ID A0A2H3IGL2_9EURO Unreviewed; 559 AA.
AC A0A2H3IGL2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase, dimerization {ECO:0000313|EMBL:PCH02577.1};
GN ORFNames=PENO1_037210 {ECO:0000313|EMBL:PCH02577.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH02577.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH02577.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH02577.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCH02577.1}.
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DR EMBL; NPFK01000081; PCH02577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IGL2; -.
DR STRING; 290292.A0A2H3IGL2; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 470..557
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 559 AA; 62096 MW; DF08CD1DAFAEFE0B CRC64;
MSEDRSLRII VVGGTAAGIA AAVRCRRLDE RASITIIEKE SYVSHANSGV PYALEGVIEK
DTTLVQQTPA GLKARFNLEV HINTELISIS KEEHMVVVQS LDSKNSYNIR YDKLILAQGA
EPAQLQIDGL ENVQNFFTMR KQMDLKRIKD YVVRHECQTA IVIGGGFIGL RAVEYLRHLG
LQVSLVESND QVYCTFDKDI AHYLETELQF NNVHLYLGMR AERYMRNEVE DCSCIQLSDG
STVSSDLFVT AVGLNPRVTI ALNAGLAVKR GVVVNTFMQT SDPDIYAVGN MVETENRLAH
SPSILALGGP GSRQGRLVAD HIYKRASVYS GDVGTTISRV FRLTAGITGM PIQKLRSIGY
NPLWVTIHTP DHEGYYPASS HLTLRIIFEA YTGRLLGAQA VGKVGVDKRI DVLSTALQAS
MSVFDLEQLE LSYAPQYGSS RDPVNLAGCT ASNVVRRDLY VLHPDELVGH TSKWQIIDVR
RAEDYSKDHV LDAENIPIDK LRQDIASIKK DPPVLVYSRV GYHGYIAYRI LKQLGYEAAS
LDGGWKLWQS GGYQARMQK
//