(data stored in ACNUC7421 zone)

SWISSPROT: Q4WD22_ASPFU

ID   Q4WD22_ASPFU            Unreviewed;       357 AA.
AC   Q4WD22;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 81.
DE   RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE            EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN   ORFNames=AFUA_6G03230 {ECO:0000313|EMBL:EAL85716.1};
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:EAL85716.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85716.1, 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 16 family.
CC       {ECO:0000256|PIRNR:PIRNR037299}.
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:EAL85716.1}.
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DR   EMBL; AAHF01000012; EAL85716.1; -; Genomic_DNA.
DR   RefSeq; XP_747754.1; XM_742661.1.
DR   EnsemblFungi; EAL85716; EAL85716; AFUA_6G03230.
DR   GeneID; 3505256; -.
DR   KEGG; afm:AFUA_6G03230; -.
DR   EuPathDB; FungiDB:Afu6g03230; -.
DR   HOGENOM; HOG000196187; -.
DR   InParanoid; Q4WD22; -.
DR   OMA; PEETFHT; -.
DR   OrthoDB; 1209387at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005618; C:cell wall; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WD22.
DR   SWISS-2DPAGE; Q4WD22.
KW   Glycosidase {ECO:0000313|EMBL:EAL85716.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037299, ECO:0000313|EMBL:EAL85716.1};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037299, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..357
FT                   /note="Glycosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004246145"
FT   TRANSMEM        331..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..220
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
SQ   SEQUENCE   357 AA;  37704 MW;  788AD261455823FB CRC64;
     MMLPLLAVSA FASLGAAQTY TSCNPTNSLK TWSLSTDFTQ GSSDGWTAIS GNVTYGSNGA
     EFTINKRYDA PTLETNFYIF FGEVEVVMRA ANGTGIVSSI VMESDDLDEI DWECTGTDTT
     QIQTNYFGKG NTTTYDRAIW ETVSSPQDEF HTYKVVWTAA AITWYIDGTA VRTLEYADAV
     DGKNYPQTPM VVKLGIWAGG DPSNSEGTIE WAGGETDYDE VPFTMYVKSV NIINYNPAAS
     YNYTDKTGSY TSIVASNSTT GSGIHSSNSV SVFAPSSSTS TFTSSRALIA TASTYPASVQ
     TSSSGVVSLS SSSASSSSAA ASSTSGSASA VFTGAAVTNL PSFFFTVFFA LAIALAF
//

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