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Database: UniProt
Entry: A0A2S5BBQ0_9BASI
LinkDB: A0A2S5BBQ0_9BASI
Original site: A0A2S5BBQ0_9BASI 
ID   A0A2S5BBQ0_9BASI        Unreviewed;       665 AA.
AC   A0A2S5BBQ0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE            EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN   ORFNames=BMF94_2752 {ECO:0000313|EMBL:POY74178.1};
OS   Rhodotorula taiwanensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=741276 {ECO:0000313|EMBL:POY74178.1, ECO:0000313|Proteomes:UP000237144};
RN   [1] {ECO:0000313|EMBL:POY74178.1, ECO:0000313|Proteomes:UP000237144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD1149 {ECO:0000313|EMBL:POY74178.1,
RC   ECO:0000313|Proteomes:UP000237144};
RX   PubMed=29375494;
RA   Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA   Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA   Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA   Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT   "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT   Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL   Front. Microbiol. 8:2528-2528(2018).
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00004760}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295}.
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:POY74178.1}.
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DR   EMBL; PJQD01000028; POY74178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5BBQ0; -.
DR   STRING; 741276.A0A2S5BBQ0; -.
DR   OrthoDB; 294339at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000237144; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03506; Delta6-FADS-like; 1.
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; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR19353:SF30; DELTA 8-(E)-SPHINGOLIPID DESATURASE; 1.
DR   PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        268..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        332..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        414..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        448..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        478..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..132
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00173"
FT   DOMAIN          304..583
FT                   /note="Fatty acid desaturase"
FT                   /evidence="ECO:0000259|Pfam:PF00487"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   665 AA;  74766 MW;  7B74ADFEECB1EC20 CRC64;
     MTAGTMDQVA AAVPVQPRAP LPASGSSSSS TTRPRQRASA RLPSPDLALP AHYDSLVTLS
     RVEVAARIAR GELLVLQPPL VYRVPHKWLD LHPGGHHAIL HYVGRDASCE IMAYHTARTV
     EERMARWIVG RVDVDDSDET EGQGWIDMTP PIQLGKWPIP IPTITVSSPP ASPARKRVRR
     VGRDTQDDDD NADDDNAQLA TDAHAKRLPD KVPQSDTLTP AMVDPPLDPA DYEHLPLTPA
     YQAHLRRSVK RLYARLQTKG LDRPPRFLAG YGPSLVIYIA LAVLSVWTYR RALGTSSTGD
     YLAAAVCLGA FYHQVTFVVH DAGHTGLTGS WMVDRLCGIG LANFIGGLSL GWWADNHNVH
     HLVTNAPEHD PDIQHLPFFA ISTRFFDSIK STYYDRLVAF DAFARFVLPY QHKLYYIVMC
     FARFNLFALS YSFLLTRWPG RRSPLFKLRI LELVGIIFFW SWFGGIVLRN MDTAAHRWLY
     VIVSFAVTSP LHVQIVLSHF SQPISIFPAD STPADDKLAG KVPRASLELL ESHPHRQLRT
     TMDVSCPTYL DFLHGGLNFQ TPHHFFPRIP RFNFRAVAKE IERWVDVENA ALETRTEKDP
     KSGEERRVRY WRSHRLKDGE GLVYKKMTFV EGNRSVLGVL KGVAQQVELL AKVAEKDAKG
     ELHHH
//
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