ID K9G3S7_PEND1 Unreviewed; 535 AA.
AC K9G3S7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Glycosyl hydrolase family 13 catalytic domain-containing protein {ECO:0000259|SMART:SM00642};
GN ORFNames=PDIP_40150 {ECO:0000313|EMBL:EKV15562.1};
OS Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV15562.1, ECO:0000313|Proteomes:UP000009886};
RN [1] {ECO:0000313|Proteomes:UP000009886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV15562.1}.
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DR EMBL; AKCU01000271; EKV15562.1; -; Genomic_DNA.
DR RefSeq; XP_014535006.1; XM_014679520.1.
DR AlphaFoldDB; K9G3S7; -.
DR GeneID; 26232333; -.
DR KEGG; pdp:PDIP_40150; -.
DR HOGENOM; CLU_024572_2_0_1; -.
DR OrthoDB; 2728918at2759; -.
DR Proteomes; UP000009886; 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;
FT DOMAIN 37..425
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 535 AA; 60805 MW; 6B37EA9DF9C98908 CRC64;
MPFLWCGSRQ KGQKWKQIEE AAANLDQLPS WNTPDNSLIL QTFEWHVPAD RQHWRRLQDR
LPEYKAIGVD QIWVPPGCKG MDANGNGYDI YDLYDLGEFD QKGAVPTKWG TKRELEDLMC
QAQHLGIGVI WDAVLNHKAG ADYPEPFQAV KVDPKRRDLE ISKPTEVNGW TGFDFAGRND
MYSSMKYHWQ HFSGVDWDDK SKQSAIYKIV ASNKDWAQDV STEFGNYDYL MFSDLDLAHP
EVRADLLQWG TWITKCLNLN GMRLDAAKHF STEFQHAFVQ HIRKTVNPDF FAIGEYWTGH
LPSLLGYLDK VENDLIAYDV PLLERFSKLS HAQAPDLRGI FKDTLVQCRP DHAVTLVANH
DTQPGQMLET PVSPSFKLLA YALVLLRKDG QPCVFYGDLY GIRANVDNPM TPSCNGLLPV
LTQARKLYAY GEQQDYFNQP NCIGFVRYGN ARHLSGLACV ISNAGPGAQR MYVGQQHADE
QWTDVLHPNM KPVIINKTGY GNFGVQGMSA SVWVNSAAVD RDNLKRDFNV NIYDN
//
