ID A0A010RBQ0_9PEZI Unreviewed; 397 AA.
AC A0A010RBQ0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN ORFNames=CFIO01_06122 {ECO:0000313|EMBL:EXF75164.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF75164.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF75164.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF75164.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:EXF75164.1}.
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; JARH01000924; EXF75164.1; -; Genomic_DNA.
DR RefSeq; XP_007601158.1; XM_007601096.1.
DR AlphaFoldDB; A0A010RBQ0; -.
DR STRING; 1445577.A0A010RBQ0; -.
DR KEGG; cfj:CFIO01_06122; -.
DR eggNOG; ENOG502S1DJ; Eukaryota.
DR HOGENOM; CLU_031864_5_0_1; -.
DR OrthoDB; 2069230at2759; -.
DR Proteomes; UP000020467; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0097237; P:cellular response to toxic substance; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR PANTHER; PTHR48105:SF29; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..397
FT /note="FAD/NAD(P)-binding domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001456884"
FT DOMAIN 28..161
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 397 AA; 42929 MW; B3CF4E0859A27DF0 CRC64;
MKFTLSSLVL SAASSLVAAL PINDTQVYDA IIVGGGPSGL SAASALGRVR RNTLLIDSGE
YRNAPTRHMH DVLGFDGVTP AWYRYAARQQ ISHYDTVTLT NGTVTKIGGN DATGFVVSAT
YADNSTKSVR ARKIILATGL QDDLPETPGL WENWGKGIYW CPWCDGHEHA DQALGLLAST
FDDLPSLVRE ILTLNTDIIA FANGTDTPAA RAETEAKNPK FQEYLDLHNV TIDNRTITAI
TRLKDGGNPP HDPSLPTAPE EDLFSVSFSE GEPVERAAFF LSYPDEQRST IGAEAGVQLW
GGRLAADVSK GYATNVAGIY AIGDANSDNS TNVPHALYTG KRTAVFLHVK LAKEDQAKET
GVNVTALRRE LDLEERSIWD VANGQPTDIL YAGEYDQ
//
