Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma01g02560.1 |
Family | PL4 |
Protein Properties | Length: 673 Molecular Weight: 76225.2 Isoelectric Point: 8.9295 |
Chromosome | Chromosome/Scaffold: 01 Start: 2089450 End: 2097520 |
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 | |||
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Family | Start | End | Evalue |
PL4 | 47 | 650 | 0 |
TENPHQVVISNGIVSLNLSKPEGHIIGIYNGINNLLEPKNKEDDRGYLDVVWNEPGKPGIFERIDGTHFSVIAANENIVEISFLRTWTASMKGSSVPMNI DKRYILRRGDYGFYSYAIFNRPSGLPAVEVYQIRIVFKLDEARFHYMAISDTRQRNMPSMRDRLSGQSLAYPEAVLLTHASEPQFKGEVDDKYQYSSENK DNTVHGWITQDDSAPVGFWLITPSNEFRHAGPIKQDLTSHVGPTTLSMFVSTHYAGKEVAMVFGEGETYKKVFGPVFVYLNSVPNKSQFRSLWSDAVEQL SNEVRRWPYDFVGSKDFLPPNQRGTVTGRLLVLDGGKRAQPANNAYVGLALPGDAGSWQRESKGYQFWIQADKDGHFLIQNIVPGDYNLYAWVPGFIGDY RYQTKITIKPGCNINLNSLVYNPPRNGPTLWEIGIPDRSAAEFYIPDPNPKFTNRLFQNDSQDKFRQYGLWERYTELYPNHDLVYTVGVSDYHNDWFYAQ VTRSTPEKTFVPTTWQIQFQLKNIIMPGNYTLQVGLASANNARLEVRFNDQNAKLPHFSTGLTGDDNAIARHGIHGLYRLYTIAVGSNHLVKGKNTIYLT QSKG |
Full Sequence |
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Protein Sequence Length: 673 Download |
MKVERVSIFQ WWVRVAVQLS LILLGAFSDR VSSIRSVSTS PPVKLNTENP HQVVISNGIV 60 SLNLSKPEGH IIGIYNGINN LLEPKNKEDD RGYLDVVWNE PGKPGIFERI DGTHFSVIAA 120 NENIVEISFL RTWTASMKGS SVPMNIDKRY ILRRGDYGFY SYAIFNRPSG LPAVEVYQIR 180 IVFKLDEARF HYMAISDTRQ RNMPSMRDRL SGQSLAYPEA VLLTHASEPQ FKGEVDDKYQ 240 YSSENKDNTV HGWITQDDSA PVGFWLITPS NEFRHAGPIK QDLTSHVGPT TLSMFVSTHY 300 AGKEVAMVFG EGETYKKVFG PVFVYLNSVP NKSQFRSLWS DAVEQLSNEV RRWPYDFVGS 360 KDFLPPNQRG TVTGRLLVLD GGKRAQPANN AYVGLALPGD AGSWQRESKG YQFWIQADKD 420 GHFLIQNIVP GDYNLYAWVP GFIGDYRYQT KITIKPGCNI NLNSLVYNPP RNGPTLWEIG 480 IPDRSAAEFY IPDPNPKFTN RLFQNDSQDK FRQYGLWERY TELYPNHDLV YTVGVSDYHN 540 DWFYAQVTRS TPEKTFVPTT WQIQFQLKNI IMPGNYTLQV GLASANNARL EVRFNDQNAK 600 LPHFSTGLTG DDNAIARHGI HGLYRLYTIA VGSNHLVKGK NTIYLTQSKG IGPFMGLMYD 660 YVRLESPPIK ST* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 1.0e-33 | 368 | 465 | 98 | + 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. | ||
cd10317 | RGL4_C | 2.0e-50 | 477 | 665 | 190 | + 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. | ||
pfam06045 | Rhamnogal_lyase | 4.0e-67 | 52 | 235 | 187 | + 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 | 1.0e-67 | 52 | 334 | 289 | + 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. |
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 | 43 | 667 | 52 | 674 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002308510.1 | 0 | 36 | 667 | 40 | 671 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002319997.1 | 0 | 53 | 668 | 1 | 618 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527245.1 | 0 | 53 | 667 | 2 | 618 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527352.1 | 0 | 41 | 669 | 4 | 633 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY969340 | 319 | 267 | 585 | 0 |
GW864372 | 313 | 181 | 489 | 0 |
EL409069 | 280 | 380 | 659 | 0 |
GO374104 | 313 | 361 | 667 | 0 |
JG640880 | 275 | 189 | 459 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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