Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_008_00160.4 |
Family | PL4 |
Protein Properties | Length: 548 Molecular Weight: 63070 Isoelectric Point: 4.3163 |
Chromosome | Chromosome/Scaffold: 8 Start: 4302795 End: 4308465 |
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 | 5 | 541 | 0 |
ASDVELQVQDDYVVIDNGLVQVTLSNPGGSVTRIQYNNVDNLLETHNEEENRGYWDLDWSKPEQLHDGIHDRISGTNFTVIMEDPDQVELSFVRYWDLSF GSKSVPLNIDVRFVMLHGIPGLYSYAIYEHLEGWPDFDLDQTRIVFKPSKDKFHYMAISDDRQRTMPMPEDRDTGQPLAYKEAVLLTNPINLDLKGEVDD KYQYSCENKDCKVHGWISNDSFTGFWTITPSNEFQSDGPFKQDLTSHVGPTTLAMFHSLHYSGEDVVLKFRDGEHWKKVFGPVFFYFNAVVDEDLENPYS TLWEDAKNQMMYEVQSWPYQFPNSEDYPHLEQRGTVTGRLFVQDRYISDDYISADSAYVGMALPGDAGSWQREGKGYQFWTKADASGCFSINNVREGNYS LYAYVPSFIGDYKYDVNITITPGCVIDVGDIVYEPPRNGPTFWEIGIADRSSAEFYIPDPSPNYINKLYLNQPNSVGMPSKSVHKFRQYGLWDRYTELYP DGDLLFVIDVSDYSNDWFYAHVTRFSSTDLYFTFTLQ |
Full Sequence |
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Protein Sequence Length: 548 Download |
MDKIASDVEL QVQDDYVVID NGLVQVTLSN PGGSVTRIQY NNVDNLLETH NEEENRGYWD 60 LDWSKPEQLH DGIHDRISGT NFTVIMEDPD QVELSFVRYW DLSFGSKSVP LNIDVRFVML 120 HGIPGLYSYA IYEHLEGWPD FDLDQTRIVF KPSKDKFHYM AISDDRQRTM PMPEDRDTGQ 180 PLAYKEAVLL TNPINLDLKG EVDDKYQYSC ENKDCKVHGW ISNDSFTGFW TITPSNEFQS 240 DGPFKQDLTS HVGPTTLAMF HSLHYSGEDV VLKFRDGEHW KKVFGPVFFY FNAVVDEDLE 300 NPYSTLWEDA KNQMMYEVQS WPYQFPNSED YPHLEQRGTV TGRLFVQDRY ISDDYISADS 360 AYVGMALPGD AGSWQREGKG YQFWTKADAS GCFSINNVRE GNYSLYAYVP SFIGDYKYDV 420 NITITPGCVI DVGDIVYEPP RNGPTFWEIG IADRSSAEFY IPDPSPNYIN KLYLNQPNSV 480 GMPSKSVHKF RQYGLWDRYT ELYPDGDLLF VIDVSDYSND WFYAHVTRFS STDLYFTFTL 540 QVASLKI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam09284 | RhgB_N | 0.003 | 214 | 291 | 78 | + Rhamnogalacturonase B, N-terminal. Members of this family are found in prokaryotic Rhamnogalacturonase B, and adopt a structure consisting of a beta supersandwich, with eighteen strands in two beta-sheets. The exact function of the domain is unknown, but a putative role includes carbohydrate-binding. | ||
cd10317 | RGL4_C | 5.0e-12 | 447 | 543 | 105 | + 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. | ||
cd10316 | RGL4_M | 2.0e-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. | ||
cd10320 | RGL4_N | 4.0e-72 | 10 | 292 | 287 | + 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-87 | 3 | 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 | 8 | 542 | 6 | 540 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 19 | 542 | 1 | 511 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 19 | 542 | 1 | 511 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 8 | 542 | 6 | 527 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527353.1 | 0 | 8 | 542 | 6 | 530 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GW864372 | 314 | 148 | 459 | 0 |
DY293973 | 348 | 5 | 349 | 0 |
JG640880 | 273 | 156 | 428 | 0 |
DW479599 | 293 | 5 | 294 | 0 |
DW479600 | 292 | 8 | 296 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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