Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10000697m |
Family | PL4 |
Protein Properties | Length: 643 Molecular Weight: 73677.5 Isoelectric Point: 8.9795 |
Chromosome | Chromosome/Scaffold: 15 Start: 1125706 End: 1129783 |
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 | 22 | 621 | 0 |
VSHDKVVVDNGIIQVTFSSPQGLITGIKYNGIDNVLDDEIDDRGYWDVVWYEPGKKGETDKLEGTKFEIITQNEEQVEISFTRTWTISKRGSLAPLNVDK RYIIRSGVSGIYMYGILERLEGWPDVDMDQIRIVFKLNPKKFDFMAISDDRQRSMPSMADRNNAKELAYKEAVLLTNPSNPMFKGEVDDKYMYSMEDKDN NVHGWISSDPPVGFWMITPSDEFRLGGPIKQDLTSHAGPITLSMFTSTHYAGKEMRMDYRNGEPWKKVFGPVFAYLNSVSPKDSTLRLWRDAKRQMAAEV KSWPYEFVKSEDYPLSHQRGTIQGQFYIKDSYVSRLRIYGKFAFVGLAPIGEAGSWQTESKGYQFWTKADRKGRFIIENVRAGNYSLYAWGFGFIGDYKY EQNITITPGSKMNVGQIVYEPPRNGPTLWEIGVPDRTAGEFYIPDPYPTLMNKLYVNPLQDRFRQYGLWDRYADLYPQNDLVYTIGVSDYRRDWFFAHVT RNVGNNTYQATTWQIIFNLKNVNRVRLYTLRIALASAADSELQVRINNPKSDHIFTTGYIGKDNAIARHGIHGLYRLYSIDVGGNLLSVGDNTIYLTQTR |
Full Sequence |
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Protein Sequence Length: 643 Download |
NKLNITKPGQ TIPAPIVQLR KVSHDKVVVD NGIIQVTFSS PQGLITGIKY NGIDNVLDDE 60 IDDRGYWDVV WYEPGKKGET DKLEGTKFEI ITQNEEQVEI SFTRTWTISK RGSLAPLNVD 120 KRYIIRSGVS GIYMYGILER LEGWPDVDMD QIRIVFKLNP KKFDFMAISD DRQRSMPSMA 180 DRNNAKELAY KEAVLLTNPS NPMFKGEVDD KYMYSMEDKD NNVHGWISSD PPVGFWMITP 240 SDEFRLGGPI KQDLTSHAGP ITLSMFTSTH YAGKEMRMDY RNGEPWKKVF GPVFAYLNSV 300 SPKDSTLRLW RDAKRQMAAE VKSWPYEFVK SEDYPLSHQR GTIQGQFYIK DSYVSRLRIY 360 GKFAFVGLAP IGEAGSWQTE SKGYQFWTKA DRKGRFIIEN VRAGNYSLYA WGFGFIGDYK 420 YEQNITITPG SKMNVGQIVY EPPRNGPTLW EIGVPDRTAG EFYIPDPYPT LMNKLYVNPL 480 QDRFRQYGLW DRYADLYPQN DLVYTIGVSD YRRDWFFAHV TRNVGNNTYQ ATTWQIIFNL 540 KNVNRVRLYT LRIALASAAD SELQVRINNP KSDHIFTTGY IGKDNAIARH GIHGLYRLYS 600 IDVGGNLLSV GDNTIYLTQT RSLGPFQGVM YDYIRLEGPS RT* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.006 | 378 | 435 | 58 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 1.0e-28 | 339 | 438 | 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-52 | 450 | 637 | 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 | 3.0e-84 | 27 | 306 | 286 | + 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-98 | 15 | 208 | 198 | + 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 | AAS99719.1 | 0 | 1 | 642 | 36 | 677 | At2g22620 [Arabidopsis thaliana] |
RefSeq | NP_179847.1 | 0 | 1 | 642 | 36 | 677 | lyase [Arabidopsis thaliana] |
RefSeq | NP_195508.2 | 0 | 1 | 640 | 35 | 676 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002308510.1 | 0 | 17 | 642 | 47 | 674 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527245.1 | 0 | 27 | 642 | 2 | 621 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DK560847 | 226 | 418 | 643 | 0 |
DY969340 | 323 | 236 | 558 | 0 |
EG486176 | 211 | 433 | 643 | 0 |
GR312932 | 283 | 361 | 640 | 0 |
EV572092 | 274 | 264 | 534 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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