ID A0A1W2TM66_ROSNE Unreviewed; 832 AA.
AC A0A1W2TM66;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative glycoside hydrolase family 74 protein {ECO:0000313|EMBL:GAP89423.2};
DE EC=3.2.1.155 {ECO:0000313|EMBL:GAP89423.2};
DE EC=3.2.1.4 {ECO:0000313|EMBL:GAP89423.2};
DE EC=3.2.1.91 {ECO:0000313|EMBL:GAP89423.2};
GN ORFNames=SAMD00023353_4000610 {ECO:0000313|EMBL:GAP89423.2};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP89423.2};
RN [1] {ECO:0000313|EMBL:GAP89423.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP89423.2};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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DR EMBL; DF977485; GAP89423.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2TM66; -.
DR STRING; 77044.A0A1W2TM66; -.
DR OMA; YSSWWPD; -.
DR OrthoDB; 1328190at2759; -.
DR Proteomes; UP000054516; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0033950; F:xyloglucan-specific exo-beta-1,4-glucanase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:GAP89423.2};
KW Hydrolase {ECO:0000313|EMBL:GAP89423.2};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..832
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012348325"
FT DOMAIN 796..832
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 741..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 86087 MW; FCA10954AD59581E CRC64;
MKLLILTELL LAAAAPIRAA FTWQNVKIGG GGGFVPGFVF HPKTKGVAYA RTDIGGLYRL
NSDDSWTAVT DSIADTANWS KWGVDAVALD PQDANKVYAA VGSYTNSWDP NNGAIIRSSD
QGATWSSTSL SFKVGGNMPG RGMGERLAVD PVNSKILYFG ARSGNGLWKS TDGGVTFAKV
SSFTAKGAFA PDPSDPNGYN NDPQGLTFVT FDSTSSTTGG ATSRIFVGTA DNATSSVWVT
EDAGTTWSAV AGQPGTFFPH KCVLQPTEKA LYLTYSDGTG PYDGTLGAVY RYDITAKTWK
NITPVSGSDL YYGFGGIGVD MLSPGTIVVA SLNSWWPDAQ LFRSTDSGAT WSRLWEWTSY
PNMNLYYSQS AAKAPWVKSG FLDADTKDLG WMIESLVINP FDSDHWLYST GLTVFGGHDL
TKWDTTHNIT IQVLADGIEE FAVLGLASAP GGSELLAAVG DDSGFTFASS AALRTSPQKP
WMDPIFSSST SVDYAGAAVK NVVRVGNTAG TQQVAVSGDG GASWNVYYGA DTSMTGGTVA
YSAGGDTILW STSANGVQRS QYTSAFAAVS SLPAAAVIAA DKQENAYFYA GSGSAFYVSK
DTGSTFAAAG TLSGATSVRT IAAHPKVAGE VWVSTDAGVF RSTDHGASFA KASTGLTNTY
QVALGLGSGS AWNVYAFGTG SAGARLYGSA DAGATWTDIQ GATQGFGAID SCKLAGSGNT
ANQVFVGTNG RGVLYASGAL SGGGGGGSTT TTSRTTLSTS TTSTTRVTSS TTTTRTTTTT
TRATTTTTSS GSTPTGTVPQ YGQCGGSGYT GPTVCVSPYT CQVQNAYYSQ CL
//