ID V2WKB2_MONRO Unreviewed; 402 AA.
AC V2WKB2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Alcohol oxidase-like protein {ECO:0000313|EMBL:ESK80620.1};
DE Flags: Fragment;
GN ORFNames=Moror_9184 {ECO:0000313|EMBL:ESK80620.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK80620.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK80620.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK80620.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:ESK80620.1}.
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DR EMBL; AWSO01003239; ESK80620.1; -; Genomic_DNA.
DR RefSeq; XP_007860074.1; XM_007861883.1.
DR AlphaFoldDB; V2WKB2; -.
DR STRING; 1381753.V2WKB2; -.
DR KEGG; mrr:Moror_9184; -.
DR HOGENOM; CLU_002865_1_0_1; -.
DR OrthoDB; 2418107at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 52..75
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 223..237
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESK80620.1"
FT NON_TER 402
FT /evidence="ECO:0000313|EMBL:ESK80620.1"
SQ SEQUENCE 402 AA; 43999 MW; A834750CBB874134 CRC64;
ILEAGEHTKG LDAHVQPARY FSHLAPTSKT VTFNIGKPSE YIGGRSLVTP SGRCLGGGSS
VNLTMYTRAA ASDYDDWETV FRNNGWHSKD LLPLKKTETY QVEPNQDTHG YDGPLKVSLG
GTITNVGKQF MDIALKIDKD RGPIHDVNGL DTGRRSDVPH HYIYNQEHNK NLAVLTGKRV
KRVIFEGNKA VGVEYVNDTV LNPDADQTVE IAKADKLVVV SAGAFGSPTI LERSGIGGSE
ILKKHGVRVK VDLPGAGENY QDHNVCFIPY QASDEAVTVD ALFRGDEAEV NNWLAVWSEG
KGLLAHNGLD AGIKMRPTAE DLKELGPEFE HRWKSYFENA PDKPVIWVGA VSCNLVDPAV
ATPRKYYSVG YFTQYPVSLG HVHITSGDDA NASHDFDPNF LA
//
