(data stored in SCRATCH zone)

SWISSPROT: Q4WCM9_ASPFU

ID   Q4WCM9_ASPFU            Unreviewed;       460 AA.
AC   Q4WCM9;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361164};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361164};
GN   ORFNames=AFUA_6G01800 {ECO:0000313|EMBL:EAL85859.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85859.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85859.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000256|RuleBase:RU361164}.
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:EAL85859.1}.
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DR   EMBL; AAHF01000012; EAL85859.1; -; Genomic_DNA.
DR   RefSeq; XP_747897.1; XM_742804.1.
DR   SMR; Q4WCM9; -.
DR   STRING; 746128.CADAFUBP00009383; -.
DR   EnsemblFungi; EAL85859; EAL85859; AFUA_6G01800.
DR   GeneID; 3505017; -.
DR   KEGG; afm:AFUA_6G01800; -.
DR   EuPathDB; FungiDB:Afu6g01800; -.
DR   HOGENOM; HOG000182210; -.
DR   InParanoid; Q4WCM9; -.
DR   KO; K19357; -.
DR   OMA; NEMDILE; -.
DR   OrthoDB; 875234at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; -; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; PTHR33753; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WCM9.
DR   SWISS-2DPAGE; Q4WCM9.
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361164};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361164};
KW   Glycosidase {ECO:0000256|RuleBase:RU361164, ECO:0000313|EMBL:EAL85859.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361164, ECO:0000313|EMBL:EAL85859.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361164};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..460
FT                   /note="Glucanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004245519"
FT   DOMAIN          424..460
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          401..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  48205 MW;  7DAAC894DB905413 CRC64;
     MDSKRGVVAA VLALLPLVSA QQPAASSAGN PKLTTYKCTT AGGCVAQDTS VVLDWGYHWI
     HTVDGYTSCT TSSGVDSTLC PDAATCAKNC VIEPANYTSA GVTTSGDSLT MYQYVQSNGV
     YTNASPRLYL LGPDKNYVML KLLGQELTFD VDLSTLPCGE NGALYLSEMS ATGGRNEYNT
     GGAEYGSGYC DAQCPVIAWK NGTLNTSGAS YCCNEMDILE ANSRANSYTP HPCSATDCDK
     GGCGFNPYAL GQKSYWGPGG TVDTSKPFTI TTQFITNDGT TTGTLSEIRR QYMQNGKVIA
     NAVSSTGVNS ITEDWCTSVD GSAATFGGLT TMGKALGRGM VLIFSIWNDA SGFMNWLDSG
     NAGPCSSTEG NPDLIKAQNP TTHVVFSNIR WGDIGSTFKG SDGSVTTTTS TTSTKTTTST
     APGPTQTHYG QCGGQGWTGP TACASPYTCQ VLNPWYSQCL
//

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