Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.002G110000.1 |
Family | PL4 |
Protein Properties | Length: 643 Molecular Weight: 73150.1 Isoelectric Point: 4.8612 |
Chromosome | Chromosome/Scaffold: 02 Start: 8107788 End: 8112051 |
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 | 6 | 614 | 0 |
VQLLVQDRHVVMDNGILQVTLSNPDGIVTGIRYSGIDNLLEVQNDESNRGYWDLVWNTAGTTGIFDVIKGRSFKVIVETEEQVEVSFTRTWDSSQEGKLV PLNIDKRFVMLRGSSGFYSYAIYEHLKEWPGFNLGETRIAFKLRKDKFHYMIAADNRQRYMPLPDDRLPPRGQPLAYPEAVQLVNPVEPDFKGEVDDKYQ YSIENKDNKVHGWICMDPAVGFWQITPSDEFRSGGPVKQNLTSHVGPTTLVMFLSAHYSGEDLVPKIGAGEAWKKVFGPVFMYFNSVMDGDDPLSLWEDA KLQMLIEVQSWPYGFPASEDYQKSDQRGNVSGRLLVRDRFVSDDYTPANGAYVGLALPGDVGSWQRECKDYQFWNRADEGGYFSINNVRTGDYNLYAWVP GVIGDYRYDVSITITSGCDIEMGDLVYEPPRDGPTLWEIGIPDRSAEEFYVPDPNPKYINKLYVNHPDRFRQYGLWERYAELYPDGDLVYTVGVSDYRKD WFYAQVTRKKDDNTYQRTTWQIKFNLDKVDHNGIYKLRVALASATVSELQVRINDPKAKPLFSSGLIGKDNSIARHGIHGLYWLYGIDVPGARLVEGDNA VFLTQPRSI |
Full Sequence |
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Protein Sequence Length: 643 Download |
MPHLGVQLLV QDRHVVMDNG ILQVTLSNPD GIVTGIRYSG IDNLLEVQND ESNRGYWDLV 60 WNTAGTTGIF DVIKGRSFKV IVETEEQVEV SFTRTWDSSQ EGKLVPLNID KRFVMLRGSS 120 GFYSYAIYEH LKEWPGFNLG ETRIAFKLRK DKFHYMIAAD NRQRYMPLPD DRLPPRGQPL 180 AYPEAVQLVN PVEPDFKGEV DDKYQYSIEN KDNKVHGWIC MDPAVGFWQI TPSDEFRSGG 240 PVKQNLTSHV GPTTLVMFLS AHYSGEDLVP KIGAGEAWKK VFGPVFMYFN SVMDGDDPLS 300 LWEDAKLQML IEVQSWPYGF PASEDYQKSD QRGNVSGRLL VRDRFVSDDY TPANGAYVGL 360 ALPGDVGSWQ RECKDYQFWN RADEGGYFSI NNVRTGDYNL YAWVPGVIGD YRYDVSITIT 420 SGCDIEMGDL VYEPPRDGPT LWEIGIPDRS AEEFYVPDPN PKYINKLYVN HPDRFRQYGL 480 WERYAELYPD GDLVYTVGVS DYRKDWFYAQ VTRKKDDNTY QRTTWQIKFN LDKVDHNGIY 540 KLRVALASAT VSELQVRIND PKAKPLFSSG LIGKDNSIAR HGIHGLYWLY GIDVPGARLV 600 EGDNAVFLTQ PRSISPFQGI MYDYIRLEGP PSSSSNSPET SF* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 1.0e-31 | 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 | 3.0e-55 | 442 | 628 | 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 | 4.0e-78 | 10 | 301 | 298 | + 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 | 4.0e-104 | 10 | 200 | 191 | + 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 | CBI19298.1 | 0 | 1 | 637 | 1 | 651 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 17 | 637 | 1 | 622 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 17 | 642 | 1 | 626 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002306520.1 | 0 | 17 | 631 | 1 | 616 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 636 | 1 | 639 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DW479599 | 295 | 1 | 292 | 0 |
DW479600 | 298 | 1 | 295 | 0 |
DT552229 | 293 | 17 | 305 | 0 |
DY293973 | 347 | 6 | 346 | 0 |
GW864372 | 311 | 144 | 454 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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