Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr3g111410.1 |
Family | PL4 |
Protein Properties | Length: 652 Molecular Weight: 74428.8 Isoelectric Point: 4.6453 |
Chromosome | Chromosome/Scaffold: 3 Start: 40329670 End: 40334922 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 6 | 626 | 0 |
VQLSIQDHHVVMDNGILRVTLSNPEGIVTGIQYSDIDNLLEVLNEESNRGYTLYWDLVWSSPTSTGTTGKFDVIKATTFKVILEDEDQVELSFTRTWDAS LEGKLVPLNIDKRFIMLRGCSGFYSYAIYEHLEDWPAFNLDETRIAFKLRKDKFHYMAMADNRQRNMPLPDDRVAPRGQALAYPEAVLLVNPIEPELKGE VDDKYQYSCDNKDSQVHGWICMDPAVGFWLITPSNEFRSGGPVKQNLTSHVGPTTLAVFLSAHYSGEDLVPKFKAGEAWKKVFGPVFIYVNSPYDGSDPI KLWDDAKLQMLMEVQSWPYNFPESDDFPKWDERGNVCGRLLVKERYIDDDYLSANCAYVGLATPGEVGSWQRECKNYQFWAKADDDGYFSISNIHVGDYN FYAWVPGFIGDYKYDVVISITEGCDIDIGDLVYEPPRDGPTLWEIGIPDRSAAEFYVPDPNPKYINKLYVNHPDKFRQYGIWERYAELYPDNDLIYTIGV SDFTKDWFFAQVTRKKEDNTYQGTTWQIKFNLDNVNRKGSYKLRVALASATYSELQVRVNDPKTNRPLFSSGLIGKDNSIARHGIHGLYWLYNVNIPGSL LVEGDNNTIFLTQARGNIPFQ |
Full Sequence |
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Protein Sequence Length: 652 Download |
MSSLGVQLSI QDHHVVMDNG ILRVTLSNPE GIVTGIQYSD IDNLLEVLNE ESNRGYTLYW 60 DLVWSSPTST GTTGKFDVIK ATTFKVILED EDQVELSFTR TWDASLEGKL VPLNIDKRFI 120 MLRGCSGFYS YAIYEHLEDW PAFNLDETRI AFKLRKDKFH YMAMADNRQR NMPLPDDRVA 180 PRGQALAYPE AVLLVNPIEP ELKGEVDDKY QYSCDNKDSQ VHGWICMDPA VGFWLITPSN 240 EFRSGGPVKQ NLTSHVGPTT LAVFLSAHYS GEDLVPKFKA GEAWKKVFGP VFIYVNSPYD 300 GSDPIKLWDD AKLQMLMEVQ SWPYNFPESD DFPKWDERGN VCGRLLVKER YIDDDYLSAN 360 CAYVGLATPG EVGSWQRECK NYQFWAKADD DGYFSISNIH VGDYNFYAWV PGFIGDYKYD 420 VVISITEGCD IDIGDLVYEP PRDGPTLWEI GIPDRSAAEF YVPDPNPKYI NKLYVNHPDK 480 FRQYGIWERY AELYPDNDLI YTIGVSDFTK DWFFAQVTRK KEDNTYQGTT WQIKFNLDNV 540 NRKGSYKLRV ALASATYSEL QVRVNDPKTN RPLFSSGLIG KDNSIARHGI HGLYWLYNVN 600 IPGSLLVEGD NNTIFLTQAR GNIPFQAIMY DYIRLEGPAT SSFRITLDLA W* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 3.0e-27 | 337 | 436 | 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-55 | 448 | 636 | 191 | + 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 | 3.0e-72 | 8 | 297 | 295 | + 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 | 1.0e-99 | 1 | 206 | 206 | + 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 | 650 | 1 | 656 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 17 | 650 | 1 | 627 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 17 | 637 | 1 | 613 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 1 | 639 | 1 | 632 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527353.1 | 0 | 1 | 642 | 1 | 637 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DW479599 | 297 | 1 | 297 | 0 |
DW479600 | 301 | 1 | 301 | 0 |
DT552229 | 296 | 17 | 311 | 0 |
DY293973 | 353 | 1 | 350 | 0 |
GR828586 | 235 | 170 | 404 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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