ID A0A166V5Z7_9AGAM Unreviewed; 843 AA.
AC A0A166V5Z7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carbohydrate-binding module family 1 protein {ECO:0000313|EMBL:KZP32381.1};
GN ORFNames=FIBSPDRAFT_916543 {ECO:0000313|EMBL:KZP32381.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP32381.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP32381.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP32381.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV417486; KZP32381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166V5Z7; -.
DR STRING; 436010.A0A166V5Z7; -.
DR OrthoDB; 1328190at2759; -.
DR Proteomes; UP000076532; 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:UP000076532};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..843
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007881040"
FT DOMAIN 805..841
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 759..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 87552 MW; 0F024FF21BCF5DBC CRC64;
MYNRGFLAAA IAAIAVPLVA AVTAQTYTWK NVKIGGGGGF VPDIVFNPSL KGLAYARTDI
GGAYRLNSDD SWTPLLDFAN DTTWHYWGTD AIATDPIDTT RVYLAVGMYT NSYDPNNGAI
LASKDQGATW TASALPFKVG GNMPGRGMGE RLAIDPHLNS VLFFGARSGH GLYKSTNYGV
TWTNVTSFTS TGNYAPDPTD TTGYNSDLTG IAWVTFDSTS GTSGTATPRI FVGVASTGTT
NIFVSNDAGS TWTAVAGQNT TYLPHKGVLS PTEKLLYVSY SNGAGPYDGT LGSVSKYNIT
SGVWADITPV SGSDLYFGFG GLAVDLQKPG TIMVAALNSW YPDGQIFRSI NSGATWTPLW
AWNGYPSIYK YYTYSDTLAP WLGPNADVFT LGTLQIGWMM EGLSIDPFDS NHWLYGTGAT
IYGGHDLLNW DSTHNVTIKS LADGIEETAV QGLISPPTGP SLLSALGDIE GFVHNSLTSP
PANSYTTPTW STTADIDFAG NDPTNIVRIG TGDSTSGKQV AISTDSGATW NQDYGAADNV
TGGKVAFSAN GDIVLWRTSG NGVQVSQYTD AFVAVPTLPS DAAIASDKKN DTIFYGASGS
KFYLSVNGGV SFTAKGSLGA STAPFKVVVN PSVTGDVWVS TDKGLFHSVD TGTTFTAITS
ITAAWAIALG APKTTGGYPA IFAAANIGGV GYFRSDDEGV TWVQINDAAH GFGSASSNVL
TADPRIYGRV YIGTNGRGIF YGDASGTVAT SAAPSSTTVA TSSTAKTTST TASTTSKATT
TSSTTTSKVT STTVTSTTTS AAAGATQTAY GQCGGSSWTG ATACVSGYTC KVSSTFYSQC
VPS
//
