ID S7QCL2_GLOTA Unreviewed; 358 AA.
AC S7QCL2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=DUF1295-domain-containing protein {ECO:0000313|EMBL:EPQ57087.1};
GN ORFNames=GLOTRDRAFT_73635 {ECO:0000313|EMBL:EPQ57087.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ57087.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ57087.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ57087.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KB469299; EPQ57087.1; -; Genomic_DNA.
DR RefSeq; XP_007864239.1; XM_007866048.1.
DR AlphaFoldDB; S7QCL2; -.
DR GeneID; 19308366; -.
DR KEGG; gtr:GLOTRDRAFT_73635; -.
DR eggNOG; ENOG502RWJV; Eukaryota.
DR HOGENOM; CLU_043418_2_0_1; -.
DR OMA; LNAWWSA; -.
DR OrthoDB; 38588at2759; -.
DR Proteomes; UP000030669; 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 Gene3D; 1.20.120.1630; -; 1.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR010721; UstE-like.
DR PANTHER; PTHR32251; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE; 1.
DR PANTHER; PTHR32251:SF15; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE (DUF1295); 1.
DR Pfam; PF06966; DUF1295; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 201..272
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 40142 MW; 0A57286EA24EA39E CRC64;
MAINFPQTYP SPPSINPNQH APPLNPDPHF PPPPRPTWSS FSRPLYTSFL LHSGLAVSTH
ALAAVATNYR LDAKDVIWPG GMLLDAWYQS VGVPVIWGGR SVGDVISGFG WRESLILGGI
TTHSLRLMYH LWKRAYKRGH DDIRYAYKKT EKSNWYLRSL VTDYLPEALF QTLICLPFTS
PFRYEPAPGY SATWNWTDSL AVFLWTAGFA METLADYQLS KAKKSGKTQG HLMTEGVWSI
VRHPNYLSNI LTHVAYPLLL VSTPLSHPAL VLGPLANYVF LRFFGGDALT ETYQEQHYAE
AADYTKLGDL QEYRHTRNAV WPGLEAVKQG WTWAVVGLGA AGVVLERGLR AWAAPRVL
//
