ID A0A1K1PED1_9BACL Unreviewed; 1020 AA.
AC A0A1K1PED1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Polygalacturonase {ECO:0000313|EMBL:SFW45951.1};
GN ORFNames=SAMN02799630_03343 {ECO:0000313|EMBL:SFW45951.1};
OS Paenibacillus sp. UNCCL117.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1502764 {ECO:0000313|EMBL:SFW45951.1, ECO:0000313|Proteomes:UP000182480};
RN [1] {ECO:0000313|EMBL:SFW45951.1, ECO:0000313|Proteomes:UP000182480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCCL117 {ECO:0000313|EMBL:SFW45951.1,
RC ECO:0000313|Proteomes:UP000182480};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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DR EMBL; FPIU01000011; SFW45951.1; -; Genomic_DNA.
DR RefSeq; WP_072331669.1; NZ_FPIU01000011.1.
DR AlphaFoldDB; A0A1K1PED1; -.
DR STRING; 1502764.SAMN02799630_03343; -.
DR OrthoDB; 9795222at2; -.
DR Proteomes; UP000182480; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 1.
DR Gene3D; 2.60.40.60; Cadherins; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR Pfam; PF06439; 3keto-disac_hyd; 2.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50268; CADHERIN_2; 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:UP000182480};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1020
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038602251"
FT DOMAIN 751..849
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 1020 AA; 109748 MW; 5B409403BB2A8CD5 CRC64;
MFTRTRKAVS LLVMLAIMLT GFLPRAAEAI ESTETYTISS TDDAAPEFVE QIAAAPTTIQ
NYPMPSIYTA SSVFSLKADN QAVPVINYLP DYDYAQFSFA GKVTIEVTAN EPITSYSISP
LAKNIEGTVN GSKLTFSLAS STYVIVTIND ARKKIVIAAD PLETDIPPST GAGIYNVTQS
PYNADKTGNS MASAGIQRAI DAAHQAGGGI VFVPPGVYKS GNLTLKSNVT FYVAGGAVIV
GTGKGEDYVN DFRKDSRNAD GTYFIRTAVN SSNITIRGRG TIDGKGIAMR ERKMPAPNKN
EGFLNNLLVP LATSNFTFDG LILRDAGFWS FMVVRSDNVT IKNLKGFQDL YKIENDVIDI
NESQNVLVKH AIAISDDDTY STKTWLQTGM SKGWPGGLEH LENVVFDDAL AWTRCAAFKI
GMGVAQAQIG VTIRNSYVYQ SARALLIDHG YQYNTLPKEG YAQNVTFENI DIERVGINQF
GNYWLGVSTS TSGDVSNVIV KNVNVRELGS QNSRISGNAT KGGMVNGVLF SDIYVKGQLA
TTLSDLKVTV GNNVNGVTII NSKPPLFSDD FEDGNTMGWT AVTGGWNVPT VGTNKVLSSG
SQTTTSLITA NAGGSWKDYA YQARVRMPVT NANAGIVFRV KDANNYYMYR IHSANQTLEL
YKSVNGQLTS VATTPFTALE KQSYTVKAVI EGNKISCYVD GELKMTWTNP TTELTTGGIG
FRTTSAGVHF DDAIVSPINK APANIALSHN SVVENTTAGG LVGTFSTSDP DAGEAFAYML
TAGAGDADNG SFTVSDDQLF LNVTPDFEAK NSYSIRVRSI DSGGMYVEKS FTIHVTDVSE
PPANPGPTTT RFSDNFEGGN TTDWSSASGS WTVTTDGTKV LTQNNSTTAL ITAGSSWTDY
TYEAKVKMPI ANANAGLVFR VQDANNYYMY RVNSSNQKLE LYKSVNQVLT LVSSTPFTAQ
PNQWYTIKAS IQGNTITGYV DGVVKMKWTN PVTELTAGKI GFRTTSAGVS FDDVLVVSPA
//