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Database: UniProt
Entry: A0A369GG77_9HYPO
LinkDB: A0A369GG77_9HYPO
Original site: A0A369GG77_9HYPO 
ID   A0A369GG77_9HYPO        Unreviewed;       270 AA.
AC   A0A369GG77;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-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=CP532_4551 {ECO:0000313|EMBL:RDA82754.1};
OS   Ophiocordyceps camponoti-leonardi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA82754.1, ECO:0000313|Proteomes:UP000252748};
RN   [1] {ECO:0000313|EMBL:RDA82754.1, ECO:0000313|Proteomes:UP000252748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA82754.1,
RC   ECO:0000313|Proteomes:UP000252748};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RDA82754.1}.
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DR   EMBL; PDHP01000265; RDA82754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369GG77; -.
DR   STRING; 2039875.A0A369GG77; -.
DR   Proteomes; UP000252748; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH.
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; 2.
DR   PIRSF; PIRSF015596; 5_alpha-SR2; 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:UP000252748};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          132..244
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
FT   REGION          156..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  30506 MW;  52F56F9AF76CADD1 CRC64;
     MQWLVKWYGM GKTSTPSRFN IPGRAAWLTM EVPGFLTLLY VLRTLPSMVG VEDLPWQNRV
     LAGLFVIHYI YRAVVFPFLQ PSMAPIHLVV WLSAISFQLF NGTCLGSWLA AYGPVSQQSW
     AEQTPLPQFV LGVSLFYAGL AANFFHDEVL REIRRPSRRR RSGQPLSSAK YKAGGGGGGG
     GGDAVRAPKR YQMPHGGLFR YVLYPHYLCE WIEWFGFLMA AGWTCAPAWA FLVNEIFAML
     PRAIRGKAWY VERFGREKVG RRRAIIPGLL
//
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