Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s60_134V6.1 |
Family | PL4 |
Protein Properties | Length: 664 Molecular Weight: 75504.2 Isoelectric Point: 6.5184 |
Chromosome | Chromosome/Scaffold: 60 Start: 834768 End: 839165 |
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 | 24 | 633 | 0 |
EVLLVEQSDYVVLDNGIVQVTLTKPGGNVTSIKYGGIENLLEYKNKETNRGYWDMNWSHEKGGQDNFLVFFGTIYKVIHKDANRVEVSFLRPYDPAYPSE LPLNVDKRFVLLKGSSGFYSYGIYERPAGWPEFNLNQTRITFKLSNDKFHYMAIADDRQRFMPSPEDLMPDRSQQLAYPEAHLLTNPIDPAFLGEVDDKY QYSKENKDLKVHGWVSTNPMVGFWIISPSYEFRNGGVTKQNLTAHVGPTCLAMFHSAHYAGLDLCPHFQQGEAWQKVFGPVFIYLNSAPVGTPYPALWQN AQAQVTREMAAWPYSWPASDAYPKAAERGTLCGRLLVSDPLQSPYTWVGRNAYLGLAIPGETGSWQSESKGYQFWTQADAYGCFSIRNIRAGLYDLYGWV PGVVGDYKFERGPIRIQQGGIIDMGDLTYYSPRNGPTVWEIGVPDRTAAGFFVPDPNPKYVNKLYLNSSQKWRQYGLWERYTELYPTNDLVYTVGQSDWR KDWFYAHLNRIMPDGSYAPTTWEIRFELLKVVPDSPYKLRIATASSHTASIQLFVNKLDYAKPVFDTLQYGRDNATARHGIHGLYTLWNIDIEPKLLQVG KNSFYLSQRK |
Full Sequence |
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Protein Sequence Length: 664 Download |
MNQQLDELIP ENDRPHTSGL AGTEVLLVEQ SDYVVLDNGI VQVTLTKPGG NVTSIKYGGI 60 ENLLEYKNKE TNRGYWDMNW SHEKGGQDNF LVFFGTIYKV IHKDANRVEV SFLRPYDPAY 120 PSELPLNVDK RFVLLKGSSG FYSYGIYERP AGWPEFNLNQ TRITFKLSND KFHYMAIADD 180 RQRFMPSPED LMPDRSQQLA YPEAHLLTNP IDPAFLGEVD DKYQYSKENK DLKVHGWVST 240 NPMVGFWIIS PSYEFRNGGV TKQNLTAHVG PTCLAMFHSA HYAGLDLCPH FQQGEAWQKV 300 FGPVFIYLNS APVGTPYPAL WQNAQAQVTR EMAAWPYSWP ASDAYPKAAE RGTLCGRLLV 360 SDPLQSPYTW VGRNAYLGLA IPGETGSWQS ESKGYQFWTQ ADAYGCFSIR NIRAGLYDLY 420 GWVPGVVGDY KFERGPIRIQ QGGIIDMGDL TYYSPRNGPT VWEIGVPDRT AAGFFVPDPN 480 PKYVNKLYLN SSQKWRQYGL WERYTELYPT NDLVYTVGQS DWRKDWFYAH LNRIMPDGSY 540 APTTWEIRFE LLKVVPDSPY KLRIATASSH TASIQLFVNK LDYAKPVFDT LQYGRDNATA 600 RHGIHGLYTL WNIDIEPKLL QVGKNSFYLS QRKDYGPFAA VMYDYLRLEA PASSFPGILD 660 SAK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 2.0e-25 | 350 | 430 | 81 | + 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 | 3.0e-48 | 462 | 649 | 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 | 4.0e-67 | 27 | 311 | 290 | + 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 | 6.0e-83 | 1 | 219 | 219 | + 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 |
RefSeq | NP_001062464.1 | 0 | 15 | 654 | 18 | 658 | Os08g0554100 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_001763359.1 | 0 | 34 | 663 | 1 | 632 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769727.1 | 0 | 34 | 661 | 4 | 630 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002445711.1 | 0 | 10 | 654 | 17 | 663 | hypothetical protein SORBIDRAFT_07g024560 [Sorghum bicolor] |
RefSeq | XP_002527352.1 | 0 | 20 | 652 | 1 | 632 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FC327604 | 260 | 170 | 429 | 0 |
FC337098 | 260 | 323 | 582 | 0 |
BY960460 | 180 | 1 | 180 | 0 |
GW864372 | 312 | 163 | 474 | 0 |
DY293973 | 351 | 20 | 364 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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