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Database: UniProt
Entry: A0A2H3IQ50_9EURO
LinkDB: A0A2H3IQ50_9EURO
Original site: A0A2H3IQ50_9EURO 
ID   A0A2H3IQ50_9EURO        Unreviewed;       240 AA.
AC   A0A2H3IQ50;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Cytochrome b561, eukaryote {ECO:0000313|EMBL:PCH08238.1};
GN   ORFNames=PENO1_007320 {ECO:0000313|EMBL:PCH08238.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH08238.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH08238.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH08238.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCH08238.1}.
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DR   EMBL; NPFK01000010; PCH08238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3IQ50; -.
DR   OrthoDB; 2045945at2759; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
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:SF24; LD43293P; 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   Reference proteome {ECO:0000313|Proteomes:UP000218381};
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        41..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        208..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          39..236
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000259|PROSITE:PS50939"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   240 AA;  26229 MW;  751DA6DC45616F50 CRC64;
     MASTDYPEDG ITNPIPNEEE PLLGSNGSVT QKDTTPIYHN FLTGTAVVAQ AGIWVLFAVI
     WSAVFSHDLI FFAAHPLLNS TALLLQVQAI LVLQPTSTPR QKSIGTHLHF AFLILSLAGF
     ISAFVVIELN KDPEHRLSSI HGVLGFITYI LIIIQALVGV AQFWIPKWVF GSVENGKKIY
     KYHRISGYVL LVLELAAVAA ATQTAYNIYV LNIALWAVLV TSVLTLLGIG ARIKISKFGF
//
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