A0A0N7LB58_9BASI Unreviewed; 1392 AA.
AC A0A0N7LB58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Arylacetamide deacetylase {ECO:0000313|EMBL:CEH18466.1};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH18466.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH18466.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCYA01000270; CEH18466.1; -; Genomic_DNA.
DR STRING; 401625.A0A0N7LB58; -.
DR OrthoDB; 1381061at2759; -.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845}.
FT DOMAIN 515..698
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ SEQUENCE 1392 AA; 146998 MW; 413F7C24C3EFAF64 CRC64;
MSGNAAAPQE RGRPRSRISF SSPPPPQAHL AAASLDAQGT HTASAPPSPA SSVSSSTTIT
LGKPLPFVEE RAQTDSTGAL HATAGHSSDR VGSSKSSSTT PSSSSTLTSR SLAALSGAMS
LGLGSSVSST AGKGPKEDGL TTSSQSLAAS QKGKAPEGRP NNPRQRSKGQ MERRRVAVGV
SGSSNAIATT LQASPAIGSA FAASPLQSVG SRQRAPATIH GQTPAGPSHT AQRLGLESGQ
RGPRLSVRLP TSASPSVPPT SSSSSTRDTP RRSAEDEELK RQIRLALSSA GNDVPSLGAE
SRSAWSSSAN QDSTTGTSAL TASSPPTFIG GLYFTDCIFI ALVYGLNLLR TCSIAELGDV
VCLGIVYLFF KLPTNLARRR TLDPDAGDAI RPGDRPAKLS AFHHTMLLLV RFMCGCFPHL
FPRILFAEQT IGPFVYWRTG GGSADLVRAF DAGLQSSPSK ASRNGKEKVQ REGENFSSHS
RRRLAAPGFK AFEFSTRPQA SSPQKLNAGA SPTTLFYLHG GGFSLGSVAF YAEALIRLRN
KLSALETANS TADHEARVVA VEYSLSPTSL FPVQLLQCLR CYAHLIEKEG QDASRICIAG
DSAGGNLAMS LLLVLSGAVK EERLNERDWT QLPLPGKALL ISPWTDLRPH ASLALSAEVQ
RRRQVKGFHW DYVTPHALQH FAQVYTGALD RPRRVAGPLG YVARLSTFGQ RIGQPTSARR
TSSSGSSPDS KHGNGGGRTR RKRPKNGPAA QRSLVSTLAT PVVTLSRLLH TMLSEPLFVL
IGAANGQAPQ STEPTIGIHD DPEGSGLDPL FPADERSCDI VTSPEDLSRR MDDSKSAFIH
PEARDLLENH PLISPAKADW TRVPPLEGGM YVTWGKHETL AYDIEEWVSR VRDGHASSHA
DQASIVPQAP DQDKDELSPV FKQTGLADTA DSVSGTAMDI ARLQAERAVQ SHIERGAGGV
HAWPFVNMYL ASSHAERERG LDLLAQFIAN PSPKTPVAPE GQGLALHLGS PAPSHESVRL
ASSEKPSLAQ SLASMNVPAD TDADVDLQAA TDVDPITGIP LYSPGSMPSD TGEGLLYSSE
DNSNSQSDGG LDEDSMEGDD GSGHGEPHED EEVEPYYTSP ETQTGPGRSR EARGGSGDVY
LMPVHLSRPS DSGLRSSAVA SAAPVNAWMA SSSSTGAAAL PEDLNPSYFG LSHYSQPRMH
STTLGLHDPN RDPRMARITH HPVEPEGLSD IAEEDSVLSG SVMSDGFQGG PLASSAQHTL
YAPASGTTHP AARQDLRLNT RAATHGRTQS PPSEGEQSGV EVDSAEEVFS PIDSPAGPFS
DEESEAVGHA RGASSSASTS AWKSSADLAQ PSLLSEQQEN AESEDAVELQ SEHDASTIRS
TPKKSSKADV WW
//
