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Database: UniProt
Entry: S3D357_OPHP1
LinkDB: S3D357_OPHP1
Original site: S3D357_OPHP1 
ID   S3D357_OPHP1            Unreviewed;       330 AA.
AC   S3D357;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Enoyl reductase tsc13 {ECO:0000313|EMBL:EPE07715.1};
GN   ORFNames=F503_00437 {ECO:0000313|EMBL:EPE07715.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE07715.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE07715.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE07715.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA   Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT   a comparison with the bark beetle-associated pine pathogen Grosmannia
RT   clavigera.";
RL   BMC Genomics 14:373-373(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC       {ECO:0000256|ARBA:ARBA00007742}.
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DR   EMBL; KE148150; EPE07715.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3D357; -.
DR   STRING; 1262450.S3D357; -.
DR   VEuPathDB; FungiDB:F503_00437; -.
DR   eggNOG; KOG1639; Eukaryota.
DR   HOGENOM; CLU_059260_0_1_1; -.
DR   OMA; WAWKKEK; -.
DR   OrthoDB; 1202332at2759; -.
DR   Proteomes; UP000016923; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.120.1630; -; 1.
DR   InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR   InterPro; IPR039357; SRD5A/TECR.
DR   PANTHER; PTHR10556; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE; 1.
DR   PANTHER; PTHR10556:SF28; VERY-LONG-CHAIN ENOYL-COA REDUCTASE; 1.
DR   Pfam; PF02544; Steroid_dh; 1.
DR   PROSITE; PS50244; S5A_REDUCTASE; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        273..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..304
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   330 AA;  37438 MW;  46257BB24B168B64 CRC64;
     MAPLQLKVAN RGKSRSVKNL PPTIDVSTAT TIEEVQQLVA KQSGVRDYNR IGIFDPVSRK
     IIRDRRAVLG AQDDVLKTKE ILVQDLGAQI GWRTVFVIEY AGPILFHLAF YYLRPIIPLP
     AFLVGTQAAS RQDPLTDIQK LVHTLFVAHF VKRELETIYL HRFSANTMPA FNIFRNSAFY
     WLLAGLFDSW SVYAPLSPFR LSSEFPRATP ARSGFGTSVL DYIGLAMFIF CELANFSVHY
     HLANLRKPGS TEKGIPNCIG SSLVTSPNYM FEVLAWVGVI ILSRDLSVLI FISIGVIYMR
     SWSRDKERAL RRLFPDRYKK KKYTMLPGLI
//
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