ID A0A135L942_PENPA Unreviewed; 388 AA.
AC A0A135L942;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase, class-II {ECO:0000313|EMBL:KXG45485.1};
GN ORFNames=PGRI_040340 {ECO:0000313|EMBL:KXG45485.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG45485.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG45485.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG45485.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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:KXG45485.1}.
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DR EMBL; LHQR01000071; KXG45485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135L942; -.
DR STRING; 5078.A0A135L942; -.
DR OMA; NNPTRHM; -.
DR OrthoDB; 2069230at2759; -.
DR Proteomes; UP000070168; 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:UP000070168};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..388
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007800313"
FT DOMAIN 29..168
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 388 AA; 43137 MW; 74F2799FA27150F0 CRC64;
MLLTWNWKKL FAVQALLTLV WAQAPQQDYD VIVIGGGPSG LSAASGLSRV LRKVALFDSG
EYRNNPTRHM HDVIGSDHVV PAEFRAAARK QISFYNMTTF FDQKVISIQK VENSFHATTA
NGTYTARKVI LASGVKDDLP NVPGLREAFG KGVFWCPWCD GFEHRDQKMG VLGDFSDAYD
SVKELYPTLN KDIRIYANGT NNNPAQINRI NSKNIDWQKV FNKYNITVNP KPILNITRTQ
NGGDVHDSTR KEFDKFLVYF TDGSYEERDA FMVNYGASQA SQLPYQLGVG FLGKKINTTA
PGLRTTIPGV WGVGDANSDN STNVPHAMAS GKKAAVFCHV EMATEELAQV SATQAKRAAM
LDDRSVHERA ARQMGDEVGK VYRRLAHF
//
