| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_031565m |
| Family | PL4 |
| Protein Properties | Length: 493 Molecular Weight: 55497 Isoelectric Point: 6.7023 |
| Chromosome | Chromosome/Scaffold: 06598 Start: 186298 End: 189639 |
| Description | Rhamnogalacturonate lyase family protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL4 | 119 | 454 | 0 |
| HEFRNGGPTKQNLTAHTGPDCLAMFHGTHYIGDEILAHFQEGEEWRKTFGPFFVYLNSTNNVSNAYNLWEDAKKQRLLEEAAWPYEFVSSSYYLTAKGLG SATGRLYVQDRFISGSLIPAKRAYVGLLAARTAGAWHTESKDYQLWVQTDSNGYFTIKNVIPGVYGLHGWVPGFIGSETQLGNLTYVPRRDGPTVWEIGF PDRTALGYYVPDVNPALFRQYGLWDRYPDMHPLSDQTFTIGINNPKKEWFFAHVDTDNKYLPLTWTIKFYLDSVTSGTYKLRLAIASATRSDLEDCKCIN AVCRHGIHGLYQLFSIGVSSSLLVKGDNSMFLTQAR | |||
| Full Sequence |
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| Protein Sequence Length: 493 Download |
| VLLDNGLVRL TILKPHGYLT GIKYGGLDNL LDLKSSQSSR GYWDINWSFP GGQERYQMMV 60 FKLRREKFHY MAISDEKQRI MPMPEDLLPG RGKQLIVPES VLLVNPINPD PRGEGSIIHE 120 FRNGGPTKQN LTAHTGPDCL AMFHGTHYIG DEILAHFQEG EEWRKTFGPF FVYLNSTNNV 180 SNAYNLWEDA KKQRLLEEAA WPYEFVSSSY YLTAKGLGSA TGRLYVQDRF ISGSLIPAKR 240 AYVGLLAART AGAWHTESKD YQLWVQTDSN GYFTIKNVIP GVYGLHGWVP GFIGSETQLG 300 NLTYVPRRDG PTVWEIGFPD RTALGYYVPD VNPALFRQYG LWDRYPDMHP LSDQTFTIGI 360 NNPKKEWFFA HVDTDNKYLP LTWTIKFYLD SVTSGTYKLR LAIASATRSD LEDCKCINAV 420 CRHGIHGLYQ LFSIGVSSSL LVKGDNSMFL TQARSGDALC GILYDYIRLE APLPSGNSCG 480 SEEGFDLDEK LI* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd10320 | RGL4_N | 9.0e-6 | 1 | 56 | 56 | + 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. | ||
| pfam06045 | Rhamnogal_lyase | 1.0e-14 | 1 | 60 | 60 | + Rhamnogalacturonate lyase family. Rhamnogalacturonate lyase (EC:4.2.2.-) degrades the rhamnogalacturonan I (RG-I) backbone of pectin. This family contains mainly members from plants, but also contains the plant pathogen Erwinia chrysanthemi. | ||
| pfam06045 | Rhamnogal_lyase | 1.0e-18 | 60 | 114 | 55 | + Rhamnogalacturonate lyase family. Rhamnogalacturonate lyase (EC:4.2.2.-) degrades the rhamnogalacturonan I (RG-I) backbone of pectin. This family contains mainly members from plants, but also contains the plant pathogen Erwinia chrysanthemi. | ||
| cd10320 | RGL4_N | 5.0e-19 | 52 | 183 | 157 | + 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 | 3.0e-38 | 314 | 470 | 173 | + 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. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI23231.1 | 1e-21 | 2 | 59 | 1 | 58 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI23231.1 | 0 | 59 | 475 | 129 | 618 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002285626.1 | 0 | 59 | 483 | 128 | 625 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002317123.1 | 6e-20 | 1 | 57 | 15 | 71 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317123.1 | 0 | 59 | 483 | 144 | 640 | predicted protein [Populus trichocarpa] |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| DY969340 | 317 | 119 | 406 | 0 |
| CO474992 | 276 | 121 | 372 | 0 |
| GW864372 | 311 | 59 | 326 | 0 |
| GT008155 | 264 | 119 | 359 | 0 |
| FC327604 | 259 | 66 | 294 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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