Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.F00438.1 |
Family | PL4 |
Protein Properties | Length: 686 Molecular Weight: 77521.4 Isoelectric Point: 4.9045 |
Chromosome | Chromosome/Scaffold: 6 Start: 5577991 End: 5583371 |
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 | 31 | 643 | 0 |
RVQLNVQDKQVVIDNGMVQVTIAKPEGFVTGIKYNGIGNLLEVLNEEWDRGYWDLVWSEAGSAGTTGTDDRMNATKFNVIVENEEQVEISFTRMWDSSMA GQMVPLNIDKRFVMLRNCSGFYSYGIYEHSGDWPAFNLPQTRIVFKLRKDKFNYMAVGDNRRRHMPLPDDRSPRRGQPLATPEAVLLVDPVEPEFKGEVD DKYQYSCENKDLQVHGWICFDPPVGFWQITPSNEFRSGGLLKQNLTSHVGPITLAMFLSAHYGGDDLVLKLAPGEPWKKIFGPVFFYLNCTSENPLKLWD DAKEQMLSEVQGWPYAFPASAEYQILDQRGYVNGRLMIRDKYISDTLIPAAGAYVGLAPPGEIGSWQTEVKGYQFWTKADSDGYFSINNVRTGDYNIYAW VPCYVGDYRNDEVITITLGCQVDVGDLVFEPPRNGPTLWEIGVPDRSAAEFYVPDPNPKYINRLYLNHPDKFRQYGLWERYTELYPDSDLIYTVGASDYT KDWFFAQVPRKIDDSTYKGTTWQIKFKLDDARPSETYKLRLALATANVAQLEVRVNSPQANPPLFSSGVIGHDNTIARHGIHGLYRSYVVDVPGAQLVVG DNTVFLSQTMSTS |
Full Sequence |
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Protein Sequence Length: 686 Download |
MIRAMMENQN ASVAQEGGKM GSDGYTAPSL RVQLNVQDKQ VVIDNGMVQV TIAKPEGFVT 60 GIKYNGIGNL LEVLNEEWDR GYWDLVWSEA GSAGTTGTDD RMNATKFNVI VENEEQVEIS 120 FTRMWDSSMA GQMVPLNIDK RFVMLRNCSG FYSYGIYEHS GDWPAFNLPQ TRIVFKLRKD 180 KFNYMAVGDN RRRHMPLPDD RSPRRGQPLA TPEAVLLVDP VEPEFKGEVD DKYQYSCENK 240 DLQVHGWICF DPPVGFWQIT PSNEFRSGGL LKQNLTSHVG PITLAMFLSA HYGGDDLVLK 300 LAPGEPWKKI FGPVFFYLNC TSENPLKLWD DAKEQMLSEV QGWPYAFPAS AEYQILDQRG 360 YVNGRLMIRD KYISDTLIPA AGAYVGLAPP GEIGSWQTEV KGYQFWTKAD SDGYFSINNV 420 RTGDYNIYAW VPCYVGDYRN DEVITITLGC QVDVGDLVFE PPRNGPTLWE IGVPDRSAAE 480 FYVPDPNPKY INRLYLNHPD KFRQYGLWER YTELYPDSDL IYTVGASDYT KDWFFAQVPR 540 KIDDSTYKGT TWQIKFKLDD ARPSETYKLR LALATANVAQ LEVRVNSPQA NPPLFSSGVI 600 GHDNTIARHG IHGLYRSYVV DVPGAQLVVG DNTVFLSQTM STSPLQGVMY DYIRFEGPPS 660 PNDKKDAKSW TCSRNSYVLD NNVHI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 4.0e-28 | 358 | 457 | 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-50 | 469 | 656 | 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 | 9.0e-70 | 36 | 322 | 290 | + 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-84 | 33 | 229 | 197 | + 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 | 30 | 668 | 4 | 654 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 43 | 668 | 1 | 625 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301114.1 | 0 | 31 | 665 | 5 | 638 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 28 | 660 | 2 | 635 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 32 | 660 | 6 | 636 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FY792769 | 270 | 360 | 629 | 0 |
FY793067 | 260 | 1 | 260 | 0 |
DY293973 | 345 | 32 | 371 | 0 |
DW479599 | 301 | 20 | 320 | 0 |
DW479600 | 301 | 23 | 323 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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