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Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa002538m |
Family | PL4 |
Protein Properties | Length: 661 Molecular Weight: 75340.9 Isoelectric Point: 4.8288 |
Chromosome | Chromosome/Scaffold: 1 Start: 45972970 End: 45978837 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 4 | 622 | 0 |
QRVQLDIQDHHVVMDNGILQVTLSKPDGIVTRIQYNGIDNLLEVLSEEVERGYWDLVWSEAGSVGTTGTFDVIKGTKFEVIVESDEQVEVSFTRKWNPSQ KGKLVPLNIDKRFIMLRNSSGFYSYAIYDHLKEWPPFNLPQTRIVFKLRKEKFQYMAIADNRQRYMPLPDDRLQERSKVLDVPEAVLLVNPIEPEFKGEV DDKYEYSSENQNLRVHGWICMDPPVGFWQITPSDEFRSGGPLKQNLTSHVGPFCLAMFLSAHYSGEDLVLKLKPDEPWKKVFGPVFIYLNSLTSNANEDP SPLWEDAKHQMMTEVQKWPYDFPASSEFPPSDQRGNVSGRIQVRDRYVSEDCIPGKGAYVGLAPPGDAGSFQRDCKGYQFWTRADEHGYYSIKNIREGQY NLYAWVPGFIGDYRYDAAINITAGCVIDVGELVYEPPRDGPTLWEIGIPDRSAAEFYVPDPNPNYINKLYVNHPDRFRQYGLWERYADLYPDQDLIYTIG TSDYAKDWFFAQVTRKKDDDTYEGTTWQIKFQLDNVNQSGTFKLQISLATANIAELQIRINDPKADPPLFTTGVIGKDNTILRHGIHGLYWLYSIDIPAT LLVEGNNTLFLTQPISNSP |
Full Sequence |
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Protein Sequence Length: 661 Download |
MSSQRVQLDI QDHHVVMDNG ILQVTLSKPD GIVTRIQYNG IDNLLEVLSE EVERGYWDLV 60 WSEAGSVGTT GTFDVIKGTK FEVIVESDEQ VEVSFTRKWN PSQKGKLVPL NIDKRFIMLR 120 NSSGFYSYAI YDHLKEWPPF NLPQTRIVFK LRKEKFQYMA IADNRQRYMP LPDDRLQERS 180 KVLDVPEAVL LVNPIEPEFK GEVDDKYEYS SENQNLRVHG WICMDPPVGF WQITPSDEFR 240 SGGPLKQNLT SHVGPFCLAM FLSAHYSGED LVLKLKPDEP WKKVFGPVFI YLNSLTSNAN 300 EDPSPLWEDA KHQMMTEVQK WPYDFPASSE FPPSDQRGNV SGRIQVRDRY VSEDCIPGKG 360 AYVGLAPPGD AGSFQRDCKG YQFWTRADEH GYYSIKNIRE GQYNLYAWVP GFIGDYRYDA 420 AINITAGCVI DVGELVYEPP RDGPTLWEIG IPDRSAAEFY VPDPNPNYIN KLYVNHPDRF 480 RQYGLWERYA DLYPDQDLIY TIGTSDYAKD WFFAQVTRKK DDDTYEGTTW QIKFQLDNVN 540 QSGTFKLQIS LATANIAELQ IRINDPKADP PLFTTGVIGK DNTILRHGIH GLYWLYSIDI 600 PATLLVEGNN TLFLTQPISN SPLAAFHGLM YDYIRLEGPP SSTSTRGVKP ANMAPNTPLD 660 * 720 |
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-33 | 336 | 435 | 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-53 | 447 | 637 | 193 | + 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-71 | 14 | 294 | 284 | + 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-95 | 1 | 203 | 203 | + 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 | 651 | 1 | 656 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 17 | 651 | 1 | 627 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301114.1 | 0 | 1 | 644 | 1 | 636 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 646 | 1 | 640 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 1 | 644 | 1 | 639 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY293973 | 350 | 1 | 349 | 0 |
DW479599 | 295 | 1 | 295 | 0 |
DW479600 | 296 | 1 | 296 | 0 |
DT552229 | 294 | 17 | 310 | 0 |
FC896579 | 284 | 69 | 351 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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