Basic Information | |
---|---|
Species | Arabidopsis lyrata |
Cazyme ID | 888241 |
Family | PL4 |
Protein Properties | Length: 676 Molecular Weight: 76607.7 Isoelectric Point: 6.6616 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
PL4 | 48 | 656 | 0 |
GVHLHIHDRYVLMDNGILQVTLSKPGGIITGIKYNGIDNVLEVRNKETNRGYWDLHWNEPGGKGIFDVISGGTFRVIVETEEQVEISFLRTWDPSLEGKF IPLNIDKRFVMLRGSSGVYSYGIYEHLKDWPGFELGETRIAFKLRKDKFHYMAVADDRKRIMPFPDDLCKGRCQTLDYQEASLLTAPCDPRLQGEVDDKY QYSCENKDLRVHGWISFDPPVGFWQITPSNEFRSGGPLKQNLTSHVGPTTLAVFHSTHYAGKTMMPRFEHGEPWKKVYGPVFIYLNSTANGDDPLCLWDD AKIKMMAEVESWPYSFVASDDYPKSEERGTARGRLLIRDRFINSDLISAGGAYVGLAPPGDSGSWQIECKGYQFWAIADEAGYFSIGNARPGEYNLYAWV PGFIGDYHNGTIVTVTSGCMIEMGDIVYEPPRDGPTLWEIGIPDRKASEFFIPDPDLTLVNRVLVHDQDRFRQYGLWKRYTDLYPNADLIYTVGVSDYRR DWFFAHVPRKKGDVHEGTTWQIRFNLENIDQKANYKLQVAIASATLAELQIRVNDAEAIRPLFTTGLIGRDNSIARHGIHGVYMLYAVNVPGNRLVQGDN TIFLKQPRC |
Full Sequence |
---|
Protein Sequence Length: 676 Download |
MKKLAGRLLH RFTNHETAFN AGHHCSQGTD QGTSGLSHRK DLNMPSQGVH LHIHDRYVLM 60 DNGILQVTLS KPGGIITGIK YNGIDNVLEV RNKETNRGYW DLHWNEPGGK GIFDVISGGT 120 FRVIVETEEQ VEISFLRTWD PSLEGKFIPL NIDKRFVMLR GSSGVYSYGI YEHLKDWPGF 180 ELGETRIAFK LRKDKFHYMA VADDRKRIMP FPDDLCKGRC QTLDYQEASL LTAPCDPRLQ 240 GEVDDKYQYS CENKDLRVHG WISFDPPVGF WQITPSNEFR SGGPLKQNLT SHVGPTTLAV 300 FHSTHYAGKT MMPRFEHGEP WKKVYGPVFI YLNSTANGDD PLCLWDDAKI KMMAEVESWP 360 YSFVASDDYP KSEERGTARG RLLIRDRFIN SDLISAGGAY VGLAPPGDSG SWQIECKGYQ 420 FWAIADEAGY FSIGNARPGE YNLYAWVPGF IGDYHNGTIV TVTSGCMIEM GDIVYEPPRD 480 GPTLWEIGIP DRKASEFFIP DPDLTLVNRV LVHDQDRFRQ YGLWKRYTDL YPNADLIYTV 540 GVSDYRRDWF FAHVPRKKGD VHEGTTWQIR FNLENIDQKA NYKLQVAIAS ATLAELQIRV 600 NDAEAIRPLF TTGLIGRDNS IARHGIHGVY MLYAVNVPGN RLVQGDNTIF LKQPRCNGPF 660 QGIMYDYIRL EGPPS* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 1.0e-27 | 374 | 473 | 100 | + 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 | 1.0e-48 | 485 | 671 | 189 | + 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-83 | 49 | 344 | 302 | + 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 | 8.0e-104 | 43 | 243 | 201 | + 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 | AAB60743.1 | 0 | 44 | 675 | 1 | 728 | F21M12.30 gene product [Arabidopsis thaliana] |
RefSeq | NP_172462.2 | 0 | 1 | 675 | 1 | 675 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002306520.1 | 0 | 60 | 674 | 1 | 616 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 44 | 673 | 1 | 631 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527353.1 | 0 | 44 | 675 | 1 | 635 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO206588 | 225 | 164 | 388 | 0 |
DK517187 | 240 | 435 | 674 | 0 |
EG452795 | 227 | 450 | 676 | 0 |
CN826718 | 235 | 270 | 500 | 0 |
CN826718 | 21 | 490 | 510 | 1.7 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|