ID   B7PL57_IXOSC            Unreviewed;       409 AA.
AC   B7PL57;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 95.
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};
DE   Flags: Fragment;
GN   ORFNames=IscW_ISCW006372 {ECO:0000313|EMBL:EEC07329.1};
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1] {ECO:0000313|EMBL:EEC07329.1, ECO:0000313|Proteomes:UP000001555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC07329.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ISCW006372-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW006372-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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; ABJB010087451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010213199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS738034; EEC07329.1; -; Genomic_DNA.
DR   RefSeq; XP_002434505.1; XM_002434460.1.
DR   AlphaFoldDB; B7PL57; -.
DR   STRING; 6945.B7PL57; -.
DR   PaxDb; 6945-B7PL57; -.
DR   EnsemblMetazoa; ISCW006372-RA; ISCW006372-PA; ISCW006372.
DR   KEGG; isc:IscW_ISCW006372; -.
DR   VEuPathDB; VectorBase:ISCI006372; -.
DR   VEuPathDB; VectorBase:ISCP_020617; -.
DR   VEuPathDB; VectorBase:ISCW006372; -.
DR   HOGENOM; CLU_013336_1_1_1; -.
DR   InParanoid; B7PL57; -.
DR   OMA; INHMGAT; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
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:UP000001555}.
FT   DOMAIN          1..311
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          320..408
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEC07329.1"
SQ   SEQUENCE   409 AA;  45658 MW;  5ABD1346FE3A0D4E CRC64;
     ALCRIYVDTV INHMTAASGS ANGTAGSSYD AEGHYEAVPY GPEDFHTKLE CGSPSGNLEN
     MFDINQVRNC RLVGLIDLDQ SRENVRDEQV RFLNKLIGMG VAGFRVDAAK HMWPEDLKVI
     YGRMDNLSAE FFPAGARPLI YQEVIDVRNG EPVTRDQYTG FGRVTEFLYG VNMGAVFRKQ
     DGKQLKDLRN FTKSWDLMPS GDALSFLSNH DNQRGHGYGG DVVLTFFDAR LYKMATALLL
     ALPYGLPRIT SSYRWQRNVV DGKDTNDWVG PPADSDWNIK PVVRELNGTC GNGWVCEHRQ
     VRRVSNLVEL RKVAGEAPVT HWWDNGGHAI AFGRRGRAFV VINNEDRPVE NVFETDLPPG
     LYCDVVTGGK AQKGCKGRLF RVSAEQTSRI LVNSAWDVPM VAIHVEARL
//