ID   A0A915NR16_9BILA        Unreviewed;       255 AA.
AC   A0A915NR16;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 10.
DE   RecName: Full=Probable pectate lyase F {ECO:0000256|ARBA:ARBA00039895};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
OS   Meloidogyne floridensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=298350 {ECO:0000313|Proteomes:UP000887560, ECO:0000313|WBParaSite:scf7180000421093.g6292};
RN   [1] {ECO:0000313|WBParaSite:scf7180000421093.g6292}
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}.
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   WBParaSite; scf7180000421093.g6292; scf7180000421093.g6292; scf7180000421093.g6292.
DR   Proteomes; UP000887560; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:TreeGrafter.
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:UP000887560};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..255
FT                   /note="Probable pectate lyase F"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5036965492"
SQ   SEQUENCE   255 AA;  27653 MW;  48C3AF3C1AEEDA5A CRC64;
     MSIFVPIIFM LLQLLQGCQS FGPAAKKTIT LQSKLVVTKN FDCGFTRYIP DPKKMGDGGA
     NEFQQPVIEV RNGATLSNCI IGAKEGFKAA DGVHCEGSCT LKNVWHEKVG EDAVTFLGTN
     PNNVYIIEGG GAINANGKVV QFNGAGTAKI NNFYMKDCTY GIASCGNCQA QFSRRIEVTN
     LKAENLKAGQ FIVAVNSNFN DQAILRNIHI LGNSAKQVFP CKIFNGVKGN GNFKLVKMGA
     DGKHCKYNNN DIHFN
//