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Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa014556m |
Family | PL4 |
Protein Properties | Length: 644 Molecular Weight: 72520.2 Isoelectric Point: 6.8361 |
Chromosome | Chromosome/Scaffold: 4 Start: 870079 End: 873945 |
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 | 614 | 0 |
KKKLKLRNQDPYVILDNGLVKLTILRPQGYLTGISYGGMDNLLDIKSNESSRGYWDINWNLPGGQDIYTLLKGAEYSVVHESNDSLEISFKNTYNPSSAQ GVKLPLSVDIRYILRTGVSGFYSYAIYDRPSGCPAFDLAQTRMVYKLRREKFHYMAITDEKQRIMPMPEDLLPGRGKQLIVPESVLLVNPINPDLKGEVD DKYQYSMDNKDGGVHGWISSGPIIGFWVIFPSQEFRNGGPTKQNLTVHTGPTCLAMLHGTHYIGEDILAHFEEGETWTKVFGPFFVYLNSTPDVSKAHNL WIDAKKQRLFEETAWPYDFVSSPYYVAAKERGLVSGRLFVQDRYVSGSLIPAKYAYVGLSVATTEGSWQTESKGYQFWVETDYTGNFTIKNVIPGVYGLH GWIPGFLGDYLGKEHITISAGSQTQLGNLTYVPPRDGPTLWEIGFPDRTAIGYYVPDVNPMYVNKLFLNSPEKFRQYGLWDRYTDVHPQFDQTFIIGSSN PKNDWFFAHVDRRGADNKYLPTTWTIKFNLNSVTTGTYKLRLAIASATRSDLKAHVNDMDIEHLVFQVLNLGTDNTVCRHGIHGLYRLFSCDISSSFLVK GDNSIFLTQARG |
Full Sequence |
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Protein Sequence Length: 644 Download |
MAKKKLKLRN QDPYVILDNG LVKLTILRPQ GYLTGISYGG MDNLLDIKSN ESSRGYWDIN 60 WNLPGGQDIY TLLKGAEYSV VHESNDSLEI SFKNTYNPSS AQGVKLPLSV DIRYILRTGV 120 SGFYSYAIYD RPSGCPAFDL AQTRMVYKLR REKFHYMAIT DEKQRIMPMP EDLLPGRGKQ 180 LIVPESVLLV NPINPDLKGE VDDKYQYSMD NKDGGVHGWI SSGPIIGFWV IFPSQEFRNG 240 GPTKQNLTVH TGPTCLAMLH GTHYIGEDIL AHFEEGETWT KVFGPFFVYL NSTPDVSKAH 300 NLWIDAKKQR LFEETAWPYD FVSSPYYVAA KERGLVSGRL FVQDRYVSGS LIPAKYAYVG 360 LSVATTEGSW QTESKGYQFW VETDYTGNFT IKNVIPGVYG LHGWIPGFLG DYLGKEHITI 420 SAGSQTQLGN LTYVPPRDGP TLWEIGFPDR TAIGYYVPDV NPMYVNKLFL NSPEKFRQYG 480 LWDRYTDVHP QFDQTFIIGS SNPKNDWFFA HVDRRGADNK YLPTTWTIKF NLNSVTTGTY 540 KLRLAIASAT RSDLKAHVND MDIEHLVFQV LNLGTDNTVC RHGIHGLYRL FSCDISSSFL 600 VKGDNSIFLT QARGGDALCG VLYDYVRLEA PATAERSELS TLA* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 2.0e-28 | 332 | 431 | 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-43 | 443 | 629 | 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-64 | 6 | 299 | 300 | + 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 | 9.0e-71 | 1 | 201 | 201 | + 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 | CBI23231.1 | 0 | 16 | 634 | 1 | 618 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001763359.1 | 0 | 15 | 634 | 1 | 623 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769727.1 | 0 | 15 | 641 | 4 | 630 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002285626.1 | 0 | 17 | 643 | 1 | 627 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002317123.1 | 0 | 1 | 642 | 1 | 644 | predicted protein [Populus trichocarpa] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GE473226 | 288 | 187 | 474 | 0 |
GW864372 | 311 | 145 | 455 | 0 |
DV995349 | 288 | 187 | 474 | 0 |
CO473731 | 278 | 187 | 464 | 0 |
DY969340 | 318 | 234 | 549 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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