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Protein

Alpha-amylase-related protein

Gene

Amyrel

Organism
Drosophila bipectinata (Fruit fly)
Status
Reviewed-Annotation score: -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:

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 bipectinata (Fruit fly)
Taxonomic identifieri42026 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Organism-specific databases

FlyBaseiFBgn0029467 Dbip\Amyrel

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
ChainiPRO_000000137321 – 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

ProteinModelPortaliQ9NJN8
SMRiQ9NJN8
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
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
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.

Q9NJN8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFKFATAVIL CLVAASSTLA QHNPHWWGNR NTIVHLFEWK WSDIAAECEN
60 70 80 90 100
FLGPRGFAGV QVSPVNENIV SAGRPWWERY QPISYKLTTR SGNEKEFADM
110 120 130 140 150
VRRCNEVGVR IYVDVLLNHM SGDFDGIAVG TAGSEAEPSK KSYPGVPYSA
160 170 180 190 200
LDFHPSCEIT DWNDRFQVQQ CELVGLKDLD QSSEWVRSKL IEFLDHLIEL
210 220 230 240 250
GVAGFRVDAA KHMAADDLSF IYSSLSDLNI EHGFPHNARP FIFQEVIDHG
260 270 280 290 300
HETVSREEYN QLGAVTEFRF SEGIGNAFRG NNALKWLQSW GTGWGFLPSG
310 320 330 340 350
QALTFVDNHD NQRDMGAVLN YKSPKQYKMA TAFHLAYPYG ISRVMSSFAF
360 370 380 390 400
DDHDTAPPQD EQEKIISPEF DEEGACVNGW ICEHRWRQIY AMVGFKNAVR
410 420 430 440 450
DTELSNWWDN GDSQISFCRG NKGFLAVNNN LYDLSQELQT CLPAGVYCDV
460 470 480 490
ISGSLVDGSC TGKSVTVDDN GYGYAHIGSD DFDGVLALHV DAKV
Length:494
Mass (Da):55,339
Last modified:October 1, 2000 - v1
Checksum:i60EEEF2C9F685491
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136936 Genomic DNA Translation: AAF25718.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136936 Genomic DNA Translation: AAF25718.1

3D structure databases

ProteinModelPortaliQ9NJN8
SMRiQ9NJN8
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13 Glycoside Hydrolase Family 13

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

FlyBaseiFBgn0029467 Dbip\Amyrel

Family and domain databases

Gene3Di2.60.40.1180, 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
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_DROBP
AccessioniPrimary (citable) accession number: Q9NJN8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: October 1, 2000
Last modified: February 28, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Documents

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

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