GenomeNet

Database: UniProt
Entry: A0A084QKF9_STAC4
LinkDB: A0A084QKF9_STAC4
Original site: A0A084QKF9_STAC4 
ID   A0A084QKF9_STAC4        Unreviewed;       491 AA.
AC   A0A084QKF9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=S40285_01066 {ECO:0000313|EMBL:KFA64444.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA64444.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA64444.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA64444.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL660686; KFA64444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QKF9; -.
DR   STRING; 1283841.A0A084QKF9; -.
DR   HOGENOM; CLU_032067_2_0_1; -.
DR   InParanoid; A0A084QKF9; -.
DR   OMA; GPWYGRV; -.
DR   OrthoDB; 2234927at2759; -.
DR   Proteomes; UP000028524; 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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR43872; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR   PANTHER; PTHR43872:SF1; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028524}.
SQ   SEQUENCE   491 AA;  54925 MW;  655DEBD4DA9809C1 CRC64;
     MASPIETHDI IILGAGLSGI NAAHMLRTQM PHRKLTMLEA RPVLGGTWTF FRYPGFRSDS
     HMSTFGLPWH PWPHAHKVAS GPEIAAYLED AARTDGSYQK IRFRHRMVGC EWHSEEQQWT
     LEVDADGKRK TLKANFVVSC TGYYSYDKAF PVNIPGLETF GGQVAHPQWW PKDLDWSGKR
     VVVVGSGATM VTLLPNLAEK AGRVTVLQRS PSYVAAMPTR SKVDDVLRML LPALWFHLLL
     RWRDSIGELL LTQFLLAFPA IGRFAITRRA KKELPQHIDV DTHFNPAYNP LQQRPCLCPD
     GDFFKALHRE NCEVVTDVIE TVTPSGILLK SGRQLEADLI ITATGLYFEL LGGVTLVVDG
     RPIAAGEHFA WRGCMLDSVP NMVFVMGYST STWTPGADAT TRLALRVVQH MERRGATSVT
     PTMQRREQAP RRLAVDATSS YFVKAADRMP KVTGSGPWYG RVSLAKDWWA LWFASMEDGL
     VYGRHGKAKP A
//
DBGET integrated database retrieval system