ID A0A0B7N0E5_9FUNG Unreviewed; 634 AA.
AC A0A0B7N0E5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN Name=PARPA_05670.1 scaffold 19499 {ECO:0000313|EMBL:CEP11781.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11781.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP11781.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11781.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; LN726961; CEP11781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N0E5; -.
DR STRING; 35722.A0A0B7N0E5; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic 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 InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR PANTHER; PTHR43400:SF1; FUMARATE REDUCTASE; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 557..633
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 535..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 68290 MW; 2FB0658E373EE7B7 CRC64;
MSLKNQIIVV GGGLSGLSAA HTVYEQGGNV LLLDKNPFFG GNSTKATSGI NGALTRTQIA
LNIKDSVEQF YQDTLKSARD LARPDLIRVL TGRSSSAVEW LQDKFALDLS LVSRLGGHSF
PRTHRGKEQF PGMTITYALM EGFEELAEKQ PTRAKIIKKA KVENLIKDSQ GNVIGVEYVL
VGKGATSQVF KEYGPVILAT GGYAADFTDN SLLKQHRPEL YNLSTTNGDH CTGDGIKMAA
AVGANTIDLE KVQVHPTGLV DPKEPDAKVK FLAAEALRGC GGILLDADGK RFCDELGHRD
YVTGMMNKNK FPIRLVLNTA ASKEIEWHCR HYAGRGLMRK FENGEALAKE MGISPKQLEQ
TFETYNKIAD GKEKDPWGKR FFHNVPIKMT DDFYVALMQP VLHYTMGGVE ITPDAEIKGT
NGSPIPGLFA TGEMCGGVHG ANRLGGSSLL GCVVFGRVAG QTAARHLFSQ LVNNNAQVAQ
QRLGAIGQHL NGGVGINITV NPNQPGVISL DISLPNGGGD NTLSSGTSTQ AIEAAAPVAA
APQQQQEAKK ADEPKKMGEY SLEDVAKHNK PDDCWVVVNG QVLDVTDFLP DHPGGKKAIL
IYAGRDATEE FNMMHKPDVV QKYAPSAIIG TLKK
//
