Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000221905 |
Family | PL4 |
Protein Properties | Length: 631 Molecular Weight: 71364.4 Isoelectric Point: 7.3125 |
Chromosome | Chromosome/Scaffold: 02259770 Start: 16557 End: 20123 |
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 | 3 | 609 | 0 |
KMKLKLRNQGPYVVMDSGVVKLTILKPQGYLTGISYGGMDNLLDVKSNETSRGLKGAEYSVVHHSNDSLEVSFKNTFIPSSANGVKLPLSVDIRYIVKTG VSGFYNYAIYERXSGCPAFDLAQTRMAFKLRREKFHYMAITDEKQRIMPMPEDVLPPRGKQLIVPESVLLXDPINPDLKGEVDDKYQYSMDNKDSGVHGW ISSGPTVGFWLIFPSQEFRNGGPTKQNLTQMLHGTHYIGEDILAHFEEGETWTKVFGPFFVYLNSTPDVSKAHDLWIDAKKQRLIEETLWPYAFVQSPYY VAAKERGSVSGRLFVQDRYVSDSLIPAKYAYVGLSVATTPGSWQTESKDYQFWIQTDIIGNFTIKNVIPGVYXLHGWIPGFVGDYLDNERITISADLSIQ XAKHXKLKTWPIFHSGSQTQLGNLTYVPLRDGPTLWEIGYPDRTAIDYYVPDVNPIYVNKLFLNSPEKYRQYGLWDRYTDVHPEFDQTFTIGSSNPKTDW FFAHVDRRGADNKYLPTTWTIKFNLKSVTTGTXKFRLAIASATRSDLKVHVNAMDIEHLVIQVLNLGTDNAVCRHGVHGLYRLFSGDIPSTLLVKGDNSI FLSQARG |
Full Sequence |
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Protein Sequence Length: 631 Download |
MAKMKLKLRN QGPYVVMDSG VVKLTILKPQ GYLTGISYGG MDNLLDVKSN ETSRGLKGAE 60 YSVVHHSNDS LEVSFKNTFI PSSANGVKLP LSVDIRYIVK TGVSGFYNYA IYERXSGCPA 120 FDLAQTRMAF KLRREKFHYM AITDEKQRIM PMPEDVLPPR GKQLIVPESV LLXDPINPDL 180 KGEVDDKYQY SMDNKDSGVH GWISSGPTVG FWLIFPSQEF RNGGPTKQNL TQMLHGTHYI 240 GEDILAHFEE GETWTKVFGP FFVYLNSTPD VSKAHDLWID AKKQRLIEET LWPYAFVQSP 300 YYVAAKERGS VSGRLFVQDR YVSDSLIPAK YAYVGLSVAT TPGSWQTESK DYQFWIQTDI 360 IGNFTIKNVI PGVYXLHGWI PGFVGDYLDN ERITISADLS IQXAKHXKLK TWPIFHSGSQ 420 TQLGNLTYVP LRDGPTLWEI GYPDRTAIDY YVPDVNPIYV NKLFLNSPEK YRQYGLWDRY 480 TDVHPEFDQT FTIGSSNPKT DWFFAHVDRR GADNKYLPTT WTIKFNLKSV TTGTXKFRLA 540 IASATRSDLK VHVNAMDIEH LVIQVLNLGT DNAVCRHGVH GLYRLFSGDI PSTLLVKGDN 600 SIFLSQARGG DALCGLFYDY LRLEAPETAX S |
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-23 | 307 | 402 | 96 | + 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-39 | 438 | 624 | 191 | + 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-49 | 6 | 274 | 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 | 1.0e-56 | 8 | 184 | 194 | + 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 |
DDBJ | BAD10227.1 | 0 | 14 | 626 | 24 | 642 | putative MYST1 [Oryza sativa Japonica Group] |
EMBL | CBI23231.1 | 0 | 16 | 629 | 1 | 618 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001062464.1 | 0 | 14 | 626 | 37 | 655 | Os08g0554100 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002317123.1 | 0 | 1 | 628 | 1 | 631 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002445711.1 | 0 | 14 | 626 | 41 | 660 | hypothetical protein SORBIDRAFT_07g024560 [Sorghum bicolor] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FC327604 | 260 | 135 | 386 | 0 |
GE473226 | 308 | 170 | 469 | 0 |
GW864372 | 331 | 128 | 450 | 0 |
DY969340 | 338 | 217 | 544 | 0 |
DV995349 | 308 | 170 | 469 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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