ID A0A150VBV7_9PEZI Unreviewed; 577 AA.
AC A0A150VBV7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=M433DRAFT_2375 {ECO:0000313|EMBL:KYG47999.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG47999.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG47999.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG47999.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:KYG47999.1}.
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DR EMBL; JPDO01000060; KYG47999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VBV7; -.
DR STRING; 766039.A0A150VBV7; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
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:UP000075602};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..577
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007571506"
FT DOMAIN 125..304
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 577 AA; 62843 MW; BEF08B7015AF65F9 CRC64;
MPFISIRLAI ASVLCSSAVL AASLHQRRGS SEAECRCFPG DACWPSMQEW DDFNRTLGGK
LIATIPLASP CHNDNFEPYN NATCTTLQNE WLLPQTHYVS SSSIMAPYFA NRSCDPFTGR
DFECVIGTYI QYAVNVSTAS DVSAGIKFAI KHNIRLVIRN TGHDYNGKST GAGALGLWMH
HLKDITFSDW SDTYYTGKAI KMGAGVQGFE AYQAANASGL QVVGGECPTV GIVGGYTQGG
GHSALASKHG LAADQTLEWE LVTGTGEHLI ANRHQNTDLY WALSGGGGGT YGVVLSLTAK
AHPDTPTSAM NLTFTSANTS QDNYYEAIST FHASLPPLVD AGGMSVWYFT NESFAISPIT
GPGISVPQLK KFLAPLMDKL DQLGIQYTSY FGQFSGYLEE YNAMQGPIDV GIAQYGGRLI
PRSLVENNNT ALTEAYRFIN NHGGQFIGVG VNVSKAVAGN VYNAVNPGWR TTLIDTVITT
PWNFTAPWQE MIANQNLMTD VLLPPLEALT PNGSCYLNEG NFRQPDWQSV FYGENYDRLL
EIKNKYDPYH MFYATTAVGA DYWEVQPDKS LCKAKSA
//
