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Database: UniProt/TrEMBL
Entry: T1PMB7_MUSDO
LinkDB: T1PMB7_MUSDO
Original site: T1PMB7_MUSDO 
ID   T1PMB7_MUSDO            Unreviewed;       502 AA.
AC   T1PMB7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN   Name=LOC101897056 {ECO:0000313|RefSeq:XP_005185288.1};
GN   Synonyms=101897056 {ECO:0000313|EnsemblMetazoa:MDOA006202-PA};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EMBL:AFP63859.1};
RN   [1] {ECO:0000313|EMBL:AFP63859.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ALHF {ECO:0000313|EMBL:AFP63859.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:AFP63859.1};
RA   Liu N., Zhang L., Li M., Reid W.;
RT   "Transcriptome of adult Musca domestica launches a platform for comparative
RT   house fly gene expression and characterization of differential gene
RT   expression among resistant and susceptible house flies.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:MDOA006202-PA}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA006202-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_005185288.1}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|RefSeq:XP_005185288.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000548,
CC         ECO:0000256|RuleBase:RU361134};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; KA649230; AFP63859.1; -; mRNA.
DR   EMBL; KA649325; AFP63954.1; -; mRNA.
DR   RefSeq; XP_005185288.1; XM_005185231.3.
DR   EnsemblMetazoa; MDOA006202-RA; MDOA006202-PA; MDOA006202.
DR   GeneID; 101897056; -.
DR   KEGG; mde:101897056; -.
DR   VEuPathDB; VectorBase:MDOA006202; -.
DR   eggNOG; KOG2212; Eukaryota.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000095301; Unassembled WGS sequence.
DR   Proteomes; UP000694905; Unplaced.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..502
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014313773"
FT   DOMAIN          33..404
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          413..500
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   502 AA;  56065 MW;  C21E1640CCC5949D CRC64;
     MRDSICSFSF VFVLLILALC WAQKDPQFHD NRTTIVHLFE WTWPEIAREC EEFLGPQGYG
     GVQISPPNEV IVTDNWWARY QPVSYKLISR SGSESDLSDM IRRCNQAGVR TYVDIVVNHM
     SGYKDGDTLG TAGSVANYGQ RSWPAVPYGP EDFHPTCDIS NYQDRQQVRN CQLSSLADLN
     QTVPHVRDMI VGYMDHLTDL GVAGFRIDAA KHMWPEDLEV IYGRLKDLNT DFGFPANTKP
     YIYQEVIDLG GEEIKKSEYN HLGAVTEFKF STDIGLVFRN KIPLKSLKNW GPEWNMLPSE
     DVIVFVDNHD NQRGHGAGGA DILTHKVPSL YKPAVAFMLA HPYGKVARVM SSYAFDNSDQ
     GPPAHEDGSI KAPSFLSNQQ CDTANNGWVC EHRWPEIVEM VKFRNLVNDA PLENWWDNEG
     KQVAFSRGNK GFVAFNLEED SELDVNLSTG LAAGEYCDVI SGGRLGNQCG GVKVVVTEDG
     SADIKLPKGP QVLAISSQSK LQ
//
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