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Reviewed, UniProtKB/Swiss-Prot O76284 (AMYR_DROBC)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-amylase-related protein
    EC=3.2.1.1
Gene names
Name: Amyrel
OrganismDrosophila bocqueti (Fruit fly)
Taxonomic identifier74549 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Binds 1 chloride ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

chloride ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 494474Alpha-amylase-related protein
PRO_0000001372

Sites

Active site2081Nucleophile By similarity
Active site2451Proton donor By similarity
Active site3101 By similarity
Metal binding1181Calcium By similarity
Metal binding1691Calcium; via carbonyl oxygen By similarity
Metal binding1781Calcium By similarity
Metal binding2121Calcium; via carbonyl oxygen By similarity
Binding site2061Chloride By similarity
Binding site3081Chloride By similarity
Binding site3431Chloride By similarity

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid By similarity
Disulfide bond48 ↔ 104 By similarity
Disulfide bond157 ↔ 171 By similarity
Disulfide bond376 ↔ 382 By similarity
Disulfide bond418 ↔ 441 Potential
Disulfide bond448 ↔ 460 By similarity

Sequences

Sequence LengthMass (Da)Tools
O76284-1 [UniParc].

Last modified August 15, 2003. Version 2.
Checksum: 53B47530A5819BEE

FASTA49455,613
        10         20         30         40         50         60 
MIKFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WSDIAEECET FLAPRGFAGV 

        70         80         90        100        110        120 
QVSPVNENII SAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM 

       130        140        150        160        170        180 
SGDFDGVAVG TAGTEAEPSK KSFPGVPYTA QDFHPSCEIT DWNNRFQVQE CELVGLKDLN 

       190        200        210        220        230        240 
QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAEDLEY IYGSLSNLNI EHGFPHNARP 

       250        260        270        280        290        300 
FIFQEVIDHG HETVSREEYN QLGAVTEFRF SEEIGNAFRG NNALKWLQSW GTGWGFLSSE 

       310        320        330        340        350        360 
QAFTFVDNHD NQRDQGSVLN YKSPRQYKMA TAFHLANPYG IIRVMSSFAF DDQDTPPPQD 

       370        380        390        400        410        420 
AQENIISPEF DEDGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSGWWDN GDNQISFCRG 

       430        440        450        460        470        480 
NKGFLAVNNN QYDLSQELNT CLPAGEYCDV ISGSLIDGAC TGKSVTVNEH GYGYIHIGSD 

       490 
DFDGVLALHV NAKV 

« Hide

References

[1]Da Lage J.-L.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AF049092 Genomic DNA. Translation: AAC39100.2.

3D structure databases

HSSPHSSP built from PDB template 1JAE based on UniProtKB P56634.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Organism-specific databases

FlyBaseFBgn0046208. Dboc\Amyrel.

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYR_DROBC
AccessionPrimary (citable) accession number: O76284
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: August 15, 2003
Last modified: June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents