GenomeNet

Database: UniProt
Entry: A0A2G5HUU7_CERBT
LinkDB: A0A2G5HUU7_CERBT
Original site: A0A2G5HUU7_CERBT 
ID   A0A2G5HUU7_CERBT        Unreviewed;       496 AA.
AC   A0A2G5HUU7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   22-FEB-2023, entry version 11.
DE   SubName: Full=Corticosteroid-binding protein {ECO:0000313|EMBL:PIA96063.1};
GN   ORFNames=CB0940_10158 {ECO:0000313|EMBL:PIA96063.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA96063.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA96063.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA96063.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIA96063.1}.
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; LKMD01000103; PIA96063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HUU7; -.
DR   OrthoDB; 2949649at2759; -.
DR   Proteomes; UP000230605; Chromosome 8.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF404; POLYAMINE OXIDASE FMS1; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          33..480
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   496 AA;  54948 MW;  61250F4C7F3E5EF5 CRC64;
     MAVQAEAPAA IDKLAPRTGV NEKAKVIVLG AGISGLRAAS VLQRHGLDVT IVEARDRIGG
     RIQTTRNEKG VPRDIGAAWC HETSQNPLVK LISKLKLDYY YDDGLPLYYT EHGRAGAQAK
     FKKVADEAAD HMEWYYETHP EAPDQPVSDF VNAFVAKHEL ITDDERLWAP QAFKEVELWI
     GTSIETASSK HLSYFITERN LYMKGGYDAI VKWTADCLLP NSIQLNSTVD SIAWTEDGSK
     KCAVEYHDDE GNVHVVEADA VVSTLPLGAL KRNLVHFDPP LPSDMQLAIS KFSYGALGKV
     FFEFADVFWS KENDQFVYFP SPPELDADQY STSPGSSSSD EQYSILNYAT VTINLWIMTG
     GKELCIQIAE PLTQRIEAMT NKKEIYKFFE PLFKLLRTEP YKSLPRLIDV ETTHWSQDPL
     AGYGSYSADK VGDDPDLLMD ALENHKGSRL QFAGEHCTLT GNGCVHGAFA TGETAAKNLL
     NSLGVEHDGG DFVSLH
//
DBGET integrated database retrieval system