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Protein

Alpha-amylase-related protein

Gene

Amyrel

Organism
Drosophila auraria (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 1 Cl- ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi118CalciumBy similarity1
Metal bindingi169Calcium; via carbonyl oxygenBy similarity1
Metal bindingi178CalciumBy similarity1
Binding sitei206ChlorideBy similarity1
Active sitei208NucleophileBy similarity1
Metal bindingi212Calcium; via carbonyl oxygenBy similarity1
Active sitei245Proton donorBy similarity1
Binding sitei308ChlorideBy similarity1
Sitei310Transition state stabilizerBy similarity1
Binding sitei343ChlorideBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism
LigandCalcium, Chloride, Metal-binding

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase-related protein (EC:3.2.1.1By similarity)
Gene namesi
Name:Amyrel
OrganismiDrosophila auraria (Fruit fly)
Taxonomic identifieri47315 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Organism-specific databases

FlyBaseiFBgn0021682. Daur\Amyrel.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
ChainiPRO_000000137021 – 494Alpha-amylase-related proteinAdd BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Pyrrolidone carboxylic acidBy similarity1
Disulfide bondi48 ↔ 104By similarity
Disulfide bondi157 ↔ 171By similarity
Disulfide bondi376 ↔ 382By similarity
Disulfide bondi418 ↔ 441Sequence analysis
Disulfide bondi448 ↔ 460By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO77020.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiView protein in InterPro
IPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiView protein in SMART
SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O77020-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WADIAEECED
60 70 80 90 100
FLAPRGFAGV QVSPVNENII SPGRPWWERY QPISYKLTTR SGNEEEFADM
110 120 130 140 150
VRRCNDVGIR IYVDVLLNHM SGDFDGVAVG TAGTEAEPSK KSFPGVPYSA
160 170 180 190 200
QDFHPSCEIT DWNDRYQVQN CELVGLKDLN QHSDYVRSKL IEFLDHLIEL
210 220 230 240 250
GVAGFRVDAA KHMASEDLEY IYDNLSNLNI EHGFPHNARA FIFQEVIDHG
260 270 280 290 300
HETVSREEYN GLGAVTEFRF SEEIGRAFRG NNALKWLQSW GTGWGFLDSD
310 320 330 340 350
QALTFVDNHD NQRDQGSVLN YKSPKQYKMA TAFHLAYPYG ISRVMSSFAF
360 370 380 390 400
DDHDTPPPQD AQENIISPEF GEDGGCLNGW ICEHRWRQIY AMVGFKNAVR
410 420 430 440 450
DTELSEWWDN GDNQIAFCRG NKGFLAINNN LYDLSQELNT CLPAGEYCDV
460 470 480 490
ISGSLIDGAC TGKSVRVNER GYGYIHIGAD EFDGVLALHV DAKV
Length:494
Mass (Da):55,725
Last modified:June 6, 2002 - v2
Checksum:i1841262603859957
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96163 Genomic DNA. Translation: AAC39113.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96163 Genomic DNA. Translation: AAC39113.2.

3D structure databases

ProteinModelPortaliO77020.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

FlyBaseiFBgn0021682. Daur\Amyrel.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiView protein in InterPro
IPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiView protein in SMART
SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMYR_DROAV
AccessioniPrimary (citable) accession number: O77020
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: June 6, 2002
Last modified: February 15, 2017
This is version 89 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.