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Basic Information | |
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Species | Vitis vinifera |
Cazyme ID | GSVIVT01009215001 |
Family | PL4 |
Protein Properties | Length: 657 Molecular Weight: 74385.1 Isoelectric Point: 4.9319 |
Chromosome | Chromosome/Scaffold: 18 Start: 6286736 End: 6292127 |
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 | 8 | 630 | 0 |
LYIQDRHVVMDNGILQVTLSNPGGIVTGIRYSAIDNLLEVLNDETNRGYWDLVWSVPGSAGIFDVIKGTNFRVIVENEEQVEISFTRMWDPSLEGKLVPL NIDKRFIMLRGSSGFYSYAIYEHLKEWPAFTLAETRIAFKLRKDNTVLKGKMKKHRLFHYMAMADNRQRFMPLPDDRLPGRGQPLAYPEAVLLVNPVEPE FKGEVDDKYQYSCDNKDNRVHGWVCLEPPVGFWQITPSDEFRTGGPVKQNLTSHVGPTTLAMFHSAHYAGEPLVPKFGPDEPWKKVFGPVFIYVNSVFGD GDPFWLWEDAKEQMTIEVQSWPYSFPASEDFPSSDQRGNVSGRLLVQDGYISDDYILASCAYVGLAPPGDVGSWQRECKDYQFWTQADLGGYFCINDIRP GDYNLYAWVPGFIGDYKLDAVITITPAGCDVFVGDLLYEPPRDGPTLWEIGIPDRSAAEFYSPDPNPTYVNKLFIGHPDRFRQYGLWERYAELYPDGDLV YTIGVSDYTKDWFFAQVTRKKDNNTYQGTTWQIKFTLDTVDQIGTYKLRVAIASATLSELQVRVNDPKANPPHFTSGLIGRDNTIARHGIHGLYWLYSVN VLGNLLVEGENTIFLTQPRSTSP |
Full Sequence |
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Protein Sequence Length: 657 Download |
MSPLGVQLYI QDRHVVMDNG ILQVTLSNPG GIVTGIRYSA IDNLLEVLND ETNRGYWDLV 60 WSVPGSAGIF DVIKGTNFRV IVENEEQVEI SFTRMWDPSL EGKLVPLNID KRFIMLRGSS 120 GFYSYAIYEH LKEWPAFTLA ETRIAFKLRK DNTVLKGKMK KHRLFHYMAM ADNRQRFMPL 180 PDDRLPGRGQ PLAYPEAVLL VNPVEPEFKG EVDDKYQYSC DNKDNRVHGW VCLEPPVGFW 240 QITPSDEFRT GGPVKQNLTS HVGPTTLAMF HSAHYAGEPL VPKFGPDEPW KKVFGPVFIY 300 VNSVFGDGDP FWLWEDAKEQ MTIEVQSWPY SFPASEDFPS SDQRGNVSGR LLVQDGYISD 360 DYILASCAYV GLAPPGDVGS WQRECKDYQF WTQADLGGYF CINDIRPGDY NLYAWVPGFI 420 GDYKLDAVIT ITPAGCDVFV GDLLYEPPRD GPTLWEIGIP DRSAAEFYSP DPNPTYVNKL 480 FIGHPDRFRQ YGLWERYAEL YPDGDLVYTI GVSDYTKDWF FAQVTRKKDN NTYQGTTWQI 540 KFTLDTVDQI GTYKLRVAIA SATLSELQVR VNDPKANPPH FTSGLIGRDN TIARHGIHGL 600 YWLYSVNVLG NLLVEGENTI FLTQPRSTSP FQGILYDYIR LEGPPSPNSN SSKKLA* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 7.0e-29 | 343 | 435 | 93 | + 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 | 455 | 642 | 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 | 2.0e-71 | 11 | 303 | 299 | + 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 | 7.0e-105 | 1 | 212 | 212 | + 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 | 656 | 1 | 656 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 17 | 656 | 1 | 627 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002285627.1 | 0 | 95 | 656 | 1 | 509 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 17 | 643 | 1 | 613 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 5 | 650 | 5 | 639 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DW479599 | 307 | 1 | 304 | 0 |
DW479600 | 311 | 1 | 308 | 0 |
DT552229 | 305 | 17 | 317 | 0 |
DY293973 | 362 | 1 | 355 | 0 |
GW864372 | 324 | 144 | 467 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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