ID F9XFD2_ZYMTI Unreviewed; 556 AA.
AC F9XFD2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=MYCGRDRAFT_45413 {ECO:0000313|EMBL:EGP85636.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP85636.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP85636.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CM001202; EGP85636.1; -; Genomic_DNA.
DR RefSeq; XP_003850660.1; XM_003850612.1.
DR AlphaFoldDB; F9XFD2; -.
DR EnsemblFungi; Mycgr3T45413; Mycgr3P45413; Mycgr3G45413.
DR GeneID; 13397398; -.
DR KEGG; ztr:MYCGRDRAFT_45413; -.
DR eggNOG; ENOG502R8I5; Eukaryota.
DR HOGENOM; CLU_018354_4_2_1; -.
DR InParanoid; F9XFD2; -.
DR OMA; RNAISHM; -.
DR OrthoDB; 1641938at2759; -.
DR Proteomes; UP000008062; Chromosome 7.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 2.
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; PTHR13878:SF179; FAD_FMN-CONTAINING ISOAMYL ALCOHOL OXIDASE MREA (AFU_ORTHOLOGUE AFUA_6G03620); 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT DOMAIN 103..283
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 556 AA; 60401 MW; D2302D3598F2F0C8 CRC64;
MQTVLKGEDV SSCRCFPGDS CWPTPQDWAI FNSSVGGRLV ATVPLAAPCH HSSFAPYDAA
ACSRLQEEWT SPHIHYTSSS SVMAPYYANA SCDPFLSAES PCVFGTYSRY AVAVHSPADA
IRTIQFAHDR DIRLVIRNTG HDWSGKSTGA GSLAIWTHHL KDINVCDYVS PQYTGKAMKM
GAGVQAFEAY AAAHASNVVV LGGECPTVGL AGGYTQGGGH SALSSRFGLA ADQILQWEVI
DGTGRYLIAT RDNDQQDLYW ALSGGGGGTY GAVLSMTVKA HPEMHTTGAK LKFSRQGTSA
GRYWQAVEGY HQTLPDIVDA GIVSIAQFDK DSFAINPITA PGVTESRVRE LLSPLVSKLE
ALGIGYELDV RQFPTYFDHV QAMFSPIGTA SFQYGSRLIP RASIAENNSA LTQAFVKAAE
DGCSFFSVAL NASRPGEEAF NSVSPVWRST LLHAVIQVAW DPLAPWTAME RRAAMITSEY
VREFEAVAPD GGAYINEADP RDPNFKQNYY GGNYDLLLRI KDKYDPFQVF YALTGVGSHR
QYVRPDGRLC SRTQDP
//
