ID V2XRP7_MONRO Unreviewed; 350 AA.
AC V2XRP7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=3-beta hydroxysteroid dehydrogenase isomerase family protein {ECO:0000313|EMBL:ESK95541.1};
GN ORFNames=Moror_12727 {ECO:0000313|EMBL:ESK95541.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95541.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK95541.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95541.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK95541.1}.
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DR EMBL; AWSO01000075; ESK95541.1; -; Genomic_DNA.
DR RefSeq; XP_007845202.1; XM_007847011.1.
DR AlphaFoldDB; V2XRP7; -.
DR STRING; 1381753.V2XRP7; -.
DR KEGG; mrr:Moror_12727; -.
DR HOGENOM; CLU_007383_9_2_1; -.
DR OrthoDB; 1435983at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10366:SF564; 3BETA_HSD DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:ESK95541.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 12..257
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 350 AA; 37845 MW; 1F7C23B2648BAD7C CRC64;
MESQPSARPY RVLITGVTGY VAAHIAQRAL DSGYLVRGSV RSQVKAAAIQ ELFSSYGDKF
ETVLIPDIVS GDLSQALQGV SAVVHVASPV IFGPVSNPKS QLLDPAVEGI LNVMHAAHRA
GVKRIILTSS LGVVLNKSIG GPWVDRTYGP DDWNSITYEE ALSGNLLPIE IYACSKTLQE
KAAWSFVEDH PEMELTTIIP PMLVGPAIQP LQSMDSLNDT AVVIWDMIGK GILHPDALPY
YCDVRDAATV HIEALTKKTV IGKRLLAGKE RGSIWKAAKI ITERRPELAQ AGRLPSLPPV
DPTAGLPVCT LDTSIVDKEL GVKFRSFEES VLDMVDHLLS VEAKLKRAGK
//
