ID W9WJ39_9EURO Unreviewed; 498 AA.
AC W9WJ39;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=A1O5_09265 {ECO:0000313|EMBL:EXJ67918.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ67918.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ67918.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ67918.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:EXJ67918.1}.
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DR EMBL; AMGX01000015; EXJ67918.1; -; Genomic_DNA.
DR RefSeq; XP_007748034.1; XM_007749844.1.
DR AlphaFoldDB; W9WJ39; -.
DR STRING; 1182543.W9WJ39; -.
DR GeneID; 19193961; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_10_0_1; -.
DR OrthoDB; 1068078at2759; -.
DR Proteomes; UP000019471; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019471}.
FT DOMAIN 49..221
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 498 AA; 53121 MW; 01DA0E9E20EE6EEB CRC64;
MGSLTQSSKR SITGEDISSL KSLLSSTNAT VLTPQDEAYG TSIKRWSSAA QKPAGVVVVP
TNADEVASVV KYATDHGIDL AVKGGGHSTA GVSSTDGGLL IDLNSKMRHV DVDLDKKLFI
IQGGAAWGDV DQAGVKHGLA TVGGTVADTG VGGLTLGGGY GWLSGQKGLA IDNLVECTIV
LATGEIKKAS EQENPDLFWA LQGAGQNFGV VTEFVLKAYD QGDVFAGMLI YPPTPEIIEK
VVAATNDLYT PDANGKTKVA GRGAGGIAFA RPPPAEGKVM LMAVIIYFGT EAEAKEKYKA
LYDIGPVVDT TAMVSYPVIN TILAPPIGLR ASMKGTSFTM PIRAGFVEDV LREYTKFTDG
NDDTGISLVL WEVYDPNQVV AHDEVGSFAN RGWHLNGMIC PIWTKQEHDQ ACRQWARDMT
ALFKTELEAQ AKTTGTGVDG GVGLRGKKGA TMLYGNYDQY DEKSRDIFGE NYPRLQQLKA
RYDPTNMFNK LFGVTPLA
//
