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AMYR_DROSE
ID   AMYR_DROSE              Reviewed;         493 AA.
AC   O76261; B4HT73; B6C8H3; B6C8H4; B6C8H9; B6C8I0; B6C8I2; B6C8I4;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Alpha-amylase-related protein;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE   Flags: Precursor;
GN   Name=Amyrel; ORFNames=GM20043;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Da Lage J.-L.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-143; SER-152; LEU-293
RP   AND SER-423.
RC   STRAIN=Seychelles-1, Seychelles-10, Seychelles-11, Seychelles-12,
RC   Seychelles-13, Seychelles-14, Seychelles-15, Seychelles-2, Seychelles-3,
RC   Seychelles-4, Seychelles-5, Seychelles-6, Seychelles-7, Seychelles-8, and
RC   Seychelles-9;
RA   Legrand D., Tenaillon M., Lachaise D., Cariou M.-L.;
RT   "Multilocus patterns of nucleotide diversity in Drosophila sechellia: the
RT   evolutionary history of the least variable Drosophila species.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P56634};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000250|UniProtKB:P56634};
CC       Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; AF039558; AAC39093.1; -; Genomic_DNA.
DR   EMBL; EU018418; ABW69388.1; -; Genomic_DNA.
DR   EMBL; EU018419; ABW69389.1; -; Genomic_DNA.
DR   EMBL; EU018420; ABW69390.1; -; Genomic_DNA.
DR   EMBL; EU018421; ABW69391.1; -; Genomic_DNA.
DR   EMBL; EU018422; ABW69392.1; -; Genomic_DNA.
DR   EMBL; EU018423; ABW69393.1; -; Genomic_DNA.
DR   EMBL; EU018424; ABW69394.1; -; Genomic_DNA.
DR   EMBL; EU018425; ABW69395.1; -; Genomic_DNA.
DR   EMBL; EU018426; ABW69396.1; -; Genomic_DNA.
DR   EMBL; EU018427; ABW69397.1; -; Genomic_DNA.
DR   EMBL; EU018428; ABW69398.1; -; Genomic_DNA.
DR   EMBL; EU018429; ABW69399.1; -; Genomic_DNA.
DR   EMBL; EU018430; ABW69400.1; -; Genomic_DNA.
DR   EMBL; EU018431; ABW69401.1; -; Genomic_DNA.
DR   EMBL; EU018432; ABW69402.1; -; Genomic_DNA.
DR   EMBL; CH480816; EDW48174.1; -; Genomic_DNA.
DR   RefSeq; XP_002034161.1; XM_002034125.1.
DR   AlphaFoldDB; O76261; -.
DR   SMR; O76261; -.
DR   STRING; 7238.O76261; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblMetazoa; FBtr0203028; FBpp0201520; FBgn0025060.
DR   GeneID; 6609476; -.
DR   KEGG; dse:6609476; -.
DR   HOGENOM; CLU_013336_2_1_1; -.
DR   OMA; QSWGTDW; -.
DR   PhylomeDB; O76261; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycosidase;
KW   Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..493
FT                   /note="Alpha-amylase-related protein"
FT                   /id="PRO_0000001386"
FT   ACT_SITE        207
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   ACT_SITE        244
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         117
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         177
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         205
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         211
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         307
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         342
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   SITE            309
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   MOD_RES         20
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..103
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        156..170
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        375..381
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        417..440
FT                   /evidence="ECO:0000255"
FT   DISULFID        447..459
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   VARIANT         143
FT                   /note="P -> T (in strain: Seychelles-1 and Seychelles-15)"
FT                   /evidence="ECO:0000269|Ref.2"
FT   VARIANT         152
FT                   /note="F -> S (in strain: Seychelles-12)"
FT                   /evidence="ECO:0000269|Ref.2"
FT   VARIANT         293
FT                   /note="W -> L (in strain: Seychelles-7 and Seychelles-8)"
FT                   /evidence="ECO:0000269|Ref.2"
FT   VARIANT         423
FT                   /note="F -> S (in strain: Seychelles-8 and Seychelles-10)"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   493 AA;  55461 MW;  5E02E633FFB270EB CRC64;
     MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ
     VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS
     GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ
     SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF
     IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ
     ALTFVDNHDN QRDAGAVLSY KSPRQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA
     QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQIAFCRGN
     KGFLAINNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNENG FGYIHIGSDD
     FDGVLALHVD AKV
 
 
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