Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g006927m |
Family | PL4 |
Protein Properties | Length: 626 Molecular Weight: 71032.2 Isoelectric Point: 4.4409 |
Chromosome | Chromosome/Scaffold: 00004 Start: 2556982 End: 2561276 |
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 | 3 | 599 | 0 |
DSSVQLQIQDHHVVMDNGLLQVTISKPDGHVTRIQGYGIDNMLEVRNKETNRGYWDLVWSETGSTGTTGTDELIKGSDFRVIVENEEQVEISFTRMWDIS LQDKLAPLNIDKRYIMLGNTSGFYSYAIYEHMGEWPAFNLPQTRMVFKLRKDKCKELAFPEAVLLVNPIEPEFNGEVDDKYQYSCENRNLKVHGWICSDP AVGFWQITPSNEFRSGGPLKQNLTSHVGPITLAMFLSAHYGGEDLVLKLKQDEPWKKVLGPVFFYINSFLDSDSDDPKAWLWEDAKQQTLNESESWPYSF PASEDFPKWNQRGNISGRLQVQDRYVSDDYITVDGAYVGLAPSGDAGSWQTECKGYQFWTTTDADGFFSISDILVGDYNLYAFVPGFIGDYRNDVVLTIT EDSDIDMGDLVFEPIRDGPTLWEIGIPSRSAAEFYIPDPDPTYVNKLYVNHPDRFRQYGLWERYSDLYPEGDLVYTVGVSDYKNDWFYAQVPRKKDDNSY EATTWQIKFKLDSVDQNATYKLRIALATANVAELQVRVNDEKAEPPLFATGQIGHDNAIARHGIHGLYRLYSMDVPAANLAAGENTIFLKQATSSSA |
Full Sequence |
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Protein Sequence Length: 626 Download |
MSDSSVQLQI QDHHVVMDNG LLQVTISKPD GHVTRIQGYG IDNMLEVRNK ETNRGYWDLV 60 WSETGSTGTT GTDELIKGSD FRVIVENEEQ VEISFTRMWD ISLQDKLAPL NIDKRYIMLG 120 NTSGFYSYAI YEHMGEWPAF NLPQTRMVFK LRKDKCKELA FPEAVLLVNP IEPEFNGEVD 180 DKYQYSCENR NLKVHGWICS DPAVGFWQIT PSNEFRSGGP LKQNLTSHVG PITLAMFLSA 240 HYGGEDLVLK LKQDEPWKKV LGPVFFYINS FLDSDSDDPK AWLWEDAKQQ TLNESESWPY 300 SFPASEDFPK WNQRGNISGR LQVQDRYVSD DYITVDGAYV GLAPSGDAGS WQTECKGYQF 360 WTTTDADGFF SISDILVGDY NLYAFVPGFI GDYRNDVVLT ITEDSDIDMG DLVFEPIRDG 420 PTLWEIGIPS RSAAEFYIPD PDPTYVNKLY VNHPDRFRQY GLWERYSDLY PEGDLVYTVG 480 VSDYKNDWFY AQVPRKKDDN SYEATTWQIK FKLDSVDQNA TYKLRIALAT ANVAELQVRV 540 NDEKAEPPLF ATGQIGHDNA IARHGIHGLY RLYSMDVPAA NLAAGENTIF LKQATSSSAV 600 AGVMYDYIRF EGPPSSNSNR EKKEI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 2.0e-5 | 362 | 408 | 47 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 3.0e-27 | 313 | 412 | 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-54 | 424 | 611 | 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 | 2.0e-62 | 14 | 278 | 283 | + 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 | 2.0e-68 | 1 | 179 | 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 | 623 | 1 | 654 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 17 | 623 | 1 | 625 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301114.1 | 0 | 1 | 618 | 1 | 636 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 620 | 1 | 640 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 1 | 618 | 1 | 639 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY293973 | 350 | 1 | 326 | 0 |
FC896579 | 280 | 73 | 328 | 0 |
DY286978 | 278 | 73 | 326 | 0 |
FC887900 | 272 | 1 | 248 | 0 |
DY302144 | 310 | 1 | 281 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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