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Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10010965m |
Family | PL4 |
Protein Properties | Length: 618 Molecular Weight: 70895.5 Isoelectric Point: 4.7865 |
Chromosome | Chromosome/Scaffold: 1 Start: 3286134 End: 3289642 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 1 | 602 | 0 |
MDNGIARVTLSKPDGIVTGIEYNGIDNLLEVLNEEVNRGYWDLVWGGSGTAGGFDVIKGTNFEVIMKNEEQIELSFTRKWDPSLEGKAVPLNIDKRFVML RGSSGFYTYAIYEHLKEWPAFSLAETRIAFKLRKDKFHYMAVTDDRQRFMPLPDDRLPDRGQALAYPEAVLLVNPVEPQFKGEVDDKYQYSCENKDITVH GWICTEQPSVGFWLITPSHEYRTGGPQKQNLTSHVGPTSLAVFMSAHYSGEDLVPKFTEGEAWKKVFGPVFVYLNSSTDDENDPLWLWQDAKSQMNVETE SWPYSFPASDDYVKAEQRGNVVGRLLVQDRYVDTDFIAANRGYVGLAVPGAAGSWQRECKEYQFWTRTDEEGFFYISGIRPGQYNLYAWVPGFIGDYKYD DIITITSGCYIYMEDLVYQPRRNGETLWEIGFPDRSAAEFYVPDPNPKYINNLYKNHPDRFRQYGLWERYAELYPDKDLVYVVGSSDYRKDWFYAQVTRR KDSKTYQGTTWQIKFELENIDKSQSYTLRVAIASATFSELQIRVNDATASPLFTSGLIGRDNSIARHGIHGLYWLFNVEVAGSKLVEGENTLFLTQPRST SP |
Full Sequence |
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Protein Sequence Length: 618 Download |
MDNGIARVTL SKPDGIVTGI EYNGIDNLLE VLNEEVNRGY WDLVWGGSGT AGGFDVIKGT 60 NFEVIMKNEE QIELSFTRKW DPSLEGKAVP LNIDKRFVML RGSSGFYTYA IYEHLKEWPA 120 FSLAETRIAF KLRKDKFHYM AVTDDRQRFM PLPDDRLPDR GQALAYPEAV LLVNPVEPQF 180 KGEVDDKYQY SCENKDITVH GWICTEQPSV GFWLITPSHE YRTGGPQKQN LTSHVGPTSL 240 AVFMSAHYSG EDLVPKFTEG EAWKKVFGPV FVYLNSSTDD ENDPLWLWQD AKSQMNVETE 300 SWPYSFPASD DYVKAEQRGN VVGRLLVQDR YVDTDFIAAN RGYVGLAVPG AAGSWQRECK 360 EYQFWTRTDE EGFFYISGIR PGQYNLYAWV PGFIGDYKYD DIITITSGCY IYMEDLVYQP 420 RRNGETLWEI GFPDRSAAEF YVPDPNPKYI NNLYKNHPDR FRQYGLWERY AELYPDKDLV 480 YVVGSSDYRK DWFYAQVTRR KDSKTYQGTT WQIKFELENI DKSQSYTLRV AIASATFSEL 540 QIRVNDATAS PLFTSGLIGR DNSIARHGIH GLYWLFNVEV AGSKLVEGEN TLFLTQPRST 600 SPFQGIMYDY IRFEAPS* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.003 | 341 | 393 | 57 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 5.0e-30 | 317 | 416 | 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 | 3.0e-56 | 428 | 614 | 189 | + 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-71 | 1 | 280 | 286 | + 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 | 6.0e-104 | 1 | 184 | 184 | + 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 | 616 | 17 | 644 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_172460.6 | 0 | 1 | 617 | 1 | 617 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002285626.1 | 0 | 1 | 616 | 1 | 615 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 1 | 615 | 1 | 613 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 616 | 17 | 633 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FD943935 | 247 | 372 | 618 | 0 |
DK498554 | 248 | 1 | 244 | 0 |
DT552229 | 294 | 1 | 291 | 0 |
DW479600 | 281 | 2 | 279 | 0 |
DW479599 | 279 | 1 | 276 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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