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Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29596.m000701 |
Family | PL4 |
Protein Properties | Length: 633 Molecular Weight: 72720.4 Isoelectric Point: 6.748 |
Chromosome | Chromosome/Scaffold: 29596 Start: 116918 End: 122690 |
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 | 4 | 613 | 0 |
PAVRLHIQDRHVVMENGIVQITLSKPEGIVTGIRYSGIDNLLEILNRESNRGYWDLFWNPPGGKGIFDVISGTNFRVIVENEEQIEISFTRMWDSSLEGK YIPLNIDKRFILLRGSSGFYSYAIYEHLPEWPGFELGETRITFKLRKDKFQYMAVANDRQRPMPLPDDRMPGRCQTLGYPEAVLLLNPKDPVLKGEVDDK YQYSCENKDNRVHGWMCFNPPVGFWQITPSNEFRTGGPLKQNLTSHVGPTTLAMFHSSHYAGKDLVPRFNPGEHWKKVFGPVFIYLNSVPPGYDSRFLWE DAKTQMMTEVQSWPYSFPASEDFQKSEQRGNICGRLLVKDRYLNEDYIFASGASVGVAPPGDVGSWQRECKDYQFWTTADGNGYFSIRNVRTGDYNLYAW VPGFIGDYRCQAVITIISGCNIDVGDLVYEPPRDGPTLWEIGIPDRSAAEFYVPDPEPRHVNKLFINHPDRFRQYGLWSRYVDLYPEVDLVYTVGLSDYS KDWFFAQVVRRRDDGTHVGTTWQIKFKLDKIDQRSNYKLRVALASATLAELQVRVNDSKAVRPLFTTGLIGRDNSIARHGIHGLYWLYNVNVPGARLVEG ENTIFFTQPR |
Full Sequence |
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Protein Sequence Length: 633 Download |
MAHPAVRLHI QDRHVVMENG IVQITLSKPE GIVTGIRYSG IDNLLEILNR ESNRGYWDLF 60 WNPPGGKGIF DVISGTNFRV IVENEEQIEI SFTRMWDSSL EGKYIPLNID KRFILLRGSS 120 GFYSYAIYEH LPEWPGFELG ETRITFKLRK DKFQYMAVAN DRQRPMPLPD DRMPGRCQTL 180 GYPEAVLLLN PKDPVLKGEV DDKYQYSCEN KDNRVHGWMC FNPPVGFWQI TPSNEFRTGG 240 PLKQNLTSHV GPTTLAMFHS SHYAGKDLVP RFNPGEHWKK VFGPVFIYLN SVPPGYDSRF 300 LWEDAKTQMM TEVQSWPYSF PASEDFQKSE QRGNICGRLL VKDRYLNEDY IFASGASVGV 360 APPGDVGSWQ RECKDYQFWT TADGNGYFSI RNVRTGDYNL YAWVPGFIGD YRCQAVITII 420 SGCNIDVGDL VYEPPRDGPT LWEIGIPDRS AAEFYVPDPE PRHVNKLFIN HPDRFRQYGL 480 WSRYVDLYPE VDLVYTVGLS DYSKDWFFAQ VVRRRDDGTH VGTTWQIKFK LDKIDQRSNY 540 KLRVALASAT LAELQVRVND SKAVRPLFTT GLIGRDNSIA RHGIHGLYWL YNVNVPGARL 600 VEGENTIFFT QPRCTCPFQG LMYDYIRLEG PSL 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.004 | 380 | 407 | 28 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 1.0e-30 | 331 | 430 | 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-53 | 442 | 629 | 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-77 | 6 | 291 | 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 | 3.0e-99 | 1 | 200 | 200 | + 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 | CBI19298.1 | 0 | 1 | 631 | 1 | 644 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 17 | 631 | 1 | 615 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002306520.1 | 0 | 17 | 631 | 1 | 615 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 1 | 633 | 1 | 633 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527353.1 | 0 | 1 | 631 | 1 | 633 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GW864372 | 311 | 144 | 454 | 0 |
DY293973 | 350 | 1 | 344 | 0 |
DW479599 | 295 | 1 | 292 | 0 |
DW479600 | 295 | 1 | 292 | 0 |
GO266963 | 263 | 1 | 263 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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