ID A0A0D2ATQ9_9EURO Unreviewed; 608 AA.
AC A0A0D2ATQ9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=PV08_11073 {ECO:0000313|EMBL:KIW10113.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW10113.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW10113.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW10113.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KN847500; KIW10113.1; -; Genomic_DNA.
DR RefSeq; XP_016230329.1; XM_016385385.1.
DR AlphaFoldDB; A0A0D2ATQ9; -.
DR STRING; 91928.A0A0D2ATQ9; -.
DR GeneID; 27338156; -.
DR VEuPathDB; FungiDB:PV08_11073; -.
DR HOGENOM; CLU_024402_0_0_1; -.
DR OrthoDB; 5474593at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT DOMAIN 108..295
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 68485 MW; D1F17F1470998A3B CRC64;
MGTSNISLSK DVPVYPLDYS GIPERLVTKV ARERDRLSKN QTKGRTSERK RGIAIPQGVS
KDQFFKAVEE LSGFIGEANV KINDQPLEDG WYMEHPNTHD AFMILDGEET VSSAAVYPGS
VQEVQTVVKW ANKHLIPIYP ISMGRNLGYG GAAPRVRGSV VVDLGRRMNK ILDINPDDCT
CLVEPGVSFY ALYEEIRKRG YKVWIDCPDL GGGSILGNTL DRGVGYTPYG DHWGVHSGLE
VVLPTGELFR TGMGALPGNN TWQTFPYGFG PMSDGLFSQS NFGVVTKIGM ALMPDPGEHE
SFMYTFQEED DLQLLVEIIR PLRIANILEN VAQIRHSIIE VAVGGGSRKE FYDGKGAIPD
NVLQKHLEST PLGRCTWIYY GTNYGPKQIR QYKLDIIHKE FMRVPGARRI DPDSLPKDHY
FWSRDRIASG EPDFEELSYL NWVPNGAHMG FSPISPTRGP DALKLWKIAK ERHHQHDIDM
FLAFVVGLRE LHMIVLVIWD RDDPERRKAV DRCMRQMIDD CAKQGYGEYR THILFQDQVA
ATYNWNDGAL MKFNEKLKDA LDPNGIMAPG RCGIWPARYR GRGWEIGKEG RDTYEGDGVH
PPTGSIQM
//
