| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01006463001 |
| Family | PL4 |
| Protein Properties | Length: 379 Molecular Weight: 42397.4 Isoelectric Point: 7.792 |
| Chromosome | Chromosome/Scaffold: Start: 26178737 End: 26180893 |
| Description | Rhamnogalacturonate lyase family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL4 | 1 | 362 | 0 |
| HGWISQKSGVGFWIITPSDEFRISGPLKQELTSHAGPVSLSVFTSSHYVGKPEEEIFKDGEAWKKVFGPIFIYLNSVSNKKEALSLWNDAKQQMLKEVDS WPYSFPLSQDFPKSHQRGSVQGRLLVLDKYINQAPTPASLAYVGLSLPGEAGSWQTETKGYQFWTQADKEGTFSIRAVRAGTYNLFAWVPGIMGDYKYDA IITIKPGNKIKLGNIVFEPPRHGPTLWEIGIPDRTAAEFFVPDVDPKFINKLYVKQDKHVTDDTFLGTTWQIVFDLPVVDMAATYKFRLVLAGASLAQLQ VRLNDPNATRPLLSTELIGRENLIARHGIHGLLRSYTADIPGFLFVEGCNTIYLTQTRASNS | |||
| Full Sequence |
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| Protein Sequence Length: 379 Download |
| HGWISQKSGV GFWIITPSDE FRISGPLKQE LTSHAGPVSL SVFTSSHYVG KPEEEIFKDG 60 EAWKKVFGPI FIYLNSVSNK KEALSLWNDA KQQMLKEVDS WPYSFPLSQD FPKSHQRGSV 120 QGRLLVLDKY INQAPTPASL AYVGLSLPGE AGSWQTETKG YQFWTQADKE GTFSIRAVRA 180 GTYNLFAWVP GIMGDYKYDA IITIKPGNKI KLGNIVFEPP RHGPTLWEIG IPDRTAAEFF 240 VPDVDPKFIN KLYVKQDKHV TDDTFLGTTW QIVFDLPVVD MAATYKFRLV LAGASLAQLQ 300 VRLNDPNATR PLLSTELIGR ENLIARHGIH GLLRSYTADI PGFLFVEGCN TIYLTQTRAS 360 NSFQGVMYDY IRLEGPPQ* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd10320 | RGL4_N | 3.0e-26 | 1 | 83 | 83 | + N-terminal catalytic domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold; the middle and C-terminal domains are both putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. | ||
| cd10317 | RGL4_C | 2.0e-33 | 227 | 374 | 163 | + C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. | ||
| cd10316 | RGL4_M | 2.0e-34 | 116 | 215 | 100 | + Middle domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle domain represented by this model and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI33193.1 | 1e-16 | 1 | 41 | 200 | 240 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI33193.1 | 0 | 1 | 378 | 336 | 752 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI33217.1 | 0 | 1 | 378 | 1 | 378 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002264484.1 | 0 | 1 | 378 | 180 | 596 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002306520.1 | 0 | 1 | 377 | 200 | 616 | predicted protein [Populus trichocarpa] |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EL385368 | 250 | 1 | 250 | 0 |
| GT008155 | 240 | 19 | 258 | 0 |
| DY969340 | 321 | 15 | 294 | 0 |
| DY830317 | 254 | 1 | 253 | 0 |
| GR451984 | 247 | 10 | 256 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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