Basic Information | |
---|---|
Species | Citrus sinensis |
Cazyme ID | orange1.1g047026m |
Family | PL4 |
Protein Properties | Length: 597 Molecular Weight: 67662.6 Isoelectric Point: 6.7204 |
Chromosome | Chromosome/Scaffold: 00007 Start: 1880270 End: 1883445 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
PL4 | 9 | 571 | 0 |
SSESSRGYWDINWNLPEGQDRYQLLNGGEYSVINMSNDSVEVSFRSSYDPSIQSTKLPLSVDIRYILRSGVSGFHCYSIYERPPGCRAFDLAQTRLAFKL RRDKFHYMAITDAKQRIMPLPEDLLPGRGKQLIVPESVLLVNPINPDLKGEVDDKYQYSMDNKDGGLHGWISSGPIIGFWIIFPSHEFRNGGPTKQNLTV HTGPTCLAMFHGTHYIGNEILAHFQEGEAWRKVFGPIFVYLNSTSDASKAYNLWIDAKKQRLLQEAAWPYDFVSSPYYLTANERGSATGRFFVQDKFVSS SLIPAKYAYIGLSSARTEGGWQTESKDYQFWVQTDSKGNFTVKNVVPGVYGLHGWVPGFIGDYLDKALVTISAGSQTELGNLTYVPLRNGPTVWEIGFPD RTALGCYVPDVNPMYVNKLFLNSPEKYRQYGLWDRYTDVHPESDQFFTVGVNDPKKDWFFAHVDRRGPDNKYLPTTWTIKFHLDSIIKGTYNLRLAIASA TRSDLEIFVNYIDQGHLVYQEMNLGMDNTVCRHGIHGLYQLFSIHVSSLLLIKGDNSMFLVQS |
Full Sequence |
---|
Protein Sequence Length: 597 Download |
MDNLLDLKSS ESSRGYWDIN WNLPEGQDRY QLLNGGEYSV INMSNDSVEV SFRSSYDPSI 60 QSTKLPLSVD IRYILRSGVS GFHCYSIYER PPGCRAFDLA QTRLAFKLRR DKFHYMAITD 120 AKQRIMPLPE DLLPGRGKQL IVPESVLLVN PINPDLKGEV DDKYQYSMDN KDGGLHGWIS 180 SGPIIGFWII FPSHEFRNGG PTKQNLTVHT GPTCLAMFHG THYIGNEILA HFQEGEAWRK 240 VFGPIFVYLN STSDASKAYN LWIDAKKQRL LQEAAWPYDF VSSPYYLTAN ERGSATGRFF 300 VQDKFVSSSL IPAKYAYIGL SSARTEGGWQ TESKDYQFWV QTDSKGNFTV KNVVPGVYGL 360 HGWVPGFIGD YLDKALVTIS AGSQTELGNL TYVPLRNGPT VWEIGFPDRT ALGCYVPDVN 420 PMYVNKLFLN SPEKYRQYGL WDRYTDVHPE SDQFFTVGVN DPKKDWFFAH VDRRGPDNKY 480 LPTTWTIKFH LDSIIKGTYN LRLAIASATR SDLEIFVNYI DQGHLVYQEM NLGMDNTVCR 540 HGIHGLYQLF SIHVSSLLLI KGDNSMFLVQ SRSGDPVCGV LYDYLRLEAP TSSFMI* 600 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 6.0e-27 | 291 | 390 | 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 | 3.0e-35 | 402 | 588 | 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. | ||
pfam06045 | Rhamnogal_lyase | 7.0e-54 | 2 | 160 | 159 | + 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 | 2.0e-56 | 3 | 258 | 257 | + 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 | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI23231.1 | 0 | 1 | 593 | 26 | 618 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001763359.1 | 0 | 1 | 594 | 27 | 624 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769727.1 | 0 | 1 | 591 | 30 | 621 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002285626.1 | 0 | 1 | 592 | 25 | 617 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002317123.1 | 0 | 1 | 592 | 41 | 631 | predicted protein [Populus trichocarpa] |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
GE473226 | 288 | 146 | 433 | 0 |
DV995349 | 288 | 146 | 433 | 0 |
CO473731 | 278 | 146 | 423 | 0 |
DY969340 | 318 | 193 | 508 | 0 |
GW864372 | 308 | 104 | 411 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|