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Basic Information | |
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Species | Vitis vinifera |
Cazyme ID | GSVIVT01006298001 |
Family | PL4 |
Protein Properties | Length: 621 Molecular Weight: 70661.1 Isoelectric Point: 9.0133 |
Chromosome | Chromosome/Scaffold: Start: 24726795 End: 24731088 |
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 | 3 | 601 | 0 |
QVEMNNGIVKITVSRPYGNLRGIKYHGVENLLDDGLDRDDRGYWDCSWEDVNGSNGKQSMILGDRFQVIMQTNNQVEVSFKTTWKSSDPLPALNVDKRYV MLSGSSGFYTYAIYERLKGWPGMFLWETRIVFKLSQKWFQYMAISDTRQRIMPTIADRERGQSLAYPEAVLLKNPMNSELEGEVDDKYQYSSESKNDRVH GWISLNSGIGFWIITPSYEFRTAGPLKQDLTGHVGPICLSMLMSAHYTGVPLNVTFENGEPWKKVFGPVFIHLNSVSDKTKATSLWGDAKQQTWKEIISW PYSFPHSPDFLKSDQRGSVIGQLSVQDQYLKVGNGPARFAHVGLAAPGDARSWEYQTKGYQFWTRTDEHGNFYIKAVLPGAYNLHAWVSGVMGNYMYEAT VTVTPGSVTKLPPLVFKPPRDGPTLWEIGIPNRHAAEFYVPNVTKNINTLYLEQDKFRQYGLWERYAELYPENDLVFTVGTSDYAKDWFFAHVLRRLPDG QFKATTWQIVFDLPKVDKVGTYKLRLVLAAAHMAEVQVRVNRRDAIRPAFTTGLTGRDNAIARHGIHGVQRSFTAALPGSLFVNGRNTIFLHQPRNQEA |
Full Sequence |
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Protein Sequence Length: 621 Download |
MFQVEMNNGI VKITVSRPYG NLRGIKYHGV ENLLDDGLDR DDRGYWDCSW EDVNGSNGKQ 60 SMILGDRFQV IMQTNNQVEV SFKTTWKSSD PLPALNVDKR YVMLSGSSGF YTYAIYERLK 120 GWPGMFLWET RIVFKLSQKW FQYMAISDTR QRIMPTIADR ERGQSLAYPE AVLLKNPMNS 180 ELEGEVDDKY QYSSESKNDR VHGWISLNSG IGFWIITPSY EFRTAGPLKQ DLTGHVGPIC 240 LSMLMSAHYT GVPLNVTFEN GEPWKKVFGP VFIHLNSVSD KTKATSLWGD AKQQTWKEII 300 SWPYSFPHSP DFLKSDQRGS VIGQLSVQDQ YLKVGNGPAR FAHVGLAAPG DARSWEYQTK 360 GYQFWTRTDE HGNFYIKAVL PGAYNLHAWV SGVMGNYMYE ATVTVTPGSV TKLPPLVFKP 420 PRDGPTLWEI GIPNRHAAEF YVPNVTKNIN TLYLEQDKFR QYGLWERYAE LYPENDLVFT 480 VGTSDYAKDW FFAHVLRRLP DGQFKATTWQ IVFDLPKVDK VGTYKLRLVL AAAHMAEVQV 540 RVNRRDAIRP AFTTGLTGRD NAIARHGIHG VQRSFTAALP GSLFVNGRNT IFLHQPRNQE 600 AFQGVMYDYI RLEGPPQSTH * 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 5.0e-30 | 317 | 416 | 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 | 7.0e-46 | 428 | 613 | 187 | + 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 | 5.0e-59 | 3 | 284 | 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 | 1.0e-65 | 1 | 186 | 189 | + 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 | CBI33189.1 | 0 | 1 | 620 | 1 | 620 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264484.1 | 0 | 6 | 617 | 1 | 596 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264864.1 | 0.0000008 | 6 | 32 | 1 | 27 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264864.1 | 0 | 157 | 620 | 48 | 510 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002271814.1 | 0 | 6 | 620 | 1 | 597 | PREDICTED: hypothetical protein [Vitis vinifera] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY969340 | 321 | 216 | 533 | 0 |
EL398250 | 271 | 120 | 390 | 0 |
GW864372 | 311 | 132 | 440 | 0 |
JG640880 | 271 | 141 | 409 | 0 |
EL450442 | 279 | 99 | 377 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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