ID A0A165P7G8_9AGAM Unreviewed; 442 AA.
AC A0A165P7G8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
DE Flags: Fragment;
GN ORFNames=NEOLEDRAFT_1122368 {ECO:0000313|EMBL:KZT20631.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT20631.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT20631.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT20631.1,
RC ECO:0000313|Proteomes:UP000076761};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295}.
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DR EMBL; KV425617; KZT20631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165P7G8; -.
DR STRING; 1314782.A0A165P7G8; -.
DR InParanoid; A0A165P7G8; -.
DR OrthoDB; 637961at2759; -.
DR Proteomes; UP000076761; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:InterPro.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR009160; Acyl-CoA_deSatase_haem/ster-bd.
DR InterPro; IPR015876; Acyl-CoA_DS.
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; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF000345; OLE1; 1.
DR PRINTS; PR00075; FACDDSATRASE.
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.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..392
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT NON_TER 442
FT /evidence="ECO:0000313|EMBL:KZT20631.1"
SQ SEQUENCE 442 AA; 50814 MW; B58E2B35B0AE10D3 CRC64;
MPQRPEITWR NAYREIRWFS LAVLVLTPML ALYGSFTTPL RRKTCIFSVL YYVFNMLGIT
AGYHRLWSHR SYNASLLLQY FLACAGAGSV QGSIRFWARL HRAHHRYTDT ALDPYSAHLG
FWHSHFGWML VKPRVKPGRA ECGDLQKNRV VMWQHRWYFP LAAFWGLLVP VAFCGLTWGD
WWGGWYWAGF ARLVAVHHST FAVNSIAHWL GSTPYSDRHS PRDHLVTALL TLGEGYHNFH
HQFPSDYRNA IRWYQYDPTK WFISLCAFFR VASNLQRFRE SEIQKCRLMM KLKILKKIQD
EVEKRWGWGV PVANLEIWSW KKFTQASATR PLMVISGFVH DVSSFMQEHP GGETYLRAHV
GKDATSAFYG GTYDHSEVAV NLLATLRVSI LRHGVEVVAA TPSSNDSHDA PHDGADERCA
AHVPPGKKLQ IIEVMPHIGL GS
//
