ID A0A1V6RW50_9EURO Unreviewed; 362 AA.
AC A0A1V6RW50;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Steroid 5-alpha reductase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS50244};
GN ORFNames=PENVUL_c020G09118 {ECO:0000313|EMBL:OQE05982.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE05982.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(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:OQE05982.1}.
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DR EMBL; MDYP01000020; OQE05982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RW50; -.
DR STRING; 29845.A0A1V6RW50; -.
DR OrthoDB; 1364739at2759; -.
DR Proteomes; UP000191518; 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:UP000191518};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..269
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 362 AA; 39625 MW; 40434809E638393A CRC64;
MGAIISTCLG ALPSTAELFP PTPAAYTPIL YGFQYFPLIT VALWILSWYP AGKTSSQSVF
NIPGRIAWSV MELVGPINLI YTMTSPSPYS PSFTDLPKPN ILIVALYCTH YLNRAVISPF
FSAPSMSPIH VVVMAAAMLF NWFNSACLAG WLRGYVVPTI PSFNTATSGN PSPRSVVVEL
LPTIGLILFA IGMAGNIYSE TEFFRLRREE AERRVAKKVD DESPGGEARG SRNKFYKVYV
IPPACGVFRY ILYPHYVFEW LEWIGFALAG TAVAPFSALP PSTSAPFLAI SPPLRLAPWL
VPAAWAADKL AVPLPLPAVI FVINAVTNML PHARWGRKWY VEKFGEKAVA GRGAVVPGCA
WM
//
