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Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.011G006200.1 |
Family | PL4 |
Protein Properties | Length: 651 Molecular Weight: 73715.4 Isoelectric Point: 6.4043 |
Chromosome | Chromosome/Scaffold: 11 Start: 509978 End: 513949 |
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 | 4 | 612 | 0 |
GNVRLINQGPYVMLDNDLVRLTILKPQGYLTGIKYGGMDNILDLQSNESNRGYWDMNWNLPGGKDRYQSVNGAEYSVIYNSNDKLEISFRSTYDPSNKGT KLPLSIDIRYILNSGVSGFHCYAIYERPAGSPAFDLVQTRMVFKLRRDKFHYMAISDEKQRVMPMPEDLLPGRGKQLIVPESVLLVNPINPDLKGEVDDK YQYSMDNKDGGVHGWIGSGPVIGFWVIFPSHEFRNGGPTKQNLTVHTGPTCLAMFHGTHYIGDDIVAQFQEGEAWRKVFGPFFVYLNSTSNVSDAYNLWI DAKKQRLLEEATWPYEFVSSPYYLNAKERGSATARLFVQERFVSESLIPAKNAYVGLSTARAQGAWQTESKDYQFWVQTDSNGNFTIKNVIPGVYGFHGW VPGFIGDFLDNALVTISEGSETQLGNLTYVPLRDGPTIWEIGFPDRTGIGFYVPDANPMYVNKLFVNSPEKFRQYGLWDRYTDVHPEYDQTFTIGISDPK KNWFFAHVDRRVADKYIPSTWTIKFLLNSIKNGIYKLRLAIASANRSDLQVYLNDMDKEHMVFQVMNLGAENAVCRHGIHGLYRLFSIDIPSSLLLNGDN SMFLVQARG |
Full Sequence |
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Protein Sequence Length: 651 Download |
MGKGNVRLIN QGPYVMLDND LVRLTILKPQ GYLTGIKYGG MDNILDLQSN ESNRGYWDMN 60 WNLPGGKDRY QSVNGAEYSV IYNSNDKLEI SFRSTYDPSN KGTKLPLSID IRYILNSGVS 120 GFHCYAIYER PAGSPAFDLV QTRMVFKLRR DKFHYMAISD EKQRVMPMPE DLLPGRGKQL 180 IVPESVLLVN PINPDLKGEV DDKYQYSMDN KDGGVHGWIG SGPVIGFWVI FPSHEFRNGG 240 PTKQNLTVHT GPTCLAMFHG THYIGDDIVA QFQEGEAWRK VFGPFFVYLN STSNVSDAYN 300 LWIDAKKQRL LEEATWPYEF VSSPYYLNAK ERGSATARLF VQERFVSESL IPAKNAYVGL 360 STARAQGAWQ TESKDYQFWV QTDSNGNFTI KNVIPGVYGF HGWVPGFIGD FLDNALVTIS 420 EGSETQLGNL TYVPLRDGPT IWEIGFPDRT GIGFYVPDAN PMYVNKLFVN SPEKFRQYGL 480 WDRYTDVHPE YDQTFTIGIS DPKKNWFFAH VDRRVADKYI PSTWTIKFLL NSIKNGIYKL 540 RLAIASANRS DLQVYLNDMD KEHMVFQVMN LGAENAVCRH GIHGLYRLFS IDIPSSLLLN 600 GDNSMFLVQA RGGDALCGIL YDYLRLEAPA SPANSKQREE LESFQFDSHV * 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 2.0e-25 | 331 | 430 | 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 | 2.0e-41 | 442 | 627 | 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. | ||
cd10320 | RGL4_N | 2.0e-69 | 6 | 298 | 299 | + 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 | 7.0e-70 | 11 | 200 | 190 | + 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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI23231.1 | 0 | 16 | 631 | 1 | 617 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001769727.1 | 0 | 15 | 635 | 4 | 626 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002285626.1 | 0 | 17 | 639 | 1 | 625 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002317123.1 | 0 | 1 | 650 | 1 | 650 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 6 | 636 | 6 | 640 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GE473226 | 288 | 186 | 473 | 0 |
DV995349 | 288 | 186 | 473 | 0 |
CO473731 | 278 | 186 | 463 | 0 |
GW864372 | 311 | 144 | 454 | 0 |
CO474992 | 282 | 236 | 517 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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