ID A0A2S6C337_9PEZI Unreviewed; 305 AA.
AC A0A2S6C337;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Steroid 5-alpha reductase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS50244};
GN ORFNames=CBER1_01076 {ECO:0000313|EMBL:PPJ54139.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ54139.1, 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:PPJ54139.1}.
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DR EMBL; PNEN01000570; PPJ54139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6C337; -.
DR STRING; 357750.A0A2S6C337; -.
DR OrthoDB; 1202332at2759; -.
DR Proteomes; UP000237631; 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: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 166..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..279
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 305 AA; 34242 MW; DF17357FBF0FD133 CRC64;
MASKPVTLQV KPRGKRIPRL PKETSIYVQG STSDLYHRIA AEAKFDINRL RITKEDGTFV
PNEKGKTVDS FGLKDGSVVQ VKDLGLQIAW RTVFIIEYLG PLLIHPIFYL LRPQIYSDAP
SEPSSLQTLS VALISLHFLK REIETFLVHR FSNATMPALN IFKNSAHYWI LAGVLIAYFI
YSPTHPTAGE LNPLIDYPAL AGYVIGELGN LNTHLVLRNL RSPGGTERGV PKGLGFDWVT
CPNYMFEALA WASMCVITRS WTTVVFSAVA IATMGAWAKK KERRYRKELG AKYQKKRFAM
IPGII
//
