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Database: UniProt
Entry: A0A2G8SEM3_9APHY
LinkDB: A0A2G8SEM3_9APHY
Original site: A0A2G8SEM3_9APHY 
ID   A0A2G8SEM3_9APHY        Unreviewed;       842 AA.
AC   A0A2G8SEM3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN   ORFNames=GSI_06732 {ECO:0000313|EMBL:PIL32028.1};
OS   Ganoderma sinense ZZ0214-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL32028.1, ECO:0000313|Proteomes:UP000230002};
RN   [1] {ECO:0000313|EMBL:PIL32028.1, ECO:0000313|Proteomes:UP000230002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL32028.1,
RC   ECO:0000313|Proteomes:UP000230002};
RX   PubMed=26046933; DOI=10.1038/srep11087;
RA   Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA   Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA   Li X., Schwartz D.C., Wang Y., Chen S.;
RT   "Chromosome-level genome map provides insights into diverse defense
RT   mechanisms in the medicinal fungus Ganoderma sinense.";
RL   Sci. Rep. 5:11087-11087(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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:PIL32028.1}.
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DR   EMBL; AYKW01000012; PIL32028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8SEM3; -.
DR   STRING; 1077348.A0A2G8SEM3; -.
DR   OrthoDB; 1328190at2759; -.
DR   Proteomes; UP000230002; 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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..842
FT                   /note="CBM1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013970373"
FT   DOMAIN          805..840
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          767..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   842 AA;  87834 MW;  6C1F5E7B9CA8B3A4 CRC64;
     MLRPTLLATV SVAAAISLVA AVSSQTYTWK NVKIGGGGGF VPNIVFNPSQ KGLAFARTDI
     GGAYRLNSDD SWTPLLDFVD DARWNYWGVD AIATDPVDPN RLYLATGMYT NSWDPNNGQI
     LISTDQGKTF TPSVLPFKVG GNMPGRGMGE RLAIDPNSHN ILYFGARSGH GLYKSTDYGA
     TWTQVKKFPS VGTYVADPTD TTGYNNDIMG LAWVTFDSTS GSNGTATPRI FVGVANKGSD
     NVFVSNDAGS TWTAVAGQNN TFLPHKGALS VAEKSLYISY SDGSGPYDGT SGSVWKYNIT
     AGTWKDVTPV SGSDLYFGFG GVAIDAQRPG TIMVAALNSW WPDGQIFRST DGGATWTGLW
     AWQSYPTLNR YYAYDDSLAP WIGPDDTIDT LTMQIGWMME GLSIDPFDSN HWLYGTGETI
     YGGHDLLEWD AGTSRNITLK SLADGVEETS VQGLISPPSG PHLISAIGDV DGFVHNDLDT
     APQVSFSNPT YSSSSDIDYA GNKPATIARV GTATDGSQGK QIAISSDAGT TWSQDYGAAD
     DVAGGKIALS ADGDTILWKT SSNAILRSQY TNAFTTVSSL PSSAVIASDK KNNSIFYGAS
     GSSLYISTDG ALTFSAAGSL GSSTSPFRVI VNPNVTGDVW VSTDKGLFHS TDSGSSFSAV
     SGVTQAWSIA LGAPKAFGGY PTIFAAANIG GVGYFRSDDA GVNWVQINDA AHGFGSASAN
     VLAADPRVYG RVYIGTNGRG IFYGDASGAA PAPTATATST TATTVKTTTA STSSTTTKAS
     STTASSTTTK ASTTTSTAPS STATGTAPLY GQCGGIGWTG PTVCASGTCV EQNDYYSQCI
     PS
//
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