Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

F1NF53

- F1NF53_CHICK

UniProt

F1NF53 - F1NF53_CHICK

Protein

Alpha-amylase

Gene

AMY2A

Organism
Gallus gallus (Chicken)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 24 (01 Oct 2014)
      Sequence version 1 (03 May 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. alpha-amylase activity Source: UniProtKB-EC
    2. cation binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    GlycosidaseUniRule annotation, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolismUniRule annotation

    Enzyme and pathway databases

    ReactomeiREACT_217787. Digestion of dietary carbohydrate.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylaseUniRule annotation (EC:3.2.1.1UniRule annotation)
    Gene namesi
    Name:AMY2AImported
    OrganismiGallus gallus (Chicken)Imported
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 8

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.UniRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00390000002882.
    KOiK01176.
    OMAiSQVRDCR.
    OrthoDBiEOG7RJPR2.
    TreeFamiTF312850.

    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.

    F1NF53-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQVLLLLAAV GLCWAQYNPN TQAGRTSIVH LFEWRWADIA LECERYLAPN    50
    GFGGVQVSPP NENIVITNPN RPWWERYQPI SYKICSRSGN ENEFRDMVTR 100
    CNNVGVRIYV DAVVNHMCGS MGGTGTHSTC GSYFNTGTRD FPAVPYSAWD 150
    FNDGKCHTAS GDIENYGDMY QVRDCKLSSL LDLALEKDYV RSTIAAYMNH 200
    LIDMGVAGFR IDAAKHMWPG DIRAFLDKLH DLNTQWFSAG TKPFIYQEVI 250
    DLGGEPITGS QYFGNGRVTE FKYGAKLGTV IRKWNGEKMA YLKNWGEGWG 300
    FVPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF 350
    TRVMSSYRWP RYFENGVDVN DWVGPPSNSD GSTKSVTINA DTTCGNDWVC 400
    EHRWRQIRNM VIFRNVVDGQ PFSNWWDNGS NQVAFGRGDR GFIVFNNDDW 450
    YMNVDLQTGL PAGTYCDVIS GQKEGSACTG KQVYVSSDGK ANFQISNSDE 500
    DPFVAIHVDA KL 512
    Length:512
    Mass (Da):57,497
    Last modified:May 3, 2011 - v1
    Checksum:iDD023415B798B8F4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AADN03005674 Genomic DNA. No translation available.
    RefSeqiNP_001001473.2. NM_001001473.2.
    UniGeneiGga.16588.

    Genome annotation databases

    EnsembliENSGALT00000002915; ENSGALP00000002911; ENSGALG00000001880.
    GeneIDi414140.
    KEGGigga:414140.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AADN03005674 Genomic DNA. No translation available.
    RefSeqi NP_001001473.2. NM_001001473.2.
    UniGenei Gga.16588.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000002915 ; ENSGALP00000002911 ; ENSGALG00000001880 .
    GeneIDi 414140.
    KEGGi gga:414140.

    Organism-specific databases

    CTDi 279.

    Phylogenomic databases

    GeneTreei ENSGT00390000002882.
    KOi K01176.
    OMAi SQVRDCR.
    OrthoDBi EOG7RJPR2.
    TreeFami TF312850.

    Enzyme and pathway databases

    Reactomei REACT_217787. Digestion of dietary carbohydrate.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR006048. 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 ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM00642. Aamy. 1 hit.
    SM00632. Aamy_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
      International Chicken Genome Sequencing Consortium
      Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
      , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
      Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Red jungle fowlImported.
    2. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.
      Strain: Red jungle fowlImported.

    Entry informationi

    Entry nameiF1NF53_CHICK
    AccessioniPrimary (citable) accession number: F1NF53
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 24 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3