(data stored in SCRATCH zone)

SWISSPROT: Q4W904_ASPFU

ID   Q4W904_ASPFU            Unreviewed;       319 AA.
AC   Q4W904;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 64.
DE   RecName: Full=Endo-chitosanase {ECO:0000256|RuleBase:RU361208};
DE            EC=3.2.1.132 {ECO:0000256|RuleBase:RU361208};
GN   ORFNames=AFUA_6G00500 {ECO:0000313|EMBL:EAL84215.1};
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:EAL84215.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84215.1, 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   -!- FUNCTION: Chitosanase catalyzing the endo-type cleavage of chitosan,
CC       the deacylated form of chitin. Chitosanase may be crucial in the
CC       degradation of the deacetylated portion of chitin in the fungal cell
CC       wall. {ECO:0000256|RuleBase:RU361208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of beta-(1->4)-linkages between D-glucosamine
CC         residues in a partly acetylated chitosan.; EC=3.2.1.132;
CC         Evidence={ECO:0000256|RuleBase:RU361208};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361208}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 75 family.
CC       {ECO:0000256|RuleBase:RU361208}.
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:EAL84215.1}.
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DR   EMBL; AAHF01000018; EAL84215.1; -; Genomic_DNA.
DR   RefSeq; XP_731505.1; XM_726412.1.
DR   STRING; 746128.CADAFUBP00009428; -.
DR   EnsemblFungi; EAL84215; EAL84215; AFUA_6G00500.
DR   GeneID; 3503631; -.
DR   KEGG; afm:AFUA_6G00500; -.
DR   EuPathDB; FungiDB:Afu6g00500; -.
DR   HOGENOM; HOG000170085; -.
DR   InParanoid; Q4W904; -.
DR   KO; K01233; -.
DR   OMA; YNVIYLQ; -.
DR   OrthoDB; 1307217at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016977; F:chitosanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR009939; Chitosanase_fungal.
DR   PANTHER; PTHR42061; PTHR42061; 1.
DR   Pfam; PF07335; Glyco_hydro_75; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4W904.
DR   SWISS-2DPAGE; Q4W904.
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361208};
KW   Glycosidase {ECO:0000256|RuleBase:RU361208, ECO:0000313|EMBL:EAL84215.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361208, ECO:0000313|EMBL:EAL84215.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361208};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Signal {ECO:0000256|RuleBase:RU361208}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361208"
FT   CHAIN           22..319
FT                   /note="Endo-chitosanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361208"
FT                   /id="PRO_5005143438"
FT   REGION          255..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..275
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..299
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  33886 MW;  E246AA5ACEE6DF0A CRC64;
     MRHRPVLVAI TATLFASQIT TKQAPSALRA FYNKARSGGD CTGADALQTG FYNTEWSGGH
     TTYCTKYLPT GKGFYLKGPG SDLANMDIDC DGEQSRGDGR CKSSTDTQGQ TRWGLKHLEK
     HGVRDLNANL HPYVVLGNEG GYSPTFDPRT VGVEPLSIVA VVCADELVYG VWGDTNGDDN
     EHPMVGEASL ALATACYGPS ISGNSGHDEA DVLYIAFAGK EAVPARAKWD ADSYEAFEES
     ITAQGDQLVS QLFGDRSTAT GGSDPHHTSA APIDSDSDSD SDDDDDGSSK HSDKSDGARR
     STIPRLCHTI LVALIALVC
//

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