ID Q0CF36_ASPTN Unreviewed; 514 AA.
AC Q0CF36;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=ATEG_07698 {ECO:0000313|EMBL:EAU31960.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU31960.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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}.
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DR EMBL; CH476604; EAU31960.1; -; Genomic_DNA.
DR RefSeq; XP_001216319.1; XM_001216319.1.
DR AlphaFoldDB; Q0CF36; -.
DR STRING; 341663.Q0CF36; -.
DR EnsemblFungi; EAU31960; EAU31960; ATEG_07698.
DR GeneID; 4322554; -.
DR VEuPathDB; FungiDB:ATEG_07698; -.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_10_1_1; -.
DR OMA; VVCCRAH; -.
DR OrthoDB; 1094055at2759; -.
DR Proteomes; UP000007963; 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 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; 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:UP000007963};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..514
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005692720"
FT DOMAIN 60..235
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 514 AA; 55097 MW; 41ECA10AF42CF6E3 CRC64;
MATKLVATLA FASALISASA ARDALLPSSL QTCLRNTGAK IVYPGDQSYD ALAQPQNSNY
QAHPEVIVVP TSAEQVSATV KCVAAEKGNV KLSPRGGGHS YAAYSFSGQV VIDPSQMKGI
SIDSEKSQVT VQFGQTLGPL ATAIGKKGFA LPHGTCPTVG VAGHSLGGGW GFPSRKWGWL
VDRIVALEFV DVNGAIKQLS ASSVGSDAEL WWALRGAGSN NFGIVTAFTF AMEKAPPATV
NYELYFGPES DCAQVLLQVQ ALGQLPADDP NGLPLDLGVE VLLMGRDNSG DSACILQGQY
LGTKSAYQTA INRVLRKLAT QGIKPVESES MVKVFSNWIS ALTDLMGPLD ASNDTLPYYA
QSLVDSGSPS YQKSHITKVF DGLRTARTVK HSEPDVSFDL LGPSAKTNLP VASGPMAYIH
RKSLFLVQIY SAYFPGFGDL AAREKAVNQI TNITRAMRQA RPESEWHSYQ NYVDPYLKDF
GREYYGDGLE RLKTLKTAAD PNLIFDFPQG LAHA
//