ID A0A066X2Z6_COLSU Unreviewed; 114 AA.
AC A0A066X2Z6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative cytochrome b5-like Heme/Steroid binding domain-containing protein {ECO:0000313|EMBL:KDN63322.1};
GN ORFNames=CSUB01_01979 {ECO:0000313|EMBL:KDN63322.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN63322.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
CC -!- FUNCTION: Membrane bound hemoprotein which function as an electron
CC carrier for several membrane bound oxygenases.
CC {ECO:0000256|ARBA:ARBA00043840}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004131}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004131}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004131}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00037877}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00037877}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00037877}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC {ECO:0000256|ARBA:ARBA00038168, 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:KDN63322.1}.
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DR EMBL; JMSE01001246; KDN63322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X2Z6; -.
DR STRING; 1173701.A0A066X2Z6; -.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_102602_3_2_1; -.
DR OMA; HEKVYDC; -.
DR OrthoDB; 2712490at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR19359; CYTOCHROME B5; 1.
DR PANTHER; PTHR19359:SF14; CYTOCHROME B5-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
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 Membrane {ECO:0000256|RuleBase:RU362121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362121};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Transmembrane {ECO:0000256|RuleBase:RU362121};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362121};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 84..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362121"
FT DOMAIN 1..58
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 57..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 114 AA; 12133 MW; 28B564CF654407D3 CRC64;
MVIHDKVYNV TKFVDEHPGG EEVLLDVAGQ DATEAFEDVG HSDEARETLE QLHIGELKRQ
PGDPAPKKAA AATSSASSTE SGGFGIGLYA VLLIGGILAY VGYQYQQQQQ NTSA
//