Basic Information | |
---|---|
Species | Arabidopsis lyrata |
Cazyme ID | 354330 |
Family | PL4 |
Protein Properties | Length: 644 Molecular Weight: 73271.5 Isoelectric Point: 4.7198 |
Chromosome | Chromosome/Scaffold: 7 Start: 7597895 End: 7600863 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
PL4 | 6 | 621 | 0 |
SVQLDVQESHVVMGNGIVKVTISKPDGFVTEISYQGVDNLLETHNEDFNRGYWDLVWSDEGAPGTTGKSERIKGTSFEVVVENEELVEISFSRKWDSSLQ DSIAPINVDKRFIMRKNVSGFYSYAIFEHLAEWPAFNLPQTRIVYKLRKDKFQYMAIADNRQRKMPLPEDRLGKRGRPLAYPEAVLLVHPVEEEFKGEVD DKYEYSCENKDLKVHGWISQNLGLGCWQIIPSNEFRSGGLSKQNLTSHVGPISLAMFLSAHYAGEDMVMKVKAGEPWKKVFGPVFTYLNCLPDKTSDPLL LWQDAKNQMLTEVQSWPYDFPASEDFAVSNKRGCISGRLLICDNDELLPANGAFVGLAPPGEVGSWQLESKGYQFWTEADADGYFAINDIREGEYNLNAY VTGWIGDYQYEQLINITAGCDIDVGNIVYEPPRDGPTVWEIGIPDRSAAEFFVPDPNPKYINKLYIGHPDRFRQYGLWERYTELYPKEDLVFTIGVSDYK KDWFFAHVTRKLEDDTYQKTTWQIKFKLENVQKNSTYKIRIALATANVAELQVRMNDDDTEKSTPMFTTGVIGHDNAIARHGIHGIYRLYNVDVPSEKLV EGENTLFLTQTMTTTG |
Full Sequence |
---|
Protein Sequence Length: 644 Download |
MSNQDSVQLD VQESHVVMGN GIVKVTISKP DGFVTEISYQ GVDNLLETHN EDFNRGYWDL 60 VWSDEGAPGT TGKSERIKGT SFEVVVENEE LVEISFSRKW DSSLQDSIAP INVDKRFIMR 120 KNVSGFYSYA IFEHLAEWPA FNLPQTRIVY KLRKDKFQYM AIADNRQRKM PLPEDRLGKR 180 GRPLAYPEAV LLVHPVEEEF KGEVDDKYEY SCENKDLKVH GWISQNLGLG CWQIIPSNEF 240 RSGGLSKQNL TSHVGPISLA MFLSAHYAGE DMVMKVKAGE PWKKVFGPVF TYLNCLPDKT 300 SDPLLLWQDA KNQMLTEVQS WPYDFPASED FAVSNKRGCI SGRLLICDND ELLPANGAFV 360 GLAPPGEVGS WQLESKGYQF WTEADADGYF AINDIREGEY NLNAYVTGWI GDYQYEQLIN 420 ITAGCDIDVG NIVYEPPRDG PTVWEIGIPD RSAAEFFVPD PNPKYINKLY IGHPDRFRQY 480 GLWERYTELY PKEDLVFTIG VSDYKKDWFF AHVTRKLEDD TYQKTTWQIK FKLENVQKNS 540 TYKIRIALAT ANVAELQVRM NDDDTEKSTP MFTTGVIGHD NAIARHGIHG IYRLYNVDVP 600 SEKLVEGENT LFLTQTMTTT GAFNGLMYDY IRLEGPPLDS NSH* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 2.0e-31 | 336 | 432 | 97 | + 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 | 6.0e-48 | 444 | 634 | 193 | + 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 | 4.0e-73 | 14 | 295 | 285 | + 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 | 5.0e-91 | 3 | 204 | 202 | + 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 |
GenBank | AAL15345.1 | 0 | 160 | 643 | 1 | 487 | AT4g24430/T22A6_260 [Arabidopsis thaliana] |
GenBank | AAU90065.1 | 0 | 160 | 643 | 1 | 487 | At4g24430 [Arabidopsis thaliana] |
RefSeq | NP_567703.4 | 0 | 1 | 643 | 1 | 646 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002301114.1 | 0 | 7 | 637 | 6 | 632 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527357.1 | 0 | 7 | 637 | 6 | 635 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
FD941014 | 257 | 385 | 641 | 0 |
CD813831 | 254 | 2 | 255 | 0 |
DY293973 | 332 | 7 | 336 | 0 |
FY792769 | 271 | 338 | 605 | 0 |
FC896579 | 281 | 70 | 348 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|