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Database: UniProt
Entry: A0A165E8R3_EXIGL
LinkDB: A0A165E8R3_EXIGL
Original site: A0A165E8R3_EXIGL 
ID   A0A165E8R3_EXIGL        Unreviewed;       123 AA.
AC   A0A165E8R3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cytochrome b5 {ECO:0000313|EMBL:KZV86333.1};
GN   ORFNames=EXIGLDRAFT_622081 {ECO:0000313|EMBL:KZV86333.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV86333.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV86333.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV86333.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR   EMBL; KV426159; KZV86333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165E8R3; -.
DR   STRING; 1314781.A0A165E8R3; -.
DR   InParanoid; A0A165E8R3; -.
DR   OrthoDB; 2712490at2759; -.
DR   Proteomes; UP000077266; 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:UP000077266};
KW   Transmembrane {ECO:0000256|RuleBase:RU362121};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362121};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362121"
FT   DOMAIN          1..78
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   123 AA;  13075 MW;  039D6F674D602FFB CRC64;
     MTIINIADVA AHKTRDSAWL VLNGKVYDAT KFLDEHPGGD EVILSECGKP DATEAFDDIG
     HSDEARALLA DMLVGTVEGA AEIKQKPVPT RPAANTGPGF NAVLVPIALL GAYLAWRAYF
     LSP
//
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