ID M4BTQ1_HYAAE Unreviewed; 522 AA.
AC M4BTQ1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP809836, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP809836}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP809836};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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; JH597858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4BTQ1; -.
DR STRING; 559515.M4BTQ1; -.
DR EnsemblProtists; HpaT809836; HpaP809836; HpaG809836.
DR VEuPathDB; FungiDB:HpaG809836; -.
DR eggNOG; ENOG502QVWT; Eukaryota.
DR HOGENOM; CLU_018354_10_1_1; -.
DR InParanoid; M4BTQ1; -.
DR OMA; WASEDIT; -.
DR Proteomes; UP000011713; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000011713}.
FT DOMAIN 75..247
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 522 AA; 56587 MW; B19366BBC61FFA8A CRC64;
MVATMSDTRR LIFALCSFIA AQSNIAASAL VKDGLALPQS SAAGIGACLK KAGIENSMPT
TSTWTVDTEA WNSRVSPKPS AVAFPKTEEE VSAALKCAAA NGVKVTTLGG NRSFSSMGFG
RNDGALVMNL KYFKHLEYDE STQLLSYGGP VMISEAANFM WNKYQRTLPH GRCPDVGMTG
VAASGFGTLS RASGTVLDNL VSVRVALANG TIVNADAKHN APLFWGIRGA ASSLGAVLDF
KIKTLAPPSK RATNYTISFG KSYEATQQDN VDALIGTQKW AQSKDNNDLL SIRFGLKKSS
TLQGFFYGSS AEAAKVFASL KKYLPAAMNV STTENDFWAS EEITTPGLVK QTLTPRRYFY
ITSVTIPSNA PLTNATAWEL FSNTAFAPKL PDASASGFVD FWAGEFAKTV RSGDSAWKHN
DNLLLVRWDM RSSAFNVPFA ETSLDNMRTN FYKFVNAYKA SGGKPGGFTT YRDEKWTTAE
MAEYLYGGGN YAKLQKIKTE YDPNELFNTD AQAIRALKKK TK
//
