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Database: UniProt
Entry: A0A2S6C8Z8_9PEZI
LinkDB: A0A2S6C8Z8_9PEZI
Original site: A0A2S6C8Z8_9PEZI 
ID   A0A2S6C8Z8_9PEZI        Unreviewed;       309 AA.
AC   A0A2S6C8Z8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Steroid 5-alpha reductase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS50244};
GN   ORFNames=CBER1_10339 {ECO:0000313|EMBL:PPJ56202.1};
OS   Cercospora berteroae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ56202.1, ECO:0000313|Proteomes:UP000237631};
RN   [1] {ECO:0000313|Proteomes:UP000237631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA   de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA   Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA   Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT   "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT   mechanisms and extends production to the genus Colletotrichum.";
RL   bioRxiv 0:0-0(2017).
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}.
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:PPJ56202.1}.
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DR   EMBL; PNEN01000523; PPJ56202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6C8Z8; -.
DR   STRING; 357750.A0A2S6C8Z8; -.
DR   OrthoDB; 1364739at2759; -.
DR   Proteomes; UP000237631; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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   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:SF43; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE 2; 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:UP000237631};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          230..283
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   309 AA;  35894 MW;  1B11EF8AF125E9EA CRC64;
     MELIPGILPP SKENWELIVW GWQFFPLVSK HLKYLMSVFK ETNRQPPQFT ATQWFIDYYP
     QGKTSVDSKW NLPGKWAWLI MELPGITIVN YCAWVLPSKL GLTEGLPWAN WTMIGLYSIH
     YIYRAILSPL WLNPSMSPIH PFVMVSAFIW QTINGLSLGG WLAGYGPTTV WDWAGRLYMI
     EIGLVIWGWS FLGNIFHDDD LREIRRAAAR RQKAQAEKDG KPVAGTDKLY MIPKNGLFHF
     ILYPHYLCEW FEWAGFWMIG GFDCVPARTF LFNEISTMLP RALSGHRWYV EKFGKERIGK
     RKAIIPGLL
//
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