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Database: UniProt
Entry: A0A2G5HTM3_CERBT
LinkDB: A0A2G5HTM3_CERBT
Original site: A0A2G5HTM3_CERBT 
ID   A0A2G5HTM3_CERBT        Unreviewed;       205 AA.
AC   A0A2G5HTM3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Cytochrome b561 domain-containing protein {ECO:0000259|PROSITE:PS50939};
GN   ORFNames=CB0940_10214 {ECO:0000313|EMBL:PIA95879.1};
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:PIA95879.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA95879.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA95879.1,
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
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:PIA95879.1}.
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DR   EMBL; LKMD01000103; PIA95879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HTM3; -.
DR   OrthoDB; 2045945at2759; -.
DR   Proteomes; UP000230605; Chromosome 8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140575; F:transmembrane monodehydroascorbate reductase activity; IEA:InterPro.
DR   CDD; cd08761; Cyt_b561_CYB561D2_like; 1.
DR   Gene3D; 1.20.120.1770; -; 1.
DR   InterPro; IPR045150; CYB561D1/2.
DR   InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR   PANTHER; PTHR15422:SF44; ASCORBATE FERRIREDUCTASE (TRANSMEMBRANE); 1.
DR   PANTHER; PTHR15422; OS05G0565100 PROTEIN; 1.
DR   Pfam; PF03188; Cytochrom_B561; 1.
DR   SMART; SM00665; B561; 1.
DR   PROSITE; PS50939; CYTOCHROME_B561; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        32..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..197
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000259|PROSITE:PS50939"
SQ   SEQUENCE   205 AA;  22053 MW;  FB5FD8E1F190D31C CRC64;
     MASGTAVVAQ AGAWIIAAIV WGAVFSNDLI LFSAHPLLNS AAFLFLIQGI LVLQPTHTAQ
     QKKQGTYTHA ALNDVGILAA IAGLVVIEYN KFDHNGTHFE SPHAILGLVT YILVTLQALV
     GFTQYFTPGL YGSVDKAKSL YKYHRVGGYI TTVFMLATIC AATYTTFNVN VLQIQLWAVV
     VASILVVLGI ASRIRLAKFG WLAGK
//
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