ID Q0V295_PHANO Unreviewed; 510 AA.
AC Q0V295;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=Glycosyl hydrolase family 13 catalytic domain-containing protein {ECO:0000259|SMART:SM00642};
GN ORFNames=SNOG_01869 {ECO:0000313|EMBL:EAT90081.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT90081.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445327; EAT90081.1; -; Genomic_DNA.
DR RefSeq; XP_001792493.1; XM_001792441.1.
DR AlphaFoldDB; Q0V295; -.
DR STRING; 321614.Q0V295; -.
DR EnsemblFungi; SNOT_01869; SNOT_01869; SNOG_01869.
DR GeneID; 5969343; -.
DR KEGG; pno:SNOG_01869; -.
DR VEuPathDB; FungiDB:JI435_018690; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_024572_2_0_1; -.
DR InParanoid; Q0V295; -.
DR OMA; FFHWYYP; -.
DR OrthoDB; 2728918at2759; -.
DR Proteomes; UP000001055; 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:SF7; ALPHA-AMYLASE 2-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT DOMAIN 13..399
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 510 AA; 57502 MW; A6F338DCBD4024A3 CRC64;
MGSEEQKPTP ENNTLLQGYE WNCPSDNKHY KRLAAEVPKL KAIGINNIWL PPGCKAANPK
GVGFDIYDLY DLGEFDQKGT RATKWGSKED LLELSKIAKE NGVGLYWDAV LNHKAGADKT
EKCRVVEVDN EDRTKEVGEP YEIEGWLGFD FAGRGDKYSS MKYHWEHFSG TDYNQANEKK
AIYKIVGDNK GWSNSVDNEG GNADYMMFAD IDYRHPEVQE DVKNWGVWIT KELGLKGFRL
DAVQHFSERF TNEWIENVRE QCGKDIFMVG EFWSGDRTVM IDWLADLDHK FSLYDSPLLN
NFARLSTTPD ADLRTVFDGS LVQAEPVNAV TVVTNHDTQP GQTMETKIEG FFVPLAYSLI
LLRKEGYPCP FYGDLYGLNE PHETPASCGG KLADLILARK LYAYGDQEDY WNDPNLIGFV
RRGTWDKPAG LACLMSNKGP GEIKMAVGEM HAGEKWTDVL GWEEGEVEID QDGYGLFKCP
GTSVAIWVKA DAQGRDQFPV NFDADIYGKA
//