ID A0A067D885_SAPPC Unreviewed; 490 AA.
AC A0A067D885;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=SPRG_00048 {ECO:0000313|EMBL:KDO35202.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO35202.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO35202.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO35202.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583189; KDO35202.1; -; Genomic_DNA.
DR RefSeq; XP_012193554.1; XM_012338164.1.
DR AlphaFoldDB; A0A067D885; -.
DR SMR; A0A067D885; -.
DR STRING; 695850.A0A067D885; -.
DR EnsemblProtists; KDO35202; KDO35202; SPRG_00048.
DR GeneID; 24122709; -.
DR KEGG; spar:SPRG_00048; -.
DR VEuPathDB; FungiDB:SPRG_00048; -.
DR OMA; HAMSHRE; -.
DR OrthoDB; 1094055at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
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 Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
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 Reference proteome {ECO:0000313|Proteomes:UP000030745}.
FT DOMAIN 65..234
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 490 AA; 53716 MW; 792C7D2F572D38FC CRC64;
MGGTCTKVSA ASLGGRDAGR TRSTAANIEK YGRFLQEIPV DGTVVLASMA EEYQRLRSSA
YAFVDCGYPF AIFRPLHARD IALFLQAVGH LKLHIAVAGG KHSALCLPDN SVVIDLHYLS
DIRVNAEDKY IDIGGGARMG AADAELRGSG LAFVGGTHPD TGVGGFAQTG GWGWLSRQHG
LAVDHWLEAD VVLANGDIVT ASDSNEHCHL MRALRGGAGN FGVVTRFRFA LHRIDRCHYS
TPLRFCPTIV SAKKTAKAFR DRMDAAPTYA SGMLVLHCGK PLVSQVITAI GDANVVTDTT
WIDDMRHLDG GQWATLRASR RDGGYHLGLQ SVLEPLTQRG HTMTTSYFVK DLSDAVLSVL
VRYTRVQYPG ARSVIAAAAW GGQIPLEGRP HAMSHRENGW WILVHAVLPD MSWYQVTKHK
QWVLAVKVAL QDVDNSAMQA PHVSFDTITR NATAKTRAFD DVTHLFLRQV KTEYDRKNVF
HMNHNIRPLV
//
