ID A0A1F7ZVY1_9EURO Unreviewed; 346 AA.
AC A0A1F7ZVY1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=Heme/steroid binding protein {ECO:0000313|EMBL:OGM43633.1};
GN ORFNames=ABOM_008525 {ECO:0000313|EMBL:OGM43633.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM43633.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM43633.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC {ECO:0000256|RuleBase:RU362121}.
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:OGM43633.1}.
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DR EMBL; LYCR01000067; OGM43633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZVY1; -.
DR STRING; 109264.A0A1F7ZVY1; -.
DR OrthoDB; 163533at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR PANTHER; PTHR46237:SF1; CYTOCHROME B5 REDUCTASE 4; 1.
DR PANTHER; PTHR46237; CYTOCHROME B5 REDUCTASE 4 FAMILY MEMBER; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362121};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..346
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009534247"
FT DOMAIN 253..331
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 24..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 36539 MW; FC18C02E7EF9FF21 CRC64;
MGWLGVATLI ATACFLLYRH PPSSWTSEPT ISSPPSKPTL AEPPADRAID DTKVKSDSKP
LEEKNGNLED PQSTPKASAS SPPSLEVPTL HLDSGKAEKP AIATENQADK KPIQNGSAKP
SEPVAIAVKN AAMPPPPLPT ASTSSLMPPP PPPRLRQTMS QTQQPQSAPA GRYPPRPNPG
SSLRPPPSAA ASLRVPPSGR SSSNSLAPIK LTAQPSNSSK RAVLEPGYSP LDWAALTSNP
KNNLRGANLP PTLVKVTPSM LKAQNGRKGR DAWTSYQGKV YNITPYVPFH PGGKGELLRG
AGKDSAKLFM EIHPWVNWDA ILGECLVGIL VSENDGAAEN ALDAMD
//
