ID   Q2H7E6_CHAGB            Unreviewed;       733 AA.
AC   Q2H7E6;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=CHGG_05419 {ECO:0000313|EMBL:EAQ88800.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ88800.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH408031; EAQ88800.1; -; Genomic_DNA.
DR   RefSeq; XP_001221514.1; XM_001221513.1.
DR   AlphaFoldDB; Q2H7E6; -.
DR   STRING; 306901.Q2H7E6; -.
DR   GeneID; 4390232; -.
DR   VEuPathDB; FungiDB:CHGG_05419; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_378112_0_0_1; -.
DR   InParanoid; Q2H7E6; -.
DR   OMA; MLITFEY; -.
DR   OrthoDB; 1820950at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR002563; Flavin_Rdtase-like_dom.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   PANTHER; PTHR43812; BLR2425 PROTEIN; 1.
DR   PANTHER; PTHR43812:SF2; FLAVIN REDUCTASE LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF01613; Flavin_Reduct; 1.
DR   SMART; SM00903; Flavin_Reduct; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..733
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004208597"
FT   DOMAIN          54..215
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          597..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  78986 MW;  401F92641664AF3A CRC64;
     MVRPRALLGA VLLACNVNAA PDYTDVCQDI AGQLSEAIQV LRYTTATQHW FRSSNGDAAC
     VVEVGSVEDI SLVLEIVGAS STPFAVYSGG HSSNPGFSST TGVHITLKRL NQVDLSEDKT
     IVTLGFGQGW ADVYDALDGT GVSVVGGRVP GPGVGGFTLG GGYSWSHLRH SQVFQRGASV
     TTASDDQNQD LFFALRGGLN RYGIVTSAEF YTHPQPAQVW GGLRAYPSSQ IPALLNATQR
     FFEESKDPKA QIITTLDGGG LGVTSLTLFF YDGPEKPEIF DMFDGLLTTL DNTGKKSYKN
     LVNSFPAEIV LNARGTFGSF STTRLTNRFI EAVKQEVEDI GKTSALHGGT MVSYEIEPFI
     DYGKHAKPGA FPHADSLLPL NLYFAWAKQS DDEWWYATAR QSLARLKEVA KEEGIYEDTF
     LDYSNYVFAD TPAEKLYGVE NTARLRQIRD QIDPDRIMDL AGGTMFYQPG KTPHNLPYDP
     FKACVIPRPI GWISTTSPLP AATAQHPNPQ PTHNLAPYSQ FAPLTFDPPY VLFSANQASH
     SGAGARKDTV RNVEATGKFA WSLATYALRE AVNVTAKPVG YGVDEFGVAG LEKEFSTVLP
     GDGGDDEGGE GGNAGRGKGN PVPMVKASPV KFECVYHSTV RLPGYGPVGS VDLVIGRVVG
     VHIAEWALDG EGRLDVRKTR PIARCGYFEY AVVGGEGTIF EMVIPGADEV MLAALQGDKK
     GVDEGLKKVK AKL
//