| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra010629 |
| Family | PL4 |
| Protein Properties | Length: 721 Molecular Weight: 82267.9 Isoelectric Point: 9.4682 |
| Chromosome | Chromosome/Scaffold: 08 Start: 15681565 End: 15685632 |
| Description | Rhamnogalacturonate lyase family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL4 | 103 | 700 | 0 |
| RNKEVIVDNGIVRVTFSNPKGLITGIKYNEIGNVLNPYLRARGYWDITWQTENNSLPKLDRIEGTNFRIITQNEEQVEISFSRTWNGGSDHIPLNVDKRY IIRTNTSGIYTYGIFERQPEWPEVEMGLIRVAFKLNPDRFHYMVVADNRQRQMPTDDDRDINSGRAKPLAYKEAVKLTNPHNHMFKNQVDDKYQYSCEVK DNKVHGWISTKSNVGFWLISPSGEYRSGGPVKQGLTSHVGPTTLTTFISQHYVGPDMETRYKTGEAWKKVLGPVFIYLNSDSTRNNLQHLLWEDAKRQTE QEVEAWPYGFVASSDFPTRQERGTITGRLFVNDRFLAPAGYAYIGLAPPGEAGSWQTNTKGYQFWTQTNETGYFTIDNVRPGTYNLYGWVHGFIGDFKYQ NLVNVAAGSEISLDRVVFQPPRNGPTLWEIGVPDRTAREYFVPEPYENTMNPLYLNHTDKFRQYGLWQRYTELYPNHDLVYTVGVSNYSQDWFYAHVTRN IGGSTYVPATWQIVFELPYVNWRGSYTLQIALASAARANLKVRFNNEYSRPLLSAGVGRDNAIARHGIHGAYHLYSIDVPGRLLRTGTNTIYLRQSKA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 721 Download |
| MISQKTIASW MICFLLLLLL PIAFSEPTRN LKGTNARAPT VQQIRNKEVI VDNGIVRVTF 60 SNPKGLITGI KYNEIGNVLN PYLRARGNLK GTNARAPTVQ QIRNKEVIVD NGIVRVTFSN 120 PKGLITGIKY NEIGNVLNPY LRARGYWDIT WQTENNSLPK LDRIEGTNFR IITQNEEQVE 180 ISFSRTWNGG SDHIPLNVDK RYIIRTNTSG IYTYGIFERQ PEWPEVEMGL IRVAFKLNPD 240 RFHYMVVADN RQRQMPTDDD RDINSGRAKP LAYKEAVKLT NPHNHMFKNQ VDDKYQYSCE 300 VKDNKVHGWI STKSNVGFWL ISPSGEYRSG GPVKQGLTSH VGPTTLTTFI SQHYVGPDME 360 TRYKTGEAWK KVLGPVFIYL NSDSTRNNLQ HLLWEDAKRQ TEQEVEAWPY GFVASSDFPT 420 RQERGTITGR LFVNDRFLAP AGYAYIGLAP PGEAGSWQTN TKGYQFWTQT NETGYFTIDN 480 VRPGTYNLYG WVHGFIGDFK YQNLVNVAAG SEISLDRVVF QPPRNGPTLW EIGVPDRTAR 540 EYFVPEPYEN TMNPLYLNHT DKFRQYGLWQ RYTELYPNHD LVYTVGVSNY SQDWFYAHVT 600 RNIGGSTYVP ATWQIVFELP YVNWRGSYTL QIALASAARA NLKVRFNNEY SRPLLSAGVG 660 RDNAIARHGI HGAYHLYSID VPGRLLRTGT NTIYLRQSKA VGPFEGLMYD YIRLEEPSTA 720 * 780 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam13620 | CarboxypepD_reg | 0.009 | 468 | 516 | 49 | + Carboxypeptidase regulatory-like domain. | ||
| cd10316 | RGL4_M | 1.0e-31 | 423 | 515 | 93 | + 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-47 | 530 | 715 | 188 | + 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-70 | 104 | 389 | 291 | + 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 | 9.0e-82 | 86 | 291 | 209 | + 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| DDBJ | BAD94618.1 | 0 | 214 | 720 | 2 | 510 | LG127/30 like gene [Arabidopsis thaliana] |
| EMBL | CAB37543.1 | 2e-20 | 1 | 101 | 1 | 105 | LG127/30 like gene [Arabidopsis thaliana] |
| EMBL | CAB37543.1 | 0 | 88 | 720 | 30 | 649 | LG127/30 like gene [Arabidopsis thaliana] |
| RefSeq | NP_195516.2 | 2e-19 | 1 | 102 | 1 | 111 | lyase [Arabidopsis thaliana] |
| RefSeq | NP_195516.2 | 0 | 88 | 720 | 30 | 667 | lyase [Arabidopsis thaliana] |
