ID A0A060SDH8_PYCCI Unreviewed; 481 AA.
AC A0A060SDH8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=BN946_scf184983.g55 {ECO:0000313|EMBL:CDO72572.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO72572.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO72572.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO72572.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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:CDO72572.1}.
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DR EMBL; CCBP010000114; CDO72572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SDH8; -.
DR STRING; 5643.A0A060SDH8; -.
DR HOGENOM; CLU_009665_19_3_1; -.
DR OMA; MTGWMGP; -.
DR OrthoDB; 2092435at2759; -.
DR Proteomes; UP000029665; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF147; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01950)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029665}.
FT DOMAIN 35..384
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 53538 MW; 149A25088B4ADAAB CRC64;
MTTHTEPVPA HHAANAEGIS QRTRLYDGRK PAHRLHVLVV GCGMGGLAAA HCLGQAGHKV
TLFESAAAIG EVGAGIQVTP NVSRLLRRWG VGEKLEAVAV RPEAIVLRKY NTGERVAYTR
WSDMEEQYGA PYYHIHRADL HKLLFDLAAP FMTLRLKSTV VSVDPEAPSV TLASGEVVHG
DLIVGADGVK SMIQRVVLGH TNPAEPTGDA VYRAIIPTDY LLKDPELKPF VDHPEMTGWM
GPGRHIMAYN IRAKKEFNIV LAHPDDGSVE SWTAEGSADK MRADFADFEP RIRKLLGFVK
STLKWRLMDR QPLKKWIHSS YKVILLGDAC HPMLPYRAQG AAMAIEDAAV LGNLLSRLND
PSQLKPLLQA YEDLRLPRTA ETQRQSRLNQ KIFHLPDGPE QEARDAQMRQ AMELELRVMR
EGVAPGEVTL EGSPNQWADR KKNEAQFAYD ADREAERWWR EVGEKSLGGE GEFERAVAAR
L
//
