ID A0A3E2HIL5_SCYLI Unreviewed; 850 AA.
AC A0A3E2HIL5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
DE Flags: Fragment;
GN ORFNames=B7463_g3098 {ECO:0000313|EMBL:RFU33237.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU33237.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU33237.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU33237.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:RFU33237.1}.
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DR EMBL; NCSJ02000039; RFU33237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HIL5; -.
DR STRING; 5539.A0A3E2HIL5; -.
DR OMA; FYEAWTT; -.
DR Proteomes; UP000258309; 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; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..850
FT /note="CBM1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017821013"
FT DOMAIN 814..850
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU33237.1"
FT NON_TER 850
FT /evidence="ECO:0000313|EMBL:RFU33237.1"
SQ SEQUENCE 850 AA; 91279 MW; 3DE65EB6FE7355FF CRC64;
MRRSLNLLAG VFAIVIQDVL AQDFAGHKGY YTEPNTGIEF WTTYMDNGTI TGDGEFSTVS
WGGYQFGIAL PPSAVTTDTY DYLGMIVGSL PNGTGWAGVV HGDNIGASMS NHLMLLAWPD
EDRIVTSFRY APAYLDPLFY TGSAKLTQLY TNVNSTHWTL VYHCENCYIF DQPGQSPSNM
STTRGGWEQG WAQSYIPPDD PSDANSDIIQ HNNGMGEYSI VVESATQTSY SAWLSSATTI
SVPTSSGTSV PTSTPVSSVP VPTGATYDYV IVGGGAGGVP LADKLSQQGH SVLLIEKGFA
SSARWNGTLR PESGWLDGYN LTWFDVPGLC NRIWQPGGSN TVACQDTDQM AGCVLGGGTA
VNAGLWWNPN PSDWDVNFPA GWKSSDMATA ASRVFSRIPG TDHPSLDGQL YLQSGYNVVS
QGLANAGWRS VTANNEPGSK NFTYAHTAYM YSHGERGGPL ATYLVDAYAR PNFHLWLNTT
VDKVIRTGGH ATGVQVSATW DGGYAGTVNL TPLTGRVIIS AGAFGTAKVL FRSGIGPTDQ
LQIVQQSTDG PTMINQTQWI DLPVGYNLDD HLNTNLVISH PNVSYYDWLA AWDTPIPSDA
QEYLNSRIGP FAQAAPDIAP MFWEEIKCSD GITRQLQYTA RVEGSENEPN GNTMTLAQYL
GRGATSRGRT TIGLGLNMVV STLPWLQNSG DTEAVVKSIE HVVAAMKTVT GLTWLQPPPN
VTAADYVANM PLTYANIGDR RANHWLGTAK MGTDDGRNGG TAVVDTNTKV YGTDNIFVVD
ASIFPGMPTT NPSALIVTVA ERASDLLSAL PALQAVARYG QCGGQTYNGA QVCASPFTCQ
YQNAYYSQCL
//