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Database: UniProt
Entry: A0A1W2TM66_ROSNE
LinkDB: A0A1W2TM66_ROSNE
Original site: A0A1W2TM66_ROSNE 
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
//
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