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Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa022021m |
Family | PL4 |
Protein Properties | Length: 619 Molecular Weight: 70568.2 Isoelectric Point: 7.828 |
Chromosome | Chromosome/Scaffold: 6 Start: 19820736 End: 19824274 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 1 | 603 | 0 |
VVLNNGLVQLTFSYPGGDVIGIKYKGIDNLLDIKNQPSNRGYWDLVWNKRGEKGGVDKLQGTRFKVVRTTSDQIEISFTKTYSHSLGNASVPLNVDKRYI MQRGRSGFYAYAIFERLKGMPEVDMDQIRIVYKLQQDKFRYMAISDDRKRVMPTADDRANGLPLAYPEAVLLTNPSNPDFRGEVDDKYQYSSEDKDNKVH GWICKDPAVGFWIITPSDEFRTAGPFKQDLTSHVGPTALSMFVSTHYAGKEVGMTFRDGEAWKKVFGPVFIHLNSAPSSNEYLTLWENAKEQLVEEMQRW PYNFTQSKDFLSSDQRGSVAGQLLVRDRYRNKRLIWASSAYVGLAAPGNAGSWQKESKGYQFWTQANKQGYFLIKDVRPGNYSLYATVPGFIGDYKYEAN IIIQPGKEINLADLTYEPPRNGPTLWEIGIPDRSAAEFNVPDPSPTLMNQLYTNHTDKFRQYGLWERYSDLYPNHDLIYTVGTDNYPDDWFFAHVTRNTG NQTYEPTTWQIRFQLNKGANPGNYTLQLALASATNAEVQVRVNDWSANPPHFTTGLIGKDNAIARHGIHGLYWLFSVGLRNDRLQEGNNTIYLTQSRHKT TFD |
Full Sequence |
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Protein Sequence Length: 619 Download |
VVLNNGLVQL TFSYPGGDVI GIKYKGIDNL LDIKNQPSNR GYWDLVWNKR GEKGGVDKLQ 60 GTRFKVVRTT SDQIEISFTK TYSHSLGNAS VPLNVDKRYI MQRGRSGFYA YAIFERLKGM 120 PEVDMDQIRI VYKLQQDKFR YMAISDDRKR VMPTADDRAN GLPLAYPEAV LLTNPSNPDF 180 RGEVDDKYQY SSEDKDNKVH GWICKDPAVG FWIITPSDEF RTAGPFKQDL TSHVGPTALS 240 MFVSTHYAGK EVGMTFRDGE AWKKVFGPVF IHLNSAPSSN EYLTLWENAK EQLVEEMQRW 300 PYNFTQSKDF LSSDQRGSVA GQLLVRDRYR NKRLIWASSA YVGLAAPGNA GSWQKESKGY 360 QFWTQANKQG YFLIKDVRPG NYSLYATVPG FIGDYKYEAN IIIQPGKEIN LADLTYEPPR 420 NGPTLWEIGI PDRSAAEFNV PDPSPTLMNQ LYTNHTDKFR QYGLWERYSD LYPNHDLIYT 480 VGTDNYPDDW FFAHVTRNTG NQTYEPTTWQ IRFQLNKGAN PGNYTLQLAL ASATNAEVQV 540 RVNDWSANPP HFTTGLIGKD NAIARHGIHG LYWLFSVGLR NDRLQEGNNT IYLTQSRHKT 600 TFDGIMYDYL RLEGPPQE* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.006 | 364 | 411 | 48 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 4.0e-30 | 315 | 414 | 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-46 | 426 | 613 | 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-73 | 1 | 276 | 282 | + 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 | 2.0e-83 | 1 | 184 | 186 | + 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 |
RefSeq | XP_002285626.1 | 0 | 3 | 616 | 1 | 616 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002308510.1 | 0 | 1 | 615 | 57 | 671 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002319997.1 | 0 | 1 | 617 | 1 | 619 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527229.1 | 0 | 1 | 618 | 54 | 670 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527245.1 | 0 | 1 | 617 | 2 | 620 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY969340 | 321 | 214 | 533 | 0 |
GW864372 | 311 | 130 | 438 | 0 |
EH792178 | 294 | 289 | 579 | 0 |
JG640880 | 271 | 138 | 406 | 0 |
GO374104 | 370 | 255 | 618 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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