ID E6ZPG3_SPORE Unreviewed; 587 AA.
AC E6ZPG3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Related to 6-hydroxy-D-nicotine oxidase {ECO:0000313|EMBL:CBQ69120.1};
GN ORFNames=sr00094.2 {ECO:0000313|EMBL:CBQ69120.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ69120.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ69120.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; FQ311434; CBQ69120.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZPG3; -.
DR EnsemblFungi; CBQ69120; CBQ69120; sr00094.2.
DR VEuPathDB; FungiDB:sr00094.2; -.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_10_1_1; -.
DR OrthoDB; 1094055at2759; -.
DR Proteomes; UP000008867; Chromosome 13.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..587
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003216850"
FT DOMAIN 76..252
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 550..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 63994 MW; 5707B36D94DB0517 CRC64;
MRLAALYRLV LGASTLFSVA RASHAPNDNT TILQPRVVAA TRLQRCLGEA GIEVVAADVS
TAEVYFQASA SDNVVFHYNP TLIAYPSSAS LVQQAVVCVS EHSDAPIAAR SGGHSFAGFG
SGGMDGSVVI DLARLNSVVS HPQSGTVEVG PGARLGDVVK GLWHQGNGQR AMSTGTCAAV
GVGGLSLCGG FGPMSRKWGL TTDSILEADL VLANGSMVTV SESQHPELLW ALRGSGSFFG
IVTRFLFRSQ DASPPVISFE YRWTPSIDSL DKTIAVIMAV QAFSLQPSLS NDLGLHIQLR
RPSHGDPQPS ANRPISIEVK GIYLGPVAEW DKLQSALKGE LRSRSAPRAD VEKVSLRTYL
ELMEEWDDFG KGEHKLDTEA IHKQHNNFVT KSSLTLEPNK GFDEQALRPL FQYLWDTSLS
AGQDVNLPNG KHVFWGWNIY FELFGGGTPA HAQPKAKKLS SFPHRDGLWL IQVAVGTVSY
MDLAHSGHVY ARELDARVNG AIEASGLGRG GYSCYVDSDL NEDEWKQLYY GDSIPRLEEI
KMQLDPQNLF RNPQTLGSRR DIQARRKAAR RRRRRGQPMD TDSLLIA
//
