y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29596.m000702 |
Family | PL4 |
Protein Properties | Length: 642 Molecular Weight: 72969.3 Isoelectric Point: 4.8928 |
Chromosome | Chromosome/Scaffold: 29596 Start: 123708 End: 127835 |
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 | 619 | 0 |
VQLNIQDNHVMLDNGILQVTLSNPEGIVTGIQYNGIGNLLEVLNDESNRGYWDLVWSTPGSTGTTGIFDVIKGTSFKVIVETEEQVELSFTRSWDPSLEG KLIPLNIDKRFVMLRGSSGFYSYAIFEHLKEWPGFNLAEARIAFKLRKEKFHYMAVADNRQRYMPLPDDRLSPRGQALAYPEAVLLVNPVESEFKGELDD KYQYSCENKDIRVHGWICMDPSVGFWQITPSNEFRSGGPVKQNLTSHVGPTTLSVFLSAHYSGEDLVPKFVAGEAWKKVFGPVFMYLNSVLVGDDPLSLW EDAKEQTEIEVQSWPYFFPASEDYPKSEQRGSVSGRLLVKDRFVSDDYISANGAYVGLAPQGDVGSWQRECKDYQFWSKADENGYFSINSIRTGDYNLYA WVPGFIGDYRCDVAITITSGCDINMHDLVYEPPRDGPTLWEIGIPDRSAAEFYIPDPNPMYINKLYVNHPDRFRQYGLWDRYAELYPDGDLVYTVGVSDY RKDWFFAQVNRKKDDNTYQRTTWQIKFKLDNVDKNGIYKLRVAIASATVAELQVRINDPKANIIFSSGMIGKDNSIARHGIHGLYWLYNVDVPGVRLVQG GNTVFLTQPRSSSP |
Full Sequence |
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Protein Sequence Length: 642 Download |
MPLQGVQLNI QDNHVMLDNG ILQVTLSNPE GIVTGIQYNG IGNLLEVLND ESNRGYWDLV 60 WSTPGSTGTT GIFDVIKGTS FKVIVETEEQ VELSFTRSWD PSLEGKLIPL NIDKRFVMLR 120 GSSGFYSYAI FEHLKEWPGF NLAEARIAFK LRKEKFHYMA VADNRQRYMP LPDDRLSPRG 180 QALAYPEAVL LVNPVESEFK GELDDKYQYS CENKDIRVHG WICMDPSVGF WQITPSNEFR 240 SGGPVKQNLT SHVGPTTLSV FLSAHYSGED LVPKFVAGEA WKKVFGPVFM YLNSVLVGDD 300 PLSLWEDAKE QTEIEVQSWP YFFPASEDYP KSEQRGSVSG RLLVKDRFVS DDYISANGAY 360 VGLAPQGDVG SWQRECKDYQ FWSKADENGY FSINSIRTGD YNLYAWVPGF IGDYRCDVAI 420 TITSGCDINM HDLVYEPPRD GPTLWEIGIP DRSAAEFYIP DPNPMYINKL YVNHPDRFRQ 480 YGLWDRYAEL YPDGDLVYTV GVSDYRKDWF FAQVNRKKDD NTYQRTTWQI KFKLDNVDKN 540 GIYKLRVAIA SATVAELQVR INDPKANIIF SSGMIGKDNS IARHGIHGLY WLYNVDVPGV 600 RLVQGGNTVF LTQPRSSSPF QGIMYDYIRL EEPPASAPNK II 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 9.0e-33 | 334 | 433 | 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 | 5.0e-55 | 445 | 631 | 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 | 2.0e-75 | 11 | 304 | 297 | + 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-101 | 1 | 202 | 202 | + 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 | 5 | 639 | 5 | 650 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 17 | 639 | 1 | 621 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 17 | 631 | 1 | 612 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 642 | 1 | 642 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 1 | 636 | 1 | 637 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DW479599 | 295 | 1 | 295 | 0 |
DW479600 | 295 | 1 | 295 | 0 |
DT552229 | 293 | 17 | 308 | 0 |
DY293973 | 352 | 1 | 349 | 0 |
GW864372 | 311 | 147 | 457 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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