Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_005_00010.1 |
Family | PL4 |
Protein Properties | Length: 647 Molecular Weight: 72808 Isoelectric Point: 8.4723 |
Chromosome | Chromosome/Scaffold: 5 Start: 143207 End: 147206 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 4 | 611 | 0 |
KVILITQPSYVTLDNGLVKLTISKPAGSLTGISYGGLDNLLDLKSSQSTRGYWDINWNLPGGQDRYLLLKGMDYSVVNSSKNCVELSFRSNWNSSARGTT LPLSIDRRYIMRSGVSGFYCYAIYERSTGLPAFDLVQTRMVFILRRDLFHYMAITDHKQRIMPMPEDRLPNRCKQLIVPEAVLLTNPINPDLKGQVDDKY QYSMDNKDGGVHGWISSGPVIGFWIIHPSNESRNGGPTKQNLTCHTGPACLAMFHGTHYIGNDIVAHFIQGEAWRKVFGPFFVYLNTTPNPSDAHSLWID AKKQRLLEVTAWPYNFVSSPYFLSTKERGSTSGRLFVQDKSVSGALIPAKNVYVGLSIATTEGGWEVESKGYQFWVQTDSDGSFIINNVIPGVYGLHGWV PGFIGNFLNKTLVTISAGSETELGNLIYIPPRSGPTMWEIGYPDRSAIGFYVPDVNSMYINPLYINSPEKYRQYGLWDRYTDMHPKSDQVFTIGVNDSKK DWFFAHVDRRTPEKYVPTTWQVNFNLNSVTSGTYKLRIAMASAIRCNLQVHMNSLDEGHLVFQVLNLGMDNIICRHGIHGLYRLFSIDITSTLLIKGDNI MFLTNARG |
Full Sequence |
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Protein Sequence Length: 647 Download |
MAKKVILITQ PSYVTLDNGL VKLTISKPAG SLTGISYGGL DNLLDLKSSQ STRGYWDINW 60 NLPGGQDRYL LLKGMDYSVV NSSKNCVELS FRSNWNSSAR GTTLPLSIDR RYIMRSGVSG 120 FYCYAIYERS TGLPAFDLVQ TRMVFILRRD LFHYMAITDH KQRIMPMPED RLPNRCKQLI 180 VPEAVLLTNP INPDLKGQVD DKYQYSMDNK DGGVHGWISS GPVIGFWIIH PSNESRNGGP 240 TKQNLTCHTG PACLAMFHGT HYIGNDIVAH FIQGEAWRKV FGPFFVYLNT TPNPSDAHSL 300 WIDAKKQRLL EVTAWPYNFV SSPYFLSTKE RGSTSGRLFV QDKSVSGALI PAKNVYVGLS 360 IATTEGGWEV ESKGYQFWVQ TDSDGSFIIN NVIPGVYGLH GWVPGFIGNF LNKTLVTISA 420 GSETELGNLI YIPPRSGPTM WEIGYPDRSA IGFYVPDVNS MYINPLYINS PEKYRQYGLW 480 DRYTDMHPKS DQVFTIGVND SKKDWFFAHV DRRTPEKYVP TTWQVNFNLN SVTSGTYKLR 540 IAMASAIRCN LQVHMNSLDE GHLVFQVLNL GMDNIICRHG IHGLYRLFSI DITSTLLIKG 600 DNIMFLTNAR GGDPMCGIVY DYIRLESPAT FRLEAPTSSE WPPERR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.001 | 335 | 426 | 95 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 6.0e-28 | 330 | 429 | 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 | 4.0e-41 | 441 | 626 | 190 | + 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 | 8.0e-65 | 7 | 297 | 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-72 | 9 | 199 | 191 | + 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 | 630 | 2 | 617 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001769727.1 | 0 | 14 | 628 | 4 | 620 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002317123.1 | 0 | 5 | 630 | 6 | 631 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527356.1 | 0 | 14 | 628 | 128 | 746 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527356.1 | 1e-29 | 72 | 199 | 1 | 128 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DT769642 | 195 | 453 | 647 | 0 |
GW864372 | 311 | 143 | 453 | 0 |
GE473226 | 288 | 185 | 472 | 0 |
DV995349 | 288 | 185 | 472 | 0 |
DT769642 | 44 | 412 | 455 | 1e-17 |
Sequence Alignments (This image is cropped. Click for full image.) |
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