ID A0A1Y1WH37_9FUNG Unreviewed; 565 AA.
AC A0A1Y1WH37;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Amidase signature enzyme {ECO:0000313|EMBL:ORX72829.1};
GN ORFNames=DL89DRAFT_265016 {ECO:0000313|EMBL:ORX72829.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX72829.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX72829.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX72829.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORX72829.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFD01000002; ORX72829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1WH37; -.
DR STRING; 61395.A0A1Y1WH37; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000193922; Unassembled WGS sequence.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
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:SF4; FATTY-ACID AMIDE HYDROLASE 2; 1.
DR Pfam; PF01425; Amidase; 2.
DR PIRSF; PIRSF001221; Amidase_fungi; 3.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193922}.
FT DOMAIN 84..318
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 449..524
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 544..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 247
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
SQ SEQUENCE 565 AA; 61754 MW; ECC4E97E46898E48 CRC64;
MSILAFVIGT LILRPIQVLF WAPLRTFVFF YIHVATGIPR KIRQAKKLSE NPWTSLDSYD
PLLLVSATEL ARRIRAGELS SEAVVKAYIR RIQKVNPLIN AVVASRFETA ILEARDVDRL
VAKGGLPNGH NAQEKPFWGV PITVKESIAV QGMPNTYGLV WRTSGTYSPA QEHSVRAQKL
IDAGFIILGV TNICEALMTG ESDNRVYGRT FNPYDLARNP GGSSSGEGAI VGAAGSVIGV
GTDLGGSIRM PAFFCGVFGH KTTAEWIPKE KPNFMSPLTA EKAACSSTGP LCRYAEDMAP
FVSALIGRNI GDPRSIDLSK LRVVAFPDGL GHSMLISKLD PALHTAVIDV TSYLAQQVVG
QENVIMAQMP SYISQASVKF GPMIATGERT LPEILGGEGM PHADLTRELA SFIKGSSNYT
GYSFQNHLLR ILPTPKGTRE QVVPFWNKLR DHLETLMGEN GVMIFPPHPC VARPHGTDFF
NRPNLMYTAI FNALGFPATQ VPLGLNKDGL PLGVQVIARK GDDLKTIAVA IQLEKRFGGW
TPPRRFGAPL PEHDTEKLYN HRMKK
//
