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Database: UniProt
Entry: A0A1J9S1V3_9PEZI
LinkDB: A0A1J9S1V3_9PEZI
Original site: A0A1J9S1V3_9PEZI 
ID   A0A1J9S1V3_9PEZI        Unreviewed;       534 AA.
AC   A0A1J9S1V3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Glycoside hydrolase family 13 protein {ECO:0000313|EMBL:OJD34559.1};
GN   ORFNames=BKCO1_2200097 {ECO:0000313|EMBL:OJD34559.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD34559.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD34559.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD34559.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OJD34559.1}.
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DR   EMBL; MNUE01000022; OJD34559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9S1V3; -.
DR   STRING; 236234.A0A1J9S1V3; -.
DR   OrthoDB; 2728918at2759; -.
DR   Proteomes; UP000183809; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR   Gene3D; 2.40.30.140; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013776; A-amylase_thermo.
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   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:OJD34559.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT   DOMAIN          16..408
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   534 AA;  58943 MW;  5A99F7E71BDD6807 CRC64;
     MGDPKDEERK PTPENGTLFQ AFEWNVPADG KHWKRLIAAL PSLKYIGISN IWIPPACKAA
     SPQGNGYDVY DLYDLGEFDQ KGGTRTKWGS FDELKQLSAK ASEVGIGLYF DAVLNHKAGA
     DQKEKCQAIE VDPNDRTKEV SEPYEIEGWL GFDFPGRGDQ YSSQKYHWYH FTGTDYNAAN
     EKNAIYKIQG EGKGWSSSVD KEQGNADYMM FADVDYSHDE VIADVKNWGV WVTKTLGLKG
     FRLDAVQHFS ERFTNEWVKA LHAECGTDVF LVGEFWVGDA ATLTAWLDKM EHKFALFDAP
     LLYNFHNAGG ADSSDLRKIF DGTLLQHEPV NAVTVVANHD TQPGQTVETP VADFFKPLAY
     ALILLRPDGY PCPFYGDLYG LLPGPDTPFD DPAPPACSGK LPDLIKSRQL YAYGACEDYF
     DGEAGADGDK PVTCIGWVRR GTWDRGDGGC AVVMSNAGPG TRHMFVGDGT GGQVWTDVLG
     WARDGDSDAE VTVGDDGFGD FTCGELSVSV WVRKDAGGRD QFPVKFDTDI YKMA
//
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