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Database: UniProt
Entry: A0A0D1ZK38_9EURO
LinkDB: A0A0D1ZK38_9EURO
Original site: A0A0D1ZK38_9EURO 
ID   A0A0D1ZK38_9EURO        Unreviewed;       264 AA.
AC   A0A0D1ZK38;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN   ORFNames=PV07_08031 {ECO:0000313|EMBL:KIW28361.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW28361.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW28361.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW28361.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847043; KIW28361.1; -; Genomic_DNA.
DR   RefSeq; XP_016248577.1; XM_016395158.1.
DR   AlphaFoldDB; A0A0D1ZK38; -.
DR   STRING; 569365.A0A0D1ZK38; -.
DR   GeneID; 27347225; -.
DR   VEuPathDB; FungiDB:PV07_08031; -.
DR   HOGENOM; CLU_064531_0_0_1; -.
DR   OrthoDB; 2941630at2759; -.
DR   Proteomes; UP000054466; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   Pfam; PF00734; CBM_1; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..264
FT                   /note="CBM1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002237825"
FT   DOMAIN          25..61
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          62..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..89
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  26386 MW;  9AB0D998410FE201 CRC64;
     MRQSIIVVSL LPCISLACPA ASSGAAQGPW EQCGGINWTG GTTCTSGWTC VEQNPYYSQC
     LQASNTPSPP QPTTSSPPVV QPVSPSPSPS SSPTSASEPA TSTSPASSSG GLTYKASFTH
     YGAGDSFGSP NCNTNTAACF FFTSPGFSAA VSQNLYGAGP GQGQGPACGT CWKLVGETDS
     SGNTLSNAGT SIVVMVNNLC PADGNPLCAQ NGLSGTNQYG ANVNFDLCSD SGASEAFFGN
     SGVGLAVGSA TQVDCSEWSG TVVH
//
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