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Database: UniProt
Entry: A0A0V0TUB3_9BILA
LinkDB: A0A0V0TUB3_9BILA
Original site: A0A0V0TUB3_9BILA 
ID   A0A0V0TUB3_9BILA        Unreviewed;       744 AA.
AC   A0A0V0TUB3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   03-MAY-2023, entry version 28.
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=amy {ECO:0000313|EMBL:KRX42613.1};
GN   ORFNames=T05_9613 {ECO:0000313|EMBL:KRX42613.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX42613.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX42613.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX42613.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX42613.1}.
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DR   EMBL; JYDJ01000140; KRX42613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TUB3; -.
DR   STRING; 144512.A0A0V0TUB3; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
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   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:UP000055048}.
FT   DOMAIN          70..448
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          457..544
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   744 AA;  86580 MW;  D88B295871DD7854 CRC64;
     MIFQIKYFNN VYLCAFVTIY RQAIQHKIYR KMNVKPACEF PLFIFSTAFF YSYAFNSECF
     KQLAVDPTRQ LVVHLFEWGW TDIAKECKNY LWKSGIGAVQ VSPPNEHIII VENNDLPWWS
     RYQPISYQLY SRSGSEKEFI NMVEECNKYG IRIIADIVIN HMVGANMEGY GWHGSYFKST
     PFEEYFPSVP YNETDFHDKI CNGNIEDYGN RWQVRNCRLV NLVDLDHSNP NVQASIVAYM
     NRLIDIGVAG FRIDAAKHMW PDMLRKIIYQ LKPLNSAYFP KNQCPFIFNE VIDQGGEPIK
     AEEYLDIGRV TNFKYGLDLS AAVRRRKNFK HLINFGEAWN YFPSNGALVF VDNHDNQRGH
     GGGGPVLTFK NGNAYKMAVH FMLAWSYGLP RLMSSYYFNT ANQGPPSTGF PFFNTTSPMF
     DRNGKCIAST GWTCEHRWPS FYQMSLFHQN TSNKAIWNTV VDEHRIAFSK GNSGFFALNN
     HPTENWILHV NTGLPPGYYC DHITGNLNVK RNSCSGKTVF VNPNGWIDLL VRAEETLAIS
     SKNALSKFEP SYRRTLVFVK KKTQIGEYLF MRGRRPSSDS TRWQNQWKNK YTIPIVHVAD
     YDPSFTDYHQ WKQHDNMLQW SLPSSKIALK EKKPTVENLF KMGSPLIWTT DNKRSNAYNI
     YNRYGAHYWM LDVMMDCSKT ENDWFEFHIV KQDGEMEKII NIKQCENAYL LLLGKKIKHH
     LARCGYVNIV EYGMQNCTTD LEKI
//
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