ID   PGLR2_ASPAC             Reviewed;         369 AA.
AC   Q70HJ4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Probable endopolygalacturonase II;
DE            Short=EPG-II;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase 2;
DE   AltName: Full=Polygalacturonase II;
DE            Short=PG-II;
DE   AltName: Full=Polygalacturonase X2;
DE   Flags: Precursor;
GN   Name=pgaII; Synonyms=pg2;
OS   Aspergillus aculeatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schnorr K.M., Kauppinen S.;
RT   "Molecular and biochemical characterization of three polygalacturonases
RT   from the filamentous fungus Aspergillus aculeatus.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC       Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC       the smooth region of the plant cell wall (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC         galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ581481; CAE46194.1; -; mRNA.
DR   AlphaFoldDB; Q70HJ4; -.
DR   SMR; Q70HJ4; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   VEuPathDB; FungiDB:ASPACDRAFT_41638; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0004650; F:polygalacturonase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SMART; SM00710; PbH1; 7.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..31
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000393626"
FT   CHAIN           32..369
FT                   /note="Probable endopolygalacturonase II"
FT                   /id="PRO_0000393627"
FT   REPEAT          141..162
FT                   /note="PbH1 1"
FT   REPEAT          163..193
FT                   /note="PbH1 2"
FT   REPEAT          194..215
FT                   /note="PbH1 3"
FT   REPEAT          216..236
FT                   /note="PbH1 4"
FT   REPEAT          245..266
FT                   /note="PbH1 5"
FT   REPEAT          274..296
FT                   /note="PbH1 6"
FT   REPEAT          308..353
FT                   /note="PbH1 7"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        210..226
FT                   /evidence="ECO:0000250"
FT   DISULFID        336..341
FT                   /evidence="ECO:0000250"
FT   DISULFID        360..369
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  38064 MW;  806900F104F16C60 CRC64;
     MHSFQLLGLA AVGSVVSAAP TASRVSDLVK KSSSTCTFTS ASEASETSSS CSNVVLSNIE
     VPAGETLDLS DAADGATITF EGTTSFGYEE WDGPLIRFGG KQLTITQSDG AVIDGDGSRW
     WDSEGTNGGK TKPKFMYVHD VEDSTIKGLQ IKNTPVQAIS VQATNVYLTD ITIDNSDGDD
     NGGHNTDGFD ISESTGVYIS GATVKNQDDC IAINSGENIL FTGGTCSGGH GLSIGSVGGR
     DDNTVKNVTI SDSTVTDSAN GVRIKTIYGD TGDVSEITYS NIQLSGITDY GIVIEQDYEN
     GSPTGTPSTG VPITDVTVDG VTGSIEDDAV QVYILCGDGS CSDWTWSGVD ITGGETSSDC
     ENVPSGASC