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Database: UniProt
Entry: A0A194Q2R2_PAPXU
LinkDB: A0A194Q2R2_PAPXU
Original site: A0A194Q2R2_PAPXU 
ID   A0A194Q2R2_PAPXU        Unreviewed;       398 AA.
AC   A0A194Q2R2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Alpha-amylase 4N {ECO:0000313|EMBL:KPI99289.1};
GN   ORFNames=RR46_05473 {ECO:0000313|EMBL:KPI99289.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI99289.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPI99289.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI99289.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPI99289.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; KQ459580; KPI99289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194Q2R2; -.
DR   STRING; 66420.A0A194Q2R2; -.
DR   Proteomes; UP000053268; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
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; 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; PF02806; Alpha-amylase_C; 1.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053268}.
FT   DOMAIN          26..289
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          298..386
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   398 AA;  45761 MW;  B077E6452683A358 CRC64;
     MVLILRACSC DHHHHHRRTN QLPDRSTIVH LFEWKWKDIA EECERFLAPK GYGGVQISPP
     SENVIINLSN GKRTWYERYQ VMSYKLDTRS GDRDDFVNMT TRCNKVGVRV DAAKHMWPRD
     LREIYSRLRT LNTDYGFPPN TKPYIYQEVI YFGNEAIKPE EYTTLGDVTE FRASRNALKW
     LVSWGEQWGL SPSDTALTFI DNHDTQRSGN VLTYRESRPY KAAVAFMLAH PYGVPRIMSS
     YAFHSTDQGP PSDDKENIIS PSINEDDTCG NGWVCEHRWR QIYQMVAFRN AVRYTAVQNW
     WDNGSCQIAF SRGEKGFIAF NGEAYPLNAT LKTGLPKGEY CDVITGKKRG NSCTGTKVIV
     NDNGLADVYI SNHAEDMHLA IHVGIENELK KEYDSKYQ
//
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