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Database: UniProt
Entry: A0A2V1BHW3_9HELO
LinkDB: A0A2V1BHW3_9HELO
Original site: A0A2V1BHW3_9HELO 
ID   A0A2V1BHW3_9HELO        Unreviewed;       433 AA.
AC   A0A2V1BHW3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:PVH73006.1};
GN   ORFNames=DL98DRAFT_501634 {ECO:0000313|EMBL:PVH73006.1};
OS   Cadophora sp. DSE1049.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Cadophora.
OX   NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH73006.1, ECO:0000313|Proteomes:UP000244409};
RN   [1] {ECO:0000313|EMBL:PVH73006.1, ECO:0000313|Proteomes:UP000244409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE1049 {ECO:0000313|EMBL:PVH73006.1,
RC   ECO:0000313|Proteomes:UP000244409};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(2018).
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; KZ804253; PVH73006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1BHW3; -.
DR   STRING; 1485229.A0A2V1BHW3; -.
DR   Proteomes; UP000244409; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF238; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01680)-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:UP000244409};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..433
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015949406"
FT   DOMAIN          7..348
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   433 AA;  48250 MW;  F8F8BDD5C5DA97CB CRC64;
     MSESIHLIII GAGLAGLSAG ISTKIANPNH RVTILESVKE LAEIGAGLQL TPNATRLFKP
     WGIYDHLAPR ATFPKALSVH RYDGTKLLAH EPKFQEQIDE RYGSPFWGMH RVDLQRAMAA
     RCKELGITIR LNAKVISVDF EMVEVKLQDG EVIDGDVVLC ADGLWSSTRC QFLGKPSPAI
     LTGDLAYRIV INTADLTGPD APELQKFIRD STVNFWVGPG THVVAYTMRA GDVYNIVLLC
     PDNLPPGVSK TDGDIEEMKA LFVGWDPILR KFLDQVKGVA KWKLMWLDTL PEWANEQGTF
     LMMGDCCHPM LPYLAQGANS SLEDGAVIGS LLGKVNGSGE GKEAQLKKCA KLYQALRKER
     GEGIQRETFK QRRDFHLPDG KEQEERDELM LGMLGGELKA DFPSRWTCPR VQRWLYGYDA
     YKEVKEAFAK EPF
//
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