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Database: UniProt
Entry: A0A423VH43_9PEZI
LinkDB: A0A423VH43_9PEZI
Original site: A0A423VH43_9PEZI 
ID   A0A423VH43_9PEZI        Unreviewed;       505 AA.
AC   A0A423VH43;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=VMCG_09711 {ECO:0000313|EMBL:ROV90349.1};
OS   Valsa malicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV90349.1, ECO:0000313|Proteomes:UP000283895};
RN   [1] {ECO:0000313|EMBL:ROV90349.1, ECO:0000313|Proteomes:UP000283895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-1 {ECO:0000313|EMBL:ROV90349.1,
RC   ECO:0000313|Proteomes:UP000283895};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:ROV90349.1}.
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DR   EMBL; LKEA01000063; ROV90349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423VH43; -.
DR   STRING; 356882.A0A423VH43; -.
DR   Proteomes; UP000283895; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13789:SF306; HYDROXYLASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283895}.
FT   DOMAIN          80..425
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   505 AA;  55050 MW;  85F61B8F0DEAF250 CRC64;
     MPMATSLSMA SLSSNEARDN TVALTNGNSG SSDGGYEEWE VPKFTTTSYP SNCLRFLQNV
     NYPGATYDET PTQARAKLCI LVVGAGLGGL ATAVALRRRG HQVTVFEQAP ELMEVGAGIQ
     VPPNSGKLLE RWGVMNRLVK RAVQPANINF RRWQNGAIIG VTDLSSDFGA QYGAPYYVVH
     RAHLHAALYE QAVDLGVKMR LNSKVDAYDT DTGSVVLSDG NTFQGDLVVA ADGVKSLARS
     LVSPSGRGVP KYTGYSVYRA TVDVEKMRKS HETSWVLKQP NLNLWIGDER HVMTYCIAGG
     QSFNMVLSHP DRGNPSLPSS EAGILANMRK EFGGWDPYLT AIIDLIDKVM KTPLMSGAAL
     DKWVAPSSKL VILGDSAHAM LPYMSQGAAM AVEDGAALAV VLNQITSPKQ LKFALKVFEN
     ERVKRTSMMQ EASLVNSMIW HFKDGPLQAA RDFAMSSEVD GKHFASSPNQ WSDPATQVWA
     YGYDAERVMK EAWDKAVHDL IAYQG
//
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