ID   A0A915D3T0_9BILA        Unreviewed;       169 AA.
AC   A0A915D3T0;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 11.
DE   RecName: Full=Probable pectate lyase F {ECO:0000256|ARBA:ARBA00039895};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
OS   Ditylenchus dipsaci.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Sphaerularioidea; Anguinidae; Anguininae;
OC   Ditylenchus.
OX   NCBI_TaxID=166011 {ECO:0000313|Proteomes:UP000887574, ECO:0000313|WBParaSite:jg15264};
RN   [1] {ECO:0000313|WBParaSite:jg15264}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) to UniProtKB.
CC   -!- FUNCTION: Pectinolytic enzyme consist of four classes of enzymes:
CC       pectin lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the
CC       most important in depolymerization of pectin, since it cleaves internal
CC       glycosidic bonds of highly methylated pectins. Favors pectate, the
CC       anion, over pectin, the methyl ester. {ECO:0000256|ARBA:ARBA00025679}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC         oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC         their non-reducing ends.; EC=4.2.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000695};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000256|ARBA:ARBA00006463}.
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DR   WBParaSite; jg15264; jg15264; jg15264.
DR   Proteomes; UP000887574; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR004898; Pectate_lyase_PlyH/PlyE-like.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR33407; PECTATE LYASE F-RELATED; 1.
DR   PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000887574};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..169
FT                   /note="Probable pectate lyase F"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5036710589"
SQ   SEQUENCE   169 AA;  17648 MW;  DCCA14654FDF52F4 CRC64;
     MYNFSFLLIL FLLIATFNSV LAAFPTATDC TPVDKTFPVA SGQTYNGQNK CLTACPGLGS
     GNQDENQMAI FLVQDGGKVI NVIFGDDGAD GIHCKGSCTI LNCFWTNVGE DAATFRGGAG
     SNSVVDGGGA KGADDKCFQM DGGGTVTIKN FECDQCGKLI RSCGNCPRV
//