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Database: UniProt
Entry: A0A094D1Y9_9PEZI
LinkDB: A0A094D1Y9_9PEZI
Original site: A0A094D1Y9_9PEZI 
ID   A0A094D1Y9_9PEZI        Unreviewed;       563 AA.
AC   A0A094D1Y9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN   ORFNames=V493_02753 {ECO:0000313|EMBL:KFY28812.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY28812.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY28812.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily.
CC       {ECO:0000256|ARBA:ARBA00023445}.
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:KFY28812.1}.
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DR   EMBL; JPJV01001027; KFY28812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094D1Y9; -.
DR   STRING; 1420906.A0A094D1Y9; -.
DR   HOGENOM; CLU_419304_0_0_1; -.
DR   OrthoDB; 552946at2759; -.
DR   Proteomes; UP000029327; Unassembled WGS sequence.
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   InterPro; IPR001763; Rhodanese-like_dom.
DR   PANTHER; PTHR10366:SF562; ALDEHYDE REDUCTASE II (AFU_ORTHOLOGUE AFUA_1G11360); 1.
DR   PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029327}.
FT   DOMAIN          219..286
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   563 AA;  62563 MW;  E6AB069BE337080E CRC64;
     MARQFQFVTV SNPTGPVSSE SRKLTHSYVM RQSHAKKRRL QTQRYQIESI ICGTKQDLTI
     FKSALSSPLN HVSTNGKDPF LSLARPLTSE EYFLLDHYIQ VVVPYSVGHC GLFENPGDHR
     TQMLREWVGL AIADDALMVA AVLLSTCRYI LLDQPDHPVF TRMALQYKQI CLRTLRQEIS
     TKSSPINAMT VAKAVALAID ENISIHRIHI GIDIFCYNIM SSLATTIPTG SWVLVTGASG
     FLATHVIWQF LNRGFRVRGT VRDVRQCQWL LGGRFKTYAE NGALELVAVP DLSVDGAYDE
     AIKGVAAILH IAYVTRIVPD PNEVITPSVA GIRSIINSAV QESSVKEIVF TSSALAASSL
     TQDIDNGMVD RTSWNDAALE AAWAPPPYGM SHAMANYPAS KVAAEKQVWR FVENKLPFTV
     NVVSPAGITG EPMNRKHIEG QANWVVHAFR GNKSVMDPMQ ASFYADVKDL ALIHVAAILD
     PEVKNARLQS WGHSTHWNDI LAILRAYRPQ KKFIDDYPKP YHLKVSVDQS ESLALLRKWS
     GKDGWTSLED SISENITNSC LSD
//
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