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Database: UniProt
Entry: S3DF65_GLAL2
LinkDB: S3DF65_GLAL2
Original site: S3DF65_GLAL2 
ID   S3DF65_GLAL2            Unreviewed;       847 AA.
AC   S3DF65;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=FAD/NAD(P)-binding protein {ECO:0000313|EMBL:EPE36395.1};
GN   ORFNames=GLAREA_05733 {ECO:0000313|EMBL:EPE36395.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE36395.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE36395.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; KE145353; EPE36395.1; -; Genomic_DNA.
DR   RefSeq; XP_008077213.1; XM_008079022.1.
DR   AlphaFoldDB; S3DF65; -.
DR   GeneID; 19464787; -.
DR   KEGG; glz:GLAREA_05733; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_011025_0_0_1; -.
DR   OMA; IGYLQCA; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000016922; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd09630; CDH_like_cytochrome; 1.
DR   Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF49344; CBD9-like; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..847
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004519795"
FT   DOMAIN          811..847
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
SQ   SEQUENCE   847 AA;  90107 MW;  5162907D62CA7DD0 CRC64;
     MKLTNLSTGV LGSLLFSVSS VLAQDFAQHG TFTEPNTNIT FYTSYEPDGV DPSGFSQASI
     GGYTFGIALP PSATTVDFYD YVGLIVGSTP NGNGWTGVLQ GDMSASMPNH LMILAWPTGN
     GDEVVTSFRY SPSYQLPIAY KGTAKLTQIF SKVNATHFTL VYKCERCLIF DDPTQSEFNT
     STSAGEFIQG WGQALESAAV KADAMSDFGQ HDNGQGVFKV VVSSATHTDY SKWAALATSV
     PTGTVPTTTP TAVPYSSVPV PTATSYDYIV IGGGAAGIPI ADKLSETGKS VLLIEKGIAS
     SARWGGTLRP ESGWLDGQNL TWFDIPGECN RIWNGGSPGV ACTDMDQMAG CVLGGGAAVN
     AGLWWKANPS DWDYNFPAGW KAKDMLPATN RVFSRIPGTD HPSLDGKLYV QSGFDTIRQG
     LDNAKWTSVT ANNVPEKKNR TYAHTPYMSS HGERGGPMAT YLVTAAGRKN FQMWLNTSVE
     RITRIGGHAV SLDVSPANNG GRYGTVQLTP VTGRVILAAG TFGTTKILFR SGIGPKDQLD
     IVATSADAKV MSNSANWLNL PVGKSLNDHL NTDTVISHPN VSYYDWPAAW NTPIEKDKVD
     YLTKRIGPLT QAAPNIGPMM WEEIKGPDGI VRQFQWTSRV EGSGGFDNGN TMTLSLYLGR
     GSVSRGQTTI NKGLNMVVST LPYGDANDLA TVAMALDSMK SALKTIPGLT WLAPTLNQTG
     ADYLKTIPLT YSNVGARRSN HWMGTAKLGT DSGLTGGTSV VDTNTKIYGT DNMFVVDASI
     FPGMPSTNPS GLIVVAAERA AELIKALPAL RAVNKGGQCG GAKYTGAMVC AKPFTCKVIN
     KDLSKCS
//
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