Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 917084 |
Family | GH28 |
Protein Properties | Length: 382 Molecular Weight: 41624.6 Isoelectric Point: 8.476 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH28 | 49 | 367 | 0 |
AMCGSGGNSKTFLIPSNKTFLLQPLMFQGPCKSPSVQVKFDGKIVAPINKAAWSENKLFRWVSFKEIIGLTVTGSGTIHGRGSSFWKQLHFKSCNDLKIS GITSFNSPRNHISISECKRVKITKIKLVAPHDSPNTDGIDISRSSDVDIYDTIIGTGDDCVAINNGSMNINITRMNCGPGHGISVGSLGRDGEESIVENV QVTNCTFFRTDNGARIKTWPNGKGYAKNILFQGLTFRETKNPIIIDQNYVDKGRLDVEESAVAISNVTFTDIRGTSQVDEIIKIDCSKVTYCKDIVLDKI DIATVDGNKPVVECSNVYG |
Full Sequence |
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Protein Sequence Length: 382 Download |
MEIILRGVFF LTLLHSVLVN GQIYDVLKFG AKGNGITDDS KAFVTAWKAM CGSGGNSKTF 60 LIPSNKTFLL QPLMFQGPCK SPSVQVKFDG KIVAPINKAA WSENKLFRWV SFKEIIGLTV 120 TGSGTIHGRG SSFWKQLHFK SCNDLKISGI TSFNSPRNHI SISECKRVKI TKIKLVAPHD 180 SPNTDGIDIS RSSDVDIYDT IIGTGDDCVA INNGSMNINI TRMNCGPGHG ISVGSLGRDG 240 EESIVENVQV TNCTFFRTDN GARIKTWPNG KGYAKNILFQ GLTFRETKNP IIIDQNYVDK 300 GRLDVEESAV AISNVTFTDI RGTSQVDEII KIDCSKVTYC KDIVLDKIDI ATVDGNKPVV 360 ECSNVYGKSI NANEANGCFK T* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00295 | Glyco_hydro_28 | 6.0e-75 | 51 | 365 | 329 | + Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism. | ||
PLN02188 | PLN02188 | 8.0e-83 | 23 | 370 | 367 | + polygalacturonase/glycoside hydrolase family protein | ||
PLN02793 | PLN02793 | 1.0e-85 | 22 | 379 | 375 | + Probable polygalacturonase | ||
PLN03003 | PLN03003 | 4.0e-100 | 25 | 369 | 359 | + Probable polygalacturonase At3g15720 | ||
PLN03010 | PLN03010 | 3.0e-154 | 1 | 381 | 382 | + polygalacturonase |
Gene Ontology | |
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GO Term | Description |
GO:0004650 | polygalacturonase activity |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAC79138.1 | 0 | 1 | 380 | 1 | 380 | putative polygalacturonase [Arabidopsis thaliana] |
EMBL | CAA20037.1 | 0 | 18 | 380 | 8 | 369 | putative polygalacturonase [Arabidopsis thaliana] |
RefSeq | NP_198105.2 | 0 | 2 | 381 | 31 | 411 | glycoside hydrolase family 28 protein / polygalacturonase (pectinase) family protein [Arabidopsis thaliana] |
RefSeq | NP_199296.1 | 0 | 50 | 380 | 1 | 331 | glycoside hydrolase family 28 protein / polygalacturonase (pectinase) family protein [Arabidopsis thaliana] |
RefSeq | NP_199297.1 | 0 | 1 | 381 | 1 | 381 | glycoside hydrolase family 28 protein / polygalacturonase (pectinase) family protein [Arabidopsis thaliana] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2iq7_G | 3e-17 | 133 | 365 | 102 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2iq7_F | 3e-17 | 133 | 365 | 102 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2iq7_E | 3e-17 | 133 | 365 | 102 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2iq7_D | 3e-17 | 133 | 365 | 102 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2iq7_C | 3e-17 | 133 | 365 | 102 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |