Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10007058m |
Family | PL4 |
Protein Properties | Length: 632 Molecular Weight: 72449.2 Isoelectric Point: 6.5135 |
Chromosome | Chromosome/Scaffold: 5 Start: 12365324 End: 12369126 |
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 | 12 | 613 | 0 |
DRYVVMDNGILQVTLSKPGGIITGIKYNAIDNVLEVRNKETNRGYWDLHWNEVGGKGIFDVISGVTFRVIVETEEHVEISFLRTWDPSLEGKYIPLNIDK RFIMLRGSSGVYTYGIYEHLKEWPGFELGETRIAFKLRKDKFHYMAMADDRKRIMPFPDDLCKGRCQTLDYQEASLLTAPCDPHLQGEVDDKYQYSCENK DLRVHGWISFDPPVGFWQITPSNEFRSGGPLKQNLTSHVGPTTLAVFHSTHYAGKTMMPRFECGEPWKKVFGPVFIYLNSTANRDDSLCLWDDAKIKMKA EVESWPYSFVASEDYPKSEERGWAHGRLLIHDRFISNDLISARGAYVGLAPPGDAGSWQIECKGYQFWAIADEAGYFSIENVRPGEYNLYAWVPGFIGDY RNDTIVTVTSGCKIEMGDIVYEPPRDGPTLWEIGIPDRKASEFFIPDPDPMLVNRALVHHQDRFRQYGLWKRYTDLYPNDDLVYTIGVSDYRRDWFFAHV PRKKGDVHEGTTWQIRFKLENTDQKANYKLRVAIASATLAELQVRVNDAEAIRPLFTTGLIGRDNSIARHGIHGVYMLYTVNIPGNRFVQGDNTIFLKQP RC |
Full Sequence |
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Protein Sequence Length: 632 Download |
MPPQGVRLYI HDRYVVMDNG ILQVTLSKPG GIITGIKYNA IDNVLEVRNK ETNRGYWDLH 60 WNEVGGKGIF DVISGVTFRV IVETEEHVEI SFLRTWDPSL EGKYIPLNID KRFIMLRGSS 120 GVYTYGIYEH LKEWPGFELG ETRIAFKLRK DKFHYMAMAD DRKRIMPFPD DLCKGRCQTL 180 DYQEASLLTA PCDPHLQGEV DDKYQYSCEN KDLRVHGWIS FDPPVGFWQI TPSNEFRSGG 240 PLKQNLTSHV GPTTLAVFHS THYAGKTMMP RFECGEPWKK VFGPVFIYLN STANRDDSLC 300 LWDDAKIKMK AEVESWPYSF VASEDYPKSE ERGWAHGRLL IHDRFISNDL ISARGAYVGL 360 APPGDAGSWQ IECKGYQFWA IADEAGYFSI ENVRPGEYNL YAWVPGFIGD YRNDTIVTVT 420 SGCKIEMGDI VYEPPRDGPT LWEIGIPDRK ASEFFIPDPD PMLVNRALVH HQDRFRQYGL 480 WKRYTDLYPN DDLVYTIGVS DYRRDWFFAH VPRKKGDVHE GTTWQIRFKL ENTDQKANYK 540 LRVAIASATL AELQVRVNDA EAIRPLFTTG LIGRDNSIAR HGIHGVYMLY TVNIPGNRFV 600 QGDNTIFLKQ PRCNGPFQGI MYDYIRLEGT P* |
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 | 380 | 422 | 43 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 4.0e-30 | 331 | 430 | 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 | 5.0e-51 | 442 | 628 | 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 | 7.0e-82 | 11 | 292 | 288 | + 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 | 3.0e-101 | 1 | 200 | 200 | + 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 |
GenBank | AAB60743.1 | 0 | 1 | 631 | 1 | 727 | F21M12.30 gene product [Arabidopsis thaliana] |
RefSeq | NP_172462.2 | 0 | 1 | 631 | 44 | 674 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002306520.1 | 0 | 17 | 631 | 1 | 616 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 1 | 629 | 1 | 630 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527353.1 | 0 | 1 | 631 | 1 | 634 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DK517187 | 242 | 391 | 632 | 0 |
HO206588 | 225 | 121 | 345 | 0 |
EG452795 | 225 | 407 | 631 | 0 |
CN826718 | 235 | 227 | 457 | 0 |
CN826718 | 21 | 447 | 467 | 4.4 |
Sequence Alignments (This image is cropped. Click for full image.) |
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