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Protein

Alpha-amylase

Gene

LOC100118139

Organism
Nasonia vitripennis (Parasitic wasp)
Status
Unreviewed-Annotation score: Annotation score: 2 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.UniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotationSAAS annotation (EC:3.2.1.1UniRule annotationSAAS annotation)
Gene namesi
Name:LOC100118139Imported
OrganismiNasonia vitripennis (Parasitic wasp)Imported
Taxonomic identifieri7425 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaChalcidoideaPteromalidaePteromalinaeNasonia
ProteomesiUP000002358 Componenti: Chromosome 3

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotation

Phylogenomic databases

InParanoidiK7J0Z0.
KOiK01176.
PhylomeDBiK7J0Z0.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase_b_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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

K7J0Z0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNRNLLSRL AVASLLLLQV HWALSYDSAA YRYPHYVDGR TSMVHLFEWK
60 70 80 90 100
FKDIAEECER FLGPMGYAGV QVSPINENLV IPGRPWYERY QPMSYKIITR
110 120 130 140 150
SGNEDEFADM VKRCNKVGVR IYVDAVINHM TGNQVPAVGT GGSTAEPGKR
160 170 180 190 200
LYPGVPYGPK DFNTPCGIFN YGNGIEVRNC DLSGLHDLNQ GSEYVREKIL
210 220 230 240 250
EFLNRVIDHG VAGFRVDAAK HMWPGDLEII YGRTKNLRSD VFGENKRPFI
260 270 280 290 300
FQEVIDLGGG EGVSKWQYNY FGSVIEFVFG IQIGRFFRGW EDLSHLQHWG
310 320 330 340 350
FSDRGLLPSN DVVVMVDNHD NQRGHGAGGD AILTFKNPRL YKMAVAFMLA
360 370 380 390 400
HPYGHTRVMS SFDFSDPSQG PPADSQGNLI SPDPINGDVA SGAEANPCGH
410 420 430 440 450
GWVCEHRWSP IYGMVGFRNV VQDEALTNWW SNGQNQIAFS RGNRGFAAFN
460 470 480 490 500
GQFGTDLKET LQTGLPAGDY CDVISGRKVN GKCTGKTVKV NNDGNAYIEI
510
LKDEADGALA IHAETKL
Length:517
Mass (Da):57,523
Last modified:January 9, 2013 - v1
Checksum:iA2F57E4A132EB9EF
GO

Sequence databases

RefSeqiXP_001602184.1. XM_001602134.2.
XP_008205202.1. XM_008206980.1.
XP_008205203.1. XM_008206981.1.

Genome annotation databases

EnsemblMetazoaiNV15021-RA; NV15021-PA; NV15021.
GeneIDi100118139.
KEGGinvi:100118139.

Cross-referencesi

Sequence databases

RefSeqiXP_001602184.1. XM_001602134.2.
XP_008205202.1. XM_008206980.1.
XP_008205203.1. XM_008206981.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiNV15021-RA; NV15021-PA; NV15021.
GeneIDi100118139.
KEGGinvi:100118139.

Phylogenomic databases

InParanoidiK7J0Z0.
KOiK01176.
PhylomeDBiK7J0Z0.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase_b_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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional and evolutionary insights from the genomes of three parasitoid Nasonia species."
    Nasonia Genome Working Group
    Werren J.H., Richards S., Desjardins C.A., Niehuis O., Gadau J., Colbourne J.K., Werren J.H., Richards S., Desjardins C.A., Niehuis O., Gadau J., Colbourne J.K., Beukeboom L.W., Desplan C., Elsik C.G., Grimmelikhuijzen C.J., Kitts P., Lynch J.A.
    , Murphy T., Oliveira D.C., Smith C.D., van de Zande L., Worley K.C., Zdobnov E.M., Aerts M., Albert S., Anaya V.H., Anzola J.M., Barchuk A.R., Behura S.K., Bera A.N., Berenbaum M.R., Bertossa R.C., Bitondi M.M., Bordenstein S.R., Bork P., Bornberg-Bauer E., Brunain M., Cazzamali G., Chaboub L., Chacko J., Chavez D., Childers C.P., Choi J.H., Clark M.E., Claudianos C., Clinton R.A., Cree A.G., Cristino A.S., Dang P.M., Darby A.C., de Graaf D.C., Devreese B., Dinh H.H., Edwards R., Elango N., Elhaik E., Ermolaeva O., Evans J.D., Foret S., Fowler G.R., Gerlach D., Gibson J.D., Gilbert D.G., Graur D., Grunder S., Hagen D.E., Han Y., Hauser F., Hultmark D., Hunter H.C. IV, Hurst G.D., Jhangian S.N., Jiang H., Johnson R.M., Jones A.K., Junier T., Kadowaki T., Kamping A., Kapustin Y., Kechavarzi B., Kim J., Kim J., Kiryutin B., Koevoets T., Kovar C.L., Kriventseva E.V., Kucharski R., Lee H., Lee S.L., Lees K., Lewis L.R., Loehlin D.W., Logsdon J.M. Jr., Lopez J.A., Lozado R.J., Maglott D., Maleszka R., Mayampurath A., Mazur D.J., McClure M.A., Moore A.D., Morgan M.B., Muller J., Munoz-Torres M.C., Muzny D.M., Nazareth L.V., Neupert S., Nguyen N.B., Nunes F.M., Oakeshott J.G., Okwuonu G.O., Pannebakker B.A., Pejaver V.R., Peng Z., Pratt S.C., Predel R., Pu L.L., Ranson H., Raychoudhury R., Rechtsteiner A., Reese J.T., Reid J.G., Riddle M., Robertson H.M., Romero-Severson J., Rosenberg M., Sackton T.B., Sattelle D.B., Schluns H., Schmitt T., Schneider M., Schuler A., Schurko A.M., Shuker D.M., Simoes Z.L., Sinha S., Smith Z., Solovyev V., Souvorov A., Springauf A., Stafflinger E., Stage D.E., Stanke M., Tanaka Y., Telschow A., Trent C., Vattathil S., Verhulst E.C., Viljakainen L., Wanner K.W., Waterhouse R.M., Whitfield J.B., Wilkes T.E., Williamson M., Willis J.H., Wolschin F., Wyder S., Yamada T., Yi S.V., Zecher C.N., Zhang L., Gibbs R.A.
    Science 327:343-348(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AsymCXImported.
  2. EnsemblMetazoa
    Submitted (MAR-2014) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiK7J0Z0_NASVI
AccessioniPrimary (citable) accession number: K7J0Z0
Entry historyi
Integrated into UniProtKB/TrEMBL: January 9, 2013
Last sequence update: January 9, 2013
Last modified: March 4, 2015
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.