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Database: UniProt
Entry: A0A3E2HIL5_SCYLI
LinkDB: A0A3E2HIL5_SCYLI
Original site: A0A3E2HIL5_SCYLI 
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
//
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