ID   Q2GWE0_CHAGB            Unreviewed;      1318 AA.
AC   Q2GWE0;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAQ86461.1};
GN   ORFNames=CHGG_07714 {ECO:0000313|EMBL:EAQ86461.1};
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:EAQ86461.1, 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 GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CH408033; EAQ86461.1; -; Genomic_DNA.
DR   RefSeq; XP_001225370.1; XM_001225369.1.
DR   STRING; 306901.Q2GWE0; -.
DR   GeneID; 4393142; -.
DR   VEuPathDB; FungiDB:CHGG_07714; -.
DR   eggNOG; ENOG502QSPJ; Eukaryota.
DR   HOGENOM; CLU_002483_0_0_1; -.
DR   InParanoid; Q2GWE0; -.
DR   OMA; PTGMYHL; -.
DR   OrthoDB; 1945480at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT   DOMAIN          231..374
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          571..636
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1318 AA;  145246 MW;  3803A2B60CC7D759 CRC64;
     MDKSSARNPS GSLQVNGLLS PPLTPDPNHR ASNAMGIIDG AFDDVRPPSP NPSVSSSTGF
     SSDPRTSSTF TATSQTSSHT AASSPDLSRD DPHPLPPNYA VHDEHEYNNN NNNNKPSLTT
     ATATATSPTS PISPAAHRAS TKPRPYTDGR QDAPFPRLSK PVELLRSAYD VVVIGSGYGG
     GVPPSRKART GVSLFACSSA AREKWPGRST PAGAIDAGEG AAIIRACSRP GLGGTSLINA
     NVFMEADKET LAMKAWPPEI RENVEELDKY YKKVEEVLDP QEYPAEWPEL PKAKLLQKQA
     ELMGLGGKFK KVRQTTRFIN GPNSCGVEMS PSSLTGQDAT GVNDGSKNTT LVTYIADAWN
     WGAELFCECE VRYIEEDKNG EGYLRLWGLS TWCLTSNSYN TDETANAIGQ ECPSPYHPIG
     PTITSVIDCR EDETKPDFNP LDGFVLEEGA IPHALAPLFQ AMIDLMPGKK DPQNDTLIEK
     TQAALARYSS RFLGPYYKNG AVQKTQVYLI MSHDSNQAVL SLKDDKPMLE FLGVARGHHV
     KKLNKLLERA TEVVGGTLVQ SPFYELLGQQ VTVHPIGGAC MARDNTGKTG VTNHVGKVFR
     GRNGETHDGL IVTDGSVIPT ALAANPFATI AALAERSVEA YAKSQGLTIS EEKNAILDLL
     GEPQHKPKRM RPSHKREQIN VLEEQDSISV ANKVIRSARD VSASGIGFTE VMSGFIHPDE
     DLKEDNKDTY ELAHRMAKSL CESARFFLSV QAFNTKEMVN HAQHRGMLTG TFVCPAIRGS
     PFMVQRGEFN LFILNNKAPG TRNLTYDFDM TGVDGRKLHF HGYKVVDSSV ALAPFQFWKA
     TSTLYVTISQ HVPYMCADLD DEDAWRRAPV IAKGIMHIQP ADFFSQINTM TPTGSNLLKK
     AISAVRFLTY FTRKSLSLFL SPLTPLEYPT KTFSGFINHT PADKSVEILA SDGVSSRMHI
     WEPTHVPGND PKNIRNLFMI PGASVDHQIF ALPTIPYNAV NYLTRAGYRV FVSVHRISQL
     MIAGSNWTTY DARLDLKACL EHIRDVYGPE KIYTIAHCMG SVAFASGLLD GTIPASWILG
     ITCSQVFMNP VWGPTNMAKV MAGPLPMDRL YDLFAGSWFS CSTSHNDTLV QKAVNQALRL
     YPQARREMCN NAACHRTSLV FGRCWNHANL NEATHRQIDR FFGGVNMRQL NLLMKMGYDG
     HVMGNAPLYE PLTSEANIER LRGIPVMLFV GRDNAVLSPE ATERTYETLC DAFEDGEYKR
     KVVPGYGHLD GWMGRNAWKD VYPFVREEVD RVTRGEAYEF VEPDDRFKAM VHGGELLY
//