| Basic Information | |
|---|---|
| Species | Mimulus guttatus |
| Cazyme ID | mgv1a019191m |
| Family | PL4 |
| Protein Properties | Length: 633 Molecular Weight: 71790.4 Isoelectric Point: 6.8374 |
| Chromosome | Chromosome/Scaffold: 24 Start: 1848498 End: 1851762 |
| Description | Rhamnogalacturonate lyase family protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| PL4 | 4 | 614 | 0 |
| KNVTLITQPSYITIDNGFVKLTISKPQGLLTAIKYGGVENILDLKSNELNRGYWDINWNLPGGHNRYQLLRGSEYTVINYSNNHLEVSFKNTYNPSIRGT TLLPLTFDIRYIVRSGVSGFYCYTICERSDNCPAFDLAQTRMVFKLHRDRFHYMAITDEKQRVMPMPDDLLPGRGKQLIVPESVLLVNPINPDLKGEVDD KYQYSMDNKDGGVHGWISSDPIIGFWIIFPSQEFRNGGPTKQNLTVHTGPACLAMFHGSHYIGNEMSARFEQGETWTKVLGPVFVYLNSTSVVSNAYNLW LDAKKQRLNQESLWPYDFVNSQYYLTDKERGSVSGRLFVQDRFISSSLLPAKSAFIGLSAARTEGSWQLESKGYQFWVNTDSDGNFTIKNVVPGIYGLHG WIPGFVGDYLKQELITISQGSEIQMENITYAPPRDGPTIWEIGFADRTAQDYYVPDVNPMYVNKLFLNSPEKFRQYGLWDRYTDVNPKYDQVFTIGVSDP KKDWFFAHVDRRIGEKYVPTTWAIRFSLKSVTVGTYKLRLAIASATRSDLEVHVNEMNAEQLVFQVTNLGADNTVCRHGIHGLYRLFSADISSTLLVNGD NCIFLTQARGG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 633 Download |
| MSMKNVTLIT QPSYITIDNG FVKLTISKPQ GLLTAIKYGG VENILDLKSN ELNRGYWDIN 60 WNLPGGHNRY QLLRGSEYTV INYSNNHLEV SFKNTYNPSI RGTTLLPLTF DIRYIVRSGV 120 SGFYCYTICE RSDNCPAFDL AQTRMVFKLH RDRFHYMAIT DEKQRVMPMP DDLLPGRGKQ 180 LIVPESVLLV NPINPDLKGE VDDKYQYSMD NKDGGVHGWI SSDPIIGFWI IFPSQEFRNG 240 GPTKQNLTVH TGPACLAMFH GSHYIGNEMS ARFEQGETWT KVLGPVFVYL NSTSVVSNAY 300 NLWLDAKKQR LNQESLWPYD FVNSQYYLTD KERGSVSGRL FVQDRFISSS LLPAKSAFIG 360 LSAARTEGSW QLESKGYQFW VNTDSDGNFT IKNVVPGIYG LHGWIPGFVG DYLKQELITI 420 SQGSEIQMEN ITYAPPRDGP TIWEIGFADR TAQDYYVPDV NPMYVNKLFL NSPEKFRQYG 480 LWDRYTDVNP KYDQVFTIGV SDPKKDWFFA HVDRRIGEKY VPTTWAIRFS LKSVTVGTYK 540 LRLAIASATR SDLEVHVNEM NAEQLVFQVT NLGADNTVCR HGIHGLYRLF SADISSTLLV 600 NGDNCIFLTQ ARGGDSLCGI LYDYLRLEAP PT* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd10316 | RGL4_M | 2.0e-28 | 332 | 431 | 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 | 1.0e-40 | 443 | 628 | 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 | 7.0e-64 | 8 | 299 | 298 | + 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-65 | 1 | 201 | 201 | + 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 |
| EMBL | CBI23231.1 | 0 | 17 | 632 | 2 | 617 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_001769727.1 | 0 | 15 | 630 | 4 | 620 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002285626.1 | 0 | 17 | 632 | 1 | 617 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002317123.1 | 0 | 1 | 632 | 1 | 631 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002527357.1 | 0 | 1 | 632 | 1 | 636 | lyase, putative [Ricinus communis] |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| GE473226 | 288 | 187 | 474 | 0 |
| DV995349 | 288 | 187 | 474 | 0 |
| CO473731 | 278 | 187 | 464 | 0 |
| DY969340 | 318 | 234 | 548 | 0 |
| CO474992 | 279 | 237 | 515 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
