| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT4G38030.1 |
| Family | PL4 |
| Protein Properties | Length: 668 Molecular Weight: 76620.8 Isoelectric Point: 9.6453 |
| Chromosome | Chromosome/Scaffold: 4 Start: 17863073 End: 17866730 |
| Description | rhamnogalacturonate lyase, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL4 | 51 | 649 | 0 |
| TREVIVDNGIIRVSFSNPQGLITGIKYKGIDNVLHPHLRDRGYWDITWQGTNIRQGGLDRIEGTNFRIITQTQEQVEISFSRTWEDGHIPLNVDKRYIIR RNTSGIYMYGIFERLPEWPELDMGLIRIAFKLNPERFHYMAVADNRQREMPTEDDRDIKRGHAKALGYKEAVQLTHPHNSMFKNQVDDKYQYTCEIKDNK VHGWISTKSRVGFWIISPSGEYRSGGPIKQELTSHVGPTAITTFISGHYVGADMEAHYRPGEAWKKVLGPVFIYLNSDSTSNNKPQDLLWEDAKQQSEKE VKAWPYDFVASSDYLSRRERGSVTGRLLVNDRFLTPGKSAYVGLAPPGEAGSWQTNTKGYQFWTKTNETGYFTIENVRPGTYNLYGWVPGFIGDFRYQNL VNVAAGSVISLGRVVYKPPRNGPTLWEIGVPDRTAREYFIPEPYKDTMNPLYLNHTDKFRQYGLWQRYTELYPTHDLVYTVGVSNYSQDWFYAQVTRKTG DLTYVPTIWQIVFHLPYVNSRGSYTLQVALASAAWANLQVRINNQNSWPFFSTGTIGKDNAIARHGIHGMYRLYTIDVPGRLLRTGTNTIYLRQPKAQG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 668 Download |
| MVSQKKIASL FICFLLLLLL PLSFSKPTRN LDGISARAPT VQQIRSRHHG TREVIVDNGI 60 IRVSFSNPQG LITGIKYKGI DNVLHPHLRD RGYWDITWQG TNIRQGGLDR IEGTNFRIIT 120 QTQEQVEISF SRTWEDGHIP LNVDKRYIIR RNTSGIYMYG IFERLPEWPE LDMGLIRIAF 180 KLNPERFHYM AVADNRQREM PTEDDRDIKR GHAKALGYKE AVQLTHPHNS MFKNQVDDKY 240 QYTCEIKDNK VHGWISTKSR VGFWIISPSG EYRSGGPIKQ ELTSHVGPTA ITTFISGHYV 300 GADMEAHYRP GEAWKKVLGP VFIYLNSDST SNNKPQDLLW EDAKQQSEKE VKAWPYDFVA 360 SSDYLSRRER GSVTGRLLVN DRFLTPGKSA YVGLAPPGEA GSWQTNTKGY QFWTKTNETG 420 YFTIENVRPG TYNLYGWVPG FIGDFRYQNL VNVAAGSVIS LGRVVYKPPR NGPTLWEIGV 480 PDRTAREYFI PEPYKDTMNP LYLNHTDKFR QYGLWQRYTE LYPTHDLVYT VGVSNYSQDW 540 FYAQVTRKTG DLTYVPTIWQ IVFHLPYVNS RGSYTLQVAL ASAAWANLQV RINNQNSWPF 600 FSTGTIGKDN AIARHGIHGM YRLYTIDVPG RLLRTGTNTI YLRQPKAQGP FEGLMYDYIR 660 LEEPSRA* 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam13620 | CarboxypepD_reg | 0.001 | 414 | 461 | 48 | + Carboxypeptidase regulatory-like domain. | ||
| cd10316 | RGL4_M | 4.0e-34 | 369 | 462 | 94 | + 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 | 1.0e-53 | 476 | 662 | 189 | + 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-76 | 44 | 330 | 292 | + 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 | 5.0e-92 | 47 | 236 | 195 | + 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. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0012505 | endomembrane system |
| GO:0016829 | lyase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAS99719.1 | 0 | 22 | 667 | 38 | 677 | At2g22620 [Arabidopsis thaliana] |
| DDBJ | BAD94618.1 | 0 | 158 | 667 | 1 | 510 | LG127/30 like gene [Arabidopsis thaliana] |
| EMBL | CAB37543.1 | 0 | 1 | 667 | 1 | 649 | LG127/30 like gene [Arabidopsis thaliana] |
| RefSeq | NP_179847.1 | 0 | 22 | 667 | 38 | 677 | lyase [Arabidopsis thaliana] |
| RefSeq | NP_195516.2 | 0 | 1 | 667 | 1 | 667 | lyase [Arabidopsis thaliana] |
