ID A8N9L9_COPC7 Unreviewed; 564 AA.
AC A8N9L9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=CC1G_12057 {ECO:0000313|EMBL:EAU90304.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU90304.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU90304.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:EAU90304.2}.
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DR EMBL; AACS02000007; EAU90304.2; -; Genomic_DNA.
DR RefSeq; XP_001831525.2; XM_001831473.2.
DR AlphaFoldDB; A8N9L9; -.
DR STRING; 240176.A8N9L9; -.
DR GeneID; 6007997; -.
DR KEGG; cci:CC1G_12057; -.
DR VEuPathDB; FungiDB:CC1G_12057; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_3_1; -.
DR InParanoid; A8N9L9; -.
DR OMA; AAEDWWI; -.
DR OrthoDB; 2092435at2759; -.
DR Proteomes; UP000001861; 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; 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:UP000001861}.
FT DOMAIN 114..473
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 62158 MW; F17CB9C27A58F5DD CRC64;
MPGPNTHVHS GNSLPSLPEE HNTGSGTENT TPPGARSPPP RRRTSRAAHL GLASLSLNDP
NHNHTSYNTY GGSYRLSSKS PRFNMPAAHD ARARTPRPRN KSFGMRNPAE LALDFIIVGA
GNGLATGFAL AQAGHRVQIF DRNDGIHQRS TGVRVPPNLS KILAEWGLQD ELLSKATKCR
KSVFLSLETN ERVGVLEWQE DVIKETGGDF FLMHYDDLYS MLYNLAASKG VKITFNTTIT
SVQFDASKQR PFVTLGSGSV VYADMVIGAD GLKSIVREVV TGEQDAPNDS GMCYVSFVVP
AEKLKADPDW GKWVGVSEWP IWMGTGRNVL GYPIRNGQEY CIHAFHPDSL IKISPVERTS
ESWTDIIPTD AILHEDSHPS IHRIFSSVPD AIRVKYNPRE AIDDWVDESG TIMLIGEAAH
PLMPCTIHNL ALAVEDAAVL GVLLSHLHSR RQLPQLLEAF QDLRFSRIQQ AHQSELNNAG
FTTLPPGEHR DARDAGLRQS LLAPSAEGTE WNDDRLREQW EGISFAFGYD ALEAAEDWWL
KWGALVGGGQ TEAVEVAIEK IQLT
//
