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Database: UniProt
Entry: A0A0N0NQ38_9EURO
LinkDB: A0A0N0NQ38_9EURO
Original site: A0A0N0NQ38_9EURO 
ID   A0A0N0NQ38_9EURO        Unreviewed;       305 AA.
AC   A0A0N0NQ38;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Putative enoyl {ECO:0000313|EMBL:KPI43458.1};
GN   ORFNames=AB675_6750 {ECO:0000313|EMBL:KPI43458.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI43458.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI43458.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI43458.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) 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:KPI43458.1}.
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DR   EMBL; LFJN01000005; KPI43458.1; -; Genomic_DNA.
DR   RefSeq; XP_018003421.1; XM_018147063.1.
DR   AlphaFoldDB; A0A0N0NQ38; -.
DR   STRING; 1664694.A0A0N0NQ38; -.
DR   GeneID; 28738943; -.
DR   OrthoDB; 1202332at2759; -.
DR   Proteomes; UP000038010; 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:UP000038010};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        164..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..279
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   305 AA;  33939 MW;  9A9B776FF2D1589E CRC64;
     MSKPITLQIR PRGKPIKSLP EAVSVPADAT AADLYGLLST KSRYSVHQLR VTKGSDGSHI
     PNGTSTVHST GLRNDSTIYV KDLGPQIAWR TVFVIEYLAP IFIHPLFYAL AAHIYGGTGA
     QSQMQKTALV AIVAHFVKRE FETLFIHRFS AATMPIRNIF KNSAHYWLLS GVNMAYWIYS
     PTSSSAKDPP NQALLFAGIA LYAFGELGNL STHLTLRNLR SQGGNERGIP QGALFNLVTC
     PNYFTEVLSW VGVWLISGLN WSVVVFLVAS GAQMASWASK KERRYRKEFG DKYKRKRFVM
     LPGIW
//
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