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Q4WPQ9 (Q4WPQ9_ASPFU) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. RuleBase RU361134

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. RuleBase RU003615

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EAL89775.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site2241Nucleophile By similarity PIRSR PIRSR001024-1
Active site2481Proton donor By similarity PIRSR PIRSR001024-1
Metal binding1391Calcium 1 By similarity
Metal binding1801Calcium 1; via carbonyl oxygen By similarity
Metal binding1931Calcium 1 By similarity
Metal binding2241Calcium 2 By similarity
Metal binding2281Calcium 1; via carbonyl oxygen By similarity
Metal binding2481Calcium 2 By similarity
Site3151Transition state stabilizer By similarity PIRSR PIRSR001024-2

Amino acid modifications

Disulfide bond168 ↔ 182 By similarity PIRSR PIRSR001024-4
Disulfide bond258 ↔ 301 By similarity PIRSR PIRSR001024-4

Sequences

Sequence LengthMass (Da)Tools
Q4WPQ9 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 9B3999975976A871

FASTA49453,872
        10         20         30         40         50         60 
MHIRWSSFFL SCLAGTALAA TPAQWRSQSI YFLLTDRFAR TDGSTTASCD TSARYCGGTW 

        70         80         90        100        110        120 
QGIIEQLDYI QGMGFTAIWI TPVTKQLPQD TSEGTAYHGY WQQDIYSVNS NYGTADDLKA 

       130        140        150        160        170        180 
LASALHDRGM YLMVDVVANH MGYAGAGDSV DYSVFNPFNS QTSFHPLCFI SNYDNQTDVE 

       190        200        210        220        230        240 
NCWLGDNSVP LPDLDTTNPD VQKIWYNWVN SLVSNYSIDG LRIDTVKHVQ SDFWPGFNDA 

       250        260        270        280        290        300 
AGVYCIGEVF DGDPAYTCPY QEVLDGVLNY PIYYPLLKAF QSTSGSMSSL YDMINTVKSQ 

       310        320        330        340        350        360 
CADSTLLGTF VENHDTPRFA SYTKDMALAK NAAAFIIFSD GIPIIYAGQE QHYSGGADPA 

       370        380        390        400        410        420 
NREAVWLSGY STTSDLYKLI ATANAIRSHA ISKDPGYVTY KNNPIYKDTS TIAMRKGSDG 

       430        440        450        460        470        480 
AQIITVLSNL GASGSSYTLS LGGTGYEAGQ QLTEMFSCTT VTVGSDKKVP VSMASGLPRV 

       490 
FYPTAGLNGS TVCT 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000005 Genomic DNA. Translation: EAL89775.1.
RefSeqXP_751813.1. XM_746720.1.

3D structure databases

ProteinModelPortalQ4WPQ9.
SMRQ4WPQ9. Positions 20-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00008053.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00008053; CADAFUAP00008053; CADAFUAG00008053.
GeneID3509344.
KEGGafm:AFUA_4G10130.

Phylogenomic databases

HOGENOMHOG000165530.
KOK01176.
OMANQTQVED.
OrthoDBEOG7RBZJ4.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]
PIRSFPIRSF001024. Alph-amyl_fung. 1 hit.
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ4WPQ9_ASPFU
AccessionPrimary (citable) accession number: Q4WPQ9
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2005
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)