ID A0A0C3BXY5_HEBCY Unreviewed; 665 AA.
AC A0A0C3BXY5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DUF6314 domain-containing protein {ECO:0000259|Pfam:PF19834};
GN ORFNames=M413DRAFT_449186 {ECO:0000313|EMBL:KIM36301.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM36301.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM36301.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KN831806; KIM36301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3BXY5; -.
DR STRING; 686832.A0A0C3BXY5; -.
DR HOGENOM; CLU_023116_0_0_1; -.
DR OrthoDB; 1612588at2759; -.
DR Proteomes; UP000053424; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR045632; DUF6314.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF110; DUF6314 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF19834; DUF6314; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00370; FMOXYGENASE.
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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053424}.
FT DOMAIN 493..664
FT /note="DUF6314"
FT /evidence="ECO:0000259|Pfam:PF19834"
FT REGION 515..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 665 AA; 73572 MW; 7FFDD276CBAF6D68 CRC64;
MAKTVAIIGA GPAGLVSAKY VAEIGFSPRI FEKDESIGGL WAPNSKLCRP SMRTNLSKYE
CAFSDFSWPP GTPIFPTAVQ VGEYLSSYAQ KFLKPGVLSL GCRVTHVERS DTDDKWLITW
SSRGGKEIER AEFDHLIMSC GFFSRPHVPS IPGLETFPRS VIHSSAYTDP GVFSGKHVAI
IGGSHSSAEV AKDPGSTLLP WDFILYRRPS QPPNQQTQQE RWQKTHAFMR SVGVNPVGLS
AGSNVSMDTP PYVAISDQYT NFVRSGRIKV HSGRLASISG SQLTIVSDTS YTLPSNVTDI
IFATGFHPSA ATTILPPTLL SELDFLESDS FLPFLLHRAT LHFAFPSAGF VGHYRGPFWS
IMELQARWCA GLFSGSLPWP TDAEIRDGIL LEKTMRNSKP RVQFPRGDYV GFGTELANAV
GVVLPPPGAE LDKQRLRPQD IFGPHLLARP SWLQPSNDNR TTEPQKLVGE LEHTLDLAAT
SALFVAAAVF RSLHGSWILN RTYISRHPDY PSGVSTGTAE FIPRKASSSS PSTSQEAHGE
PRNLEYLYSE QTELTTSAGL KLAGTKQYIY QYDEPKDKLV VYFAKRDSGS TLESLFHRLD
FEVPSGNAPP KTPWGATGSH WCSPDTYEVR YTFSFKGADV EEWKIEYEVK GPNKDYSMET
WYTRT
//
