y
Basic Information | |
---|---|
Species | Linum usitatissimum |
Cazyme ID | Lus10030233 |
Family | PL4 |
Protein Properties | Length: 629 Molecular Weight: 71035.8 Isoelectric Point: 5.3879 |
Chromosome | Chromosome/Scaffold: 217 Start: 343919 End: 347357 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
PL4 | 6 | 603 | 0 |
VKLHIDNNHVVLDNGILKLTISKPQGIVTGITYNGSTNLLEVRNDEIDRGYWDLVWSKEGSTGTKGTQERISGTEFSVIVENEGQVEVSFARTWDPSLEG QLPSLNIDKRFILLRNSSGFYSYAIFEHLPEWTPFHLPQVRIVFKLNKDKFHYMAVGDSRQRFMPLPDDRLPERCKELDFPEAVLLVNPVEPQFQGEVDD KYQYSCENKDLKVHGWISSDPAVGFWQITPSNEFRSGGLVKQNLTSHCGPINLAMFLSAHYAGDDMVLKLKPGEGWKKVLGPVFMYLNTVAADDHGGGKI DPLLSLWEDAKQQSTKYHKSYRCGSETTVMPGNGGYVGLAPPGEVGSWQTDGKGYQFWSEADEQGNFSISNIRPGEYNLYAWIPGFIGDYKYDSPITIAP GSDMELGDVVYKPPRDGPTLWEIGFPDRSASGFYVPDADPVYSNKLFLGHPDRFRQYGLWERYIELYPKEDLVYTIGKSDWTKDWFFAHIPRRTNEGEYE PTTWQIKFRLDNKHNKSSSNYKLRIALATANVAELEVRINDPPQMGNPALFTTGVIGHDNTIARHGIHGLYRLYSVDVPASLLVQDNTFYFTQTQTKS |
Full Sequence |
---|
Protein Sequence Length: 629 Download |
MSNLGVKLHI DNNHVVLDNG ILKLTISKPQ GIVTGITYNG STNLLEVRND EIDRGYWDLV 60 WSKEGSTGTK GTQERISGTE FSVIVENEGQ VEVSFARTWD PSLEGQLPSL NIDKRFILLR 120 NSSGFYSYAI FEHLPEWTPF HLPQVRIVFK LNKDKFHYMA VGDSRQRFMP LPDDRLPERC 180 KELDFPEAVL LVNPVEPQFQ GEVDDKYQYS CENKDLKVHG WISSDPAVGF WQITPSNEFR 240 SGGLVKQNLT SHCGPINLAM FLSAHYAGDD MVLKLKPGEG WKKVLGPVFM YLNTVAADDH 300 GGGKIDPLLS LWEDAKQQST KYHKSYRCGS ETTVMPGNGG YVGLAPPGEV GSWQTDGKGY 360 QFWSEADEQG NFSISNIRPG EYNLYAWIPG FIGDYKYDSP ITIAPGSDME LGDVVYKPPR 420 DGPTLWEIGF PDRSASGFYV PDADPVYSNK LFLGHPDRFR QYGLWERYIE LYPKEDLVYT 480 IGKSDWTKDW FFAHIPRRTN EGEYEPTTWQ IKFRLDNKHN KSSSNYKLRI ALATANVAEL 540 EVRINDPPQM GNPALFTTGV IGHDNTIARH GIHGLYRLYS VDVPASLLVQ DNTFYFTQTQ 600 TKSPSSAPFQ GAFQGIMYDY VRLESLSE* 660 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 6.0e-27 | 335 | 413 | 79 | + 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-43 | 426 | 624 | 202 | + 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. | ||
cd10320 | RGL4_N | 1.0e-74 | 6 | 299 | 297 | + 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 | 9.0e-92 | 1 | 203 | 203 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI19298.1 | 0 | 1 | 624 | 1 | 642 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_567703.4 | 0 | 1 | 624 | 1 | 637 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002301114.1 | 0 | 1 | 624 | 1 | 629 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 5 | 624 | 5 | 631 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 1 | 624 | 1 | 632 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
DY293973 | 326 | 1 | 325 | 0 |
DW479599 | 295 | 1 | 295 | 0 |
DW479600 | 302 | 1 | 302 | 0 |
DT552229 | 299 | 17 | 315 | 0 |
FC887900 | 272 | 1 | 272 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|