y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10010628 |
Family | PL4 |
Protein Properties | Length: 335 Molecular Weight: 38609.1 Isoelectric Point: 8.7107 |
Chromosome | Chromosome/Scaffold: 296 Start: 115827 End: 118875 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 130 | 288 | 7.49695e-43 |
TEEGYLGLPMAGEAGSWQRDGKHYQFWNTTDNHGFFSIENVRPGNYGLYGFVPGVLGDYKFHGDILVTPGSHTKLGSVTYNPPRSGPTLWEIGVADRSAA EFFIPKPETVYFNKFDYTKDWYFAQVTREVKDPNDSNVTHYKATNWRINFQLEKVEVGR |
Full Sequence |
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Protein Sequence Length: 335 Download |
MPTQEDRNKG IRLAYKEAVL LNNASNTYHY SLEYQDNKVN PVGFWLIFPE LRVPYRWTHQ 60 TRTHLSRWSH SSQWKNMDTR YNSTYAWKMA WSKKRRVGLT TLSTPTTSLL DDNEELSLVN 120 SSSRIGIQCT EEGYLGLPMA GEAGSWQRDG KHYQFWNTTD NHGFFSIENV RPGNYGLYGF 180 VPGVLGDYKF HGDILVTPGS HTKLGSVTYN PPRSGPTLWE IGVADRSAAE FFIPKPETVY 240 FNKFDYTKDW YFAQVTREVK DPNDSNVTHY KATNWRINFQ LEKVEVGRTT DSEWHWLPLR 300 TPKSGEPSTI RTSHGMGPFN GVMYDYLRFE GPPT* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10317 | RGL4_C | 3.0e-8 | 219 | 330 | 176 | + 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-19 | 134 | 206 | 73 | + 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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_179847.1 | 0 | 1 | 332 | 211 | 674 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002285627.1 | 0 | 1 | 334 | 32 | 499 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
RefSeq | XP_002308510.1 | 0 | 1 | 332 | 208 | 671 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527229.1 | 0 | 1 | 332 | 205 | 667 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527245.1 | 0 | 1 | 332 | 153 | 618 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY339589 | 185 | 133 | 284 | 9.94922e-44 |
EX687792 | 192 | 133 | 290 | 8.99634e-43 |
GO538727 | 186 | 133 | 285 | 1.99965e-42 |
GE636266 | 190 | 133 | 289 | 9.99967e-42 |
CO473129 | 186 | 133 | 285 | 9.99967e-42 |
Sequence Alignments (This image is cropped. Click for full image.) |
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