| Basic Information | |
|---|---|
| Species | Mimulus guttatus |
| Cazyme ID | mgv1a003154m |
| Family | PL4 |
| Protein Properties | Length: 605 Molecular Weight: 69326.7 Isoelectric Point: 4.467 |
| Chromosome | Chromosome/Scaffold: 3 Start: 2347205 End: 2351865 |
| Description | Rhamnogalacturonate lyase family protein |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL4 | 2 | 586 | 0 |
| VTAIEYNGIDNLLQFDYKENNRGYWDLVWSKPDHPHDVFDKLDGDSFEVIMEDENQVEISFLRTWNSSETGLPLNIDKRYIMVRGSSGFYSYAIFERLEG WPDVNIAQGRIVFKLQQNLFRYMAVSDDRQRIMPTSEDRDNGEALDYPEAVLLTNPANDFLRGEVDDKYQYSSDNKDNRVHGWICSDPPTGFWIITPSNE FKTAGPVKQDLTSHAGPISLSMFFSTHYAGQPLILKFRDGEPWKKVFGPVFVYLNSVLEGEEPLALWPDAKEQMLIETESWPYDFPKSGDFPYADQRGTV SGRLVVRDSYISERLIIARSAYIGLAPPGEPGSWQRENKGYQFWTETDDMGYFLINGIRSGNYSLYAWIPGFIGDYKCDIQIEVRPGCKIRLGYIIYDPP RNGPTLWEIGIPDRTAAEFFVPDPNPTLMNQLYNIQPDKFRQYGLWDRYTDLYPDEDLVYTIGSSVYQTDWYFAHVNRNIGNKTYVPTTWKILFELDDVD ESANYTLQIALASANDAELQVRINDETTETPYFKTGLIGKDNAIARHGIHGLYWLYSVSIPGSTLVCTTTNTILLTQSRGSTPWK | |||
| Full Sequence |
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| Protein Sequence Length: 605 Download |
| MVTAIEYNGI DNLLQFDYKE NNRGYWDLVW SKPDHPHDVF DKLDGDSFEV IMEDENQVEI 60 SFLRTWNSSE TGLPLNIDKR YIMVRGSSGF YSYAIFERLE GWPDVNIAQG RIVFKLQQNL 120 FRYMAVSDDR QRIMPTSEDR DNGEALDYPE AVLLTNPAND FLRGEVDDKY QYSSDNKDNR 180 VHGWICSDPP TGFWIITPSN EFKTAGPVKQ DLTSHAGPIS LSMFFSTHYA GQPLILKFRD 240 GEPWKKVFGP VFVYLNSVLE GEEPLALWPD AKEQMLIETE SWPYDFPKSG DFPYADQRGT 300 VSGRLVVRDS YISERLIIAR SAYIGLAPPG EPGSWQRENK GYQFWTETDD MGYFLINGIR 360 SGNYSLYAWI PGFIGDYKCD IQIEVRPGCK IRLGYIIYDP PRNGPTLWEI GIPDRTAAEF 420 FVPDPNPTLM NQLYNIQPDK FRQYGLWDRY TDLYPDEDLV YTIGSSVYQT DWYFAHVNRN 480 IGNKTYVPTT WKILFELDDV DESANYTLQI ALASANDAEL QVRINDETTE TPYFKTGLIG 540 KDNAIARHGI HGLYWLYSVS IPGSTLVCTT TNTILLTQSR GSTPWKGIMY DYIRLEAPSS 600 NMHA* 660 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd10316 | RGL4_M | 1.0e-28 | 297 | 394 | 98 | + 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 | 6.0e-51 | 408 | 596 | 191 | + 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-64 | 3 | 257 | 260 | + 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 | 4.0e-72 | 2 | 166 | 168 | + 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 |
| RefSeq | XP_002308510.1 | 0 | 2 | 598 | 75 | 671 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002319997.1 | 0 | 2 | 598 | 19 | 617 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002527229.1 | 0 | 2 | 601 | 72 | 670 | lyase, putative [Ricinus communis] |
| RefSeq | XP_002527245.1 | 0 | 2 | 599 | 20 | 619 | lyase, putative [Ricinus communis] |
| RefSeq | XP_002527353.1 | 0 | 1 | 601 | 32 | 636 | lyase, putative [Ricinus communis] |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| DY969340 | 321 | 196 | 515 | 0 |
| GR019925 | 221 | 387 | 605 | 0 |
| EL398250 | 271 | 100 | 370 | 0 |
| EL450442 | 279 | 79 | 357 | 0 |
| GW864372 | 311 | 112 | 420 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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