ID A0A3E2HG52_SCYLI Unreviewed; 1155 AA.
AC A0A3E2HG52;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7463_g4203 {ECO:0000313|EMBL:RFU32123.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU32123.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU32123.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU32123.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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:RFU32123.1}.
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DR EMBL; NCSJ02000061; RFU32123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HG52; -.
DR STRING; 5539.A0A3E2HG52; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR46072:SF2; AMIDASE (EUROFUNG); 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309}.
FT DOMAIN 28..382
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 408..568
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
FT DOMAIN 686..1142
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU32123.1"
FT NON_TER 1155
FT /evidence="ECO:0000313|EMBL:RFU32123.1"
SQ SEQUENCE 1155 AA; 126720 MW; 79C6782682E6AEB1 CRC64;
MSPSAHNETY KNGHDVIMNG SGGNDVENVV VVGAGPAGLM LASNLARYGI KPVVVDDRSD
KTTTGRADGL QPKTIETLKQ LGLADSLIRQ GVKIFDICFW NSTPTTPMHR TRREVHYPPE
VDVKDPYILL CHQGMIEDLF IEDLRERGVE VTRSSPFDHY TGSNFKEPLE IVCNDTISGS
QKVLQAKYLV GCDGARSKVR SSIPGAVMLG DVARAPWGVL DGVIETDFPD LWSKVIIHSE
EEGTILCIPR ERNMTRLYIE LNAGMHEMLS SEAASQEFVM KKAQEIIAPF SLTWKSVEWF
SVYKVGQRVA NRFTDDIDRV FITGDAAHTH SPKAAQGMNV SMHDAFNLSW KLNLAIRGLA
LPSLLSTYSH ERRKIAQDLI NFDFEHANAF AEGDSKALAA NFAANIAFIS GIGASYAPNV
LNIESPNTGG CLRSGALLLQ ARVTRYIDAN PVDIQLDIPM LGQFRVFFFT RNPHASSAFL
TTVSSHLTST NSVLGRASLA ASHSYTILNT PAPDSDGFSQ PQRYTAVSKL FTPALITTIS
KEEVEIADLP PMLRESRWTF YLDDVPGEKQ TCTDKWVGGC SEDEVVVVNV RPDGYVGAIG
RWTNGEAAKA CDYLDAYYGG FLMGEAPVKV TVSSWERIAE SKQAIREAAV APYLLAANPA
TDPITDINDV EELAELLSSG KLKAEEVILA YIKKAAVAHK ATNCLTEICF EAAIQRARTL
DKYYQDHGKT IGPLHGIPIT LKDQFNIKGL DTTLGYVNMA FKPAEDDAVV VKILQDLGAV
MIAKSNLPQS IMWCETENPL FGLTTNPRNA SFTPGGSTGG EGALLSLKAS IVGWGTDIGG
SIRIPSSING LYGFKPSSAR MPYQGVPVST EGQEHVPSSI GPMTRSLSSI TTITKAVINA
EPWLLDPKVV PIPWRDSIYH EVQSRPLVIG IITDDGVIKP HPPIERALRE LAAKLKVAGH
EVINWEPSLN KECVAIMDKF YTADGGEDIR RAVKAGGEPF LPHVEALINR GKPISVFEYW
QLNKEKIAAQ KAYLDKWNST RGPVSGRVVD ILLTPTMPHS AVPHRTTRWV GYTKVWNVLD
YTALSFPVDT ISIEKDPVPS PPYEPRSDLD AFNWKLYDPV AMNGHPVGLQ IVGRRFDEEK
VLGAAKVIEE VMKKY
//
