ID A0A395SW40_9HYPO Unreviewed; 597 AA.
AC A0A395SW40;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Amidase domain-containing protein {ECO:0000259|Pfam:PF01425};
GN ORFNames=FLONG3_5150 {ECO:0000313|EMBL:RGP76710.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP76710.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP76710.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP76710.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP76710.1}.
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; PXOG01000111; RGP76710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SW40; -.
DR STRING; 694270.A0A395SW40; -.
DR Proteomes; UP000266234; 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; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR46072:SF4; AMIDASE C550.07-RELATED; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR PIRSF; PIRSF001221; Amidase_fungi; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234}.
FT DOMAIN 132..583
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 284
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 281..284
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 597 AA; 65054 MW; EE6802A2C9518D73 CRC64;
MSLRATSISQ FGPVSSVKTA SIDTADQLEL VNPEQSVTET ALPGLPVIQV TPILRGTLDF
ETKRAALLEE FASKVPQVFR LPVGLIRNPP KNVSVIPPIC SILSQEELEI TEHDAVGLLE
GIASRKYTSV AVARAFCKRA IVAHQLTCCL TQWYMDEAIA QAQKLDAYFE QHGKPIGLLH
GLPISIKEHI QVAGTYSSQG CFASITYDDT DADIVAILRS QGAVIYCKTN QPQSIMHLET
DSHWGTVLNP YNIYLSAGGS TGGEAALIAM KGSVLGVGTD IGGSIRGPSA FCGIYGFKTT
SNTLPTRGYV KGAPPPSVLN VPLSTGPMCR SLRDMDLFMR CVLSAKPFLS DPNVVSLPWT
GLKTSFGRRL KVGVVDNDGF IEPQPPVKRA VWWAKSVLSD SKYADVIEVK DFKVFGSEEA
WKQVRRLYWP DGAQLTKNGI MSSGEPLHPL TKWIAQDAEP LGMQTALDIT LQHKDRDDFR
LAFAQSWTDQ DVDVIIGPSF VGPACAHDTA LYWSYTSLYN LVDYPGAVIP TPIKAESGEG
YDESYAPLSE ACSRVKKMWD EGDFAGAPVN LQVVARRHHD DELFGAMNVL KDVFGLV
//
