Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 334271 |
Family | PL4 |
Protein Properties | Length: 634 Molecular Weight: 72500.4 Isoelectric Point: 5.1575 |
Chromosome | Chromosome/Scaffold: 1 Start: 3768986 End: 3772718 |
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 | 5 | 618 | 0 |
KLQLHDKGNHVVLDNGIARVTLSKPDGIVTGIEYNGIDNLLEVLNEEVNRGYWDLVWGGSGTAGGFDVIKGTNFEVIMKNEEQIELSFTRKWDPSQEGKA VPLNIDKRFVMLRGSSGFYTYAIYEHLKEWPAFSLAETRIAFKLRKEKFHYMAVTDDRQRFMPLPDDRLPDRGQALAYPEAVLLVNPVEPQFKGEVDDKY QYSCENKDITVHGWICTEQPSVGFWLITPSHEYRTGGPQKQNLTSHVGPTALAVFVSAHYTGEDLVPKFSEGEAWKKVFGPVFVYLNSSTDDDNDPLWLW QDAKSQMNVEAESWPYSFPASDDYVKAEQRGNVVGRLLVQDRYVDKDFIAANRGYVGLAVPGAAGSWQRECKEYQFWTRTDEEGFFYISGIRPGQYNLYA WIPGFLGDYKYDDIITITSGCYIYVEDLVYQPPRNGATLWEIGFPDRSAADFYVPDPNPKYINKLYQNHPDRFRQYGLWERYAELYPDKDLVYVVGSSDY RKDWFYAQVTRKKDSKTYQGTTWQIKFELKNIDKNHSYTLRVAIASATFSELQIRVNDANASPLFTSGLIGRDNSIARHGIHGLYWLFNVEVAGSKLVEG ENTLFLTQPRSTSP |
Full Sequence |
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Protein Sequence Length: 634 Download |
MSSVKLQLHD KGNHVVLDNG IARVTLSKPD GIVTGIEYNG IDNLLEVLNE EVNRGYWDLV 60 WGGSGTAGGF DVIKGTNFEV IMKNEEQIEL SFTRKWDPSQ EGKAVPLNID KRFVMLRGSS 120 GFYTYAIYEH LKEWPAFSLA ETRIAFKLRK EKFHYMAVTD DRQRFMPLPD DRLPDRGQAL 180 AYPEAVLLVN PVEPQFKGEV DDKYQYSCEN KDITVHGWIC TEQPSVGFWL ITPSHEYRTG 240 GPQKQNLTSH VGPTALAVFV SAHYTGEDLV PKFSEGEAWK KVFGPVFVYL NSSTDDDNDP 300 LWLWQDAKSQ MNVEAESWPY SFPASDDYVK AEQRGNVVGR LLVQDRYVDK DFIAANRGYV 360 GLAVPGAAGS WQRECKEYQF WTRTDEEGFF YISGIRPGQY NLYAWIPGFL GDYKYDDIIT 420 ITSGCYIYVE DLVYQPPRNG ATLWEIGFPD RSAADFYVPD PNPKYINKLY QNHPDRFRQY 480 GLWERYAELY PDKDLVYVVG SSDYRKDWFY AQVTRKKDSK TYQGTTWQIK FELKNIDKNH 540 SYTLRVAIAS ATFSELQIRV NDANASPLFT SGLIGRDNSI ARHGIHGLYW LFNVEVAGSK 600 LVEGENTLFL TQPRSTSPFQ GIMYDYIRFE APS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.006 | 357 | 409 | 57 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 3.0e-29 | 333 | 432 | 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-55 | 444 | 630 | 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 | 3.0e-74 | 8 | 299 | 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 | 8.0e-107 | 1 | 200 | 200 | + 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 | 632 | 1 | 644 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_172460.6 | 0 | 17 | 633 | 1 | 617 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002285626.1 | 0 | 17 | 632 | 1 | 615 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 17 | 631 | 1 | 613 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 6 | 632 | 6 | 633 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DK498554 | 264 | 1 | 260 | 0 |
FD943935 | 247 | 388 | 634 | 0 |
DT552229 | 294 | 17 | 307 | 0 |
DW479599 | 292 | 4 | 292 | 0 |
DW479600 | 295 | 4 | 295 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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