ID A0A0K9PY52_ZOSMR Unreviewed; 459 AA.
AC A0A0K9PY52;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Polygalacturonase, family GH28 {ECO:0000313|EMBL:KMZ73135.1};
GN ORFNames=ZOSMA_153G00270 {ECO:0000313|EMBL:KMZ73135.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ73135.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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:KMZ73135.1}.
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DR EMBL; LFYR01000601; KMZ73135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PY52; -.
DR STRING; 29655.A0A0K9PY52; -.
DR OMA; PCHWGKA; -.
DR OrthoDB; 445147at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31339:SF0; PECTIN LYASE-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..459
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005527993"
SQ SEQUENCE 459 AA; 50749 MW; 34198D0907497605 CRC64;
MATLQLYFLL FLLNPLTIQL KSQLLPITTT ISVLDFGATA DGITFDTVAI QSAINQISSS
GGGTLNFPTN LSFLTATLFL KSGVTLEVEE GARIIAGVRE EDYPPEHRLW YLIVADGEKN
VGIKGKGIID GRGEMFVQRK DPKKNIMVSW NQTGNCNGDE CRPKLIGFLD STGVKVEEIN
LLQPALWCLH LVRCNDTVIG GVSINGDFNS PNNDGIDIED SNNTVITGCK IDTGDDAICP
KTYTTPMHNL TVRNCWIKTK SSGVKFGSGS WFDFKNMLFD NLTIFDSHRG LALQIRDGGD
VSNITFSNIE LRTRYYDPSW WGRAEPIYIT TCPRDQSSKA GSISNLRFVN ISAVSENGVF
MSGSEGAELS DVSFVNISIT YQRWTDFAGG LDDYRPGCQG LVQHNSTPGI IMEYVSGFEI
RHANMRWSHS SILNGWNNPL QFRSFTVSNL SFHDLNLSI
//
