ID A0A1J7IT87_9PEZI Unreviewed; 507 AA.
AC A0A1J7IT87;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:OIW30702.1};
GN ORFNames=CONLIGDRAFT_574117 {ECO:0000313|EMBL:OIW30702.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW30702.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW30702.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW30702.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family.
CC {ECO:0000256|ARBA:ARBA00009219}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV875096; OIW30702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7IT87; -.
DR STRING; 1408157.A0A1J7IT87; -.
DR InParanoid; A0A1J7IT87; -.
DR OrthoDB; 1649721at2759; -.
DR Proteomes; UP000182658; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43245; BIFUNCTIONAL POLYMYXIN RESISTANCE PROTEIN ARNA; 1.
DR PANTHER; PTHR43245:SF51; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY 42E, MEMBER 2; 1.
DR Pfam; PF01073; 3Beta_HSD; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000182658};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..211
FT /note="3-beta hydroxysteroid dehydrogenase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF01073"
FT DOMAIN 251..368
FT /note="3-beta hydroxysteroid dehydrogenase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF01073"
SQ SEQUENCE 507 AA; 56593 MW; 1C3C1325E28BA702 CRC64;
MDQLLRAAGQ WPFWCSLILP LLVFYLFQIN RLLSGTPDTV RRLSPARWTK EMLFETYKRL
EKRPITIDTY VDQLPPKLDR RYIVTGGSGL VGGHIVLQLL ARGQHPASIR IVDFQKPHRH
DMLDGPASDV DFVQTDISSS ESTDRAFSKA WHPSVAHLPL TVFHTAAIIT PSDRSKLVYG
FCEAVNVRGT QHVVSAARRS GADILVSTTS GSISIRPVEY WVQPWKLWSS WPRNFFQILD
ETDFFEPLRP HEDFYANYPV SKAVAERIVC EANTADFRTG CIRPANGVYG NPTDNTVGSA
LQSATMFPQW TDHIVQSFVH GANAAIAHLL FEAVLTSPDS SSRPQAGRPF TVTDPNPPIT
YGDLYYALSL LAITGFRTLR LPPMLLLLPS YIVEWYTLLL ARFKVARVLL PSAKGDIQHL
KPALFSITTH LVATNAAASR PVEQGGLGYR GVLTSMDGMV QEVVEWNREH MDSSKPRKTY
RTSVSFADDI QRLSSAATSV GALQLRD
//
