y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.010G032900.1 |
Family | PL4 |
Protein Properties | Length: 650 Molecular Weight: 73681.8 Isoelectric Point: 4.8631 |
Chromosome | Chromosome/Scaffold: 10 Start: 2951474 End: 2958584 |
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 | 6 | 621 | 0 |
VQLHTQDTHVMIDNGLLQLTLLNPDGIVTGIRYNGIDNLLEVLNGEDNRGYWDLVWNSPGTPGTTGSFDVIKGTSFKVIVENEDQVEVSFTRTWDSSQEG KLVPLNIDKRFIVLRGCSGFYTYAIYEHLKDWPGFNLAETRIAFKLRKDKFHYMAMADNRQRYMPLPDDRLSGRGQALAYPEAVLLVNPVEPDFKGEVDD KYQYSCDNKDSQVHGWICTTDQPAVGFWMVTPSNEFRSGGPVKQNLTSHVGPTTLAVFLSAHYTGEDLVPKFSAGEAWKKVFGPVFIYLNCTMDGDEPLS LWEDAKQQMIIEVQSWPYTFPASDDFPKSNQRGNVNGRLLVNDRYASDDNIPANGAYIGLVPPGNVGSWQRECKDYQFWTKTDINGYFLINDIRPGDYNL YAWVPGFIGDYQYSAAITITPGSEIEVGDLVYKPPRNGPTLWEIGIPDRSAAEFYVPDPNPKYINKVYVNHPDRFRQYGLWERYAELYPNEDLVYTVGTS DYKKDWFFAQVTRKIDTNKYQGTTWQIRFKLDNVDQGSSYKLRVAIASATFSELQVQINDPKTNPLFSSGLIGRDNSIARHGIHGLYWLYNVDVPGKLLV QGDNTIFLTQPRSSSP |
Full Sequence |
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Protein Sequence Length: 650 Download |
MPFIGVQLHT QDTHVMIDNG LLQLTLLNPD GIVTGIRYNG IDNLLEVLNG EDNRGYWDLV 60 WNSPGTPGTT GSFDVIKGTS FKVIVENEDQ VEVSFTRTWD SSQEGKLVPL NIDKRFIVLR 120 GCSGFYTYAI YEHLKDWPGF NLAETRIAFK LRKDKFHYMA MADNRQRYMP LPDDRLSGRG 180 QALAYPEAVL LVNPVEPDFK GEVDDKYQYS CDNKDSQVHG WICTTDQPAV GFWMVTPSNE 240 FRSGGPVKQN LTSHVGPTTL AVFLSAHYTG EDLVPKFSAG EAWKKVFGPV FIYLNCTMDG 300 DEPLSLWEDA KQQMIIEVQS WPYTFPASDD FPKSNQRGNV NGRLLVNDRY ASDDNIPANG 360 AYIGLVPPGN VGSWQRECKD YQFWTKTDIN GYFLINDIRP GDYNLYAWVP GFIGDYQYSA 420 AITITPGSEI EVGDLVYKPP RNGPTLWEIG IPDRSAAEFY VPDPNPKYIN KVYVNHPDRF 480 RQYGLWERYA ELYPNEDLVY TVGTSDYKKD WFFAQVTRKI DTNKYQGTTW QIRFKLDNVD 540 QGSSYKLRVA IASATFSELQ VQINDPKTNP LFSSGLIGRD NSIARHGIHG LYWLYNVDVP 600 GKLLVQGDNT IFLTQPRSSS PFQGIMYDYI RLEGPSKLSS NEEYMSSTL* 660 |
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 | 385 | 432 | 48 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 4.0e-30 | 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 | 1.0e-56 | 447 | 633 | 189 | + 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 | 1.0e-74 | 8 | 306 | 302 | + 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-102 | 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 | 641 | 1 | 650 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_172460.6 | 0 | 17 | 636 | 1 | 617 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002285626.1 | 0 | 17 | 641 | 1 | 621 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 17 | 634 | 1 | 613 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 642 | 1 | 640 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DW479599 | 296 | 1 | 296 | 0 |
DW479600 | 300 | 1 | 300 | 0 |
DT552229 | 295 | 17 | 310 | 0 |
DY293973 | 349 | 6 | 351 | 0 |
GW864372 | 313 | 147 | 459 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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