y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.F00442.1 |
Family | PL4 |
Protein Properties | Length: 676 Molecular Weight: 76995.6 Isoelectric Point: 6.5521 |
Chromosome | Chromosome/Scaffold: 6 Start: 5608757 End: 5615389 |
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 | 49 | 660 | 0 |
GVHLHIRHNQVIMDNGIVQVTLSKPDGIVIGVRYNGVDNLLEICNQESNRGYWDLVWNAPGSKGIFDVIKGTCFNVIVENEEQVELSFVRTWDFSLEGKY VPLNIDKRFIMLRGSSGFYSYAIYDHLADWPSFEIGETRITFKLRKDKFHYMAIADDRQRKMPLPDDRLPGRCQTLAYPEAVLLVNPVDPELRGEVDDKY QYSCNNKDIQVHGWISSDPAIGFWQITPSDEFRSGGPLKQSLTSHVGPTTLAIFLSAHYAGKDLVPKFGPGEPWKKVFGPVFIYLNSASARDDPRFLWED AKIQMMNEVERWPYNFPASEDFPKSHQRGNVRGRLLVQDRYVSNDYISAKRAYVGLAPPGDAGSWQRECKGYQFWTQADNDGYFSINNVRSGDYNLYAWV PGFIGDYRHDNIITISSGLDHDMGDLVYEPPREGATLWEIGIPDRSAAEFYVPDPDASYINRLYVHHPDRFRQYGLWSRYGELYPEKDLVYTIGVSDHTK DWFFAQVPRRKQDGSHEGTTWQIKFNLSYVERSKSHKLRIAIASATLAELQVRVNDPKARRPLFTSGLIGRDNSIARHGIQGLYWLFNVNVPGTLLNEGE NTIFLTQPRCDS |
Full Sequence |
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Protein Sequence Length: 676 Download |
MGLCSSTRLK DQVSDPQRLQ GVPGHNRESH AGQHIHGNFA GQEAMSTPGV HLHIRHNQVI 60 MDNGIVQVTL SKPDGIVIGV RYNGVDNLLE ICNQESNRGY WDLVWNAPGS KGIFDVIKGT 120 CFNVIVENEE QVELSFVRTW DFSLEGKYVP LNIDKRFIML RGSSGFYSYA IYDHLADWPS 180 FEIGETRITF KLRKDKFHYM AIADDRQRKM PLPDDRLPGR CQTLAYPEAV LLVNPVDPEL 240 RGEVDDKYQY SCNNKDIQVH GWISSDPAIG FWQITPSDEF RSGGPLKQSL TSHVGPTTLA 300 IFLSAHYAGK DLVPKFGPGE PWKKVFGPVF IYLNSASARD DPRFLWEDAK IQMMNEVERW 360 PYNFPASEDF PKSHQRGNVR GRLLVQDRYV SNDYISAKRA YVGLAPPGDA GSWQRECKGY 420 QFWTQADNDG YFSINNVRSG DYNLYAWVPG FIGDYRHDNI ITISSGLDHD MGDLVYEPPR 480 EGATLWEIGI PDRSAAEFYV PDPDASYINR LYVHHPDRFR QYGLWSRYGE LYPEKDLVYT 540 IGVSDHTKDW FFAQVPRRKQ DGSHEGTTWQ IKFNLSYVER SKSHKLRIAI ASATLAELQV 600 RVNDPKARRP LFTSGLIGRD NSIARHGIQG LYWLFNVNVP GTLLNEGENT IFLTQPRCDS 660 PFQGLMYDYL RLEGP* 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 9.0e-35 | 375 | 474 | 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 | 2.0e-49 | 486 | 673 | 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-76 | 57 | 341 | 291 | + 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-104 | 44 | 244 | 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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI19298.1 | 0 | 45 | 675 | 1 | 644 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 61 | 675 | 1 | 615 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002306520.1 | 0 | 61 | 675 | 1 | 615 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 45 | 675 | 1 | 631 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527353.1 | 0 | 45 | 675 | 1 | 633 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY293973 | 358 | 37 | 388 | 0 |
GW864372 | 311 | 188 | 498 | 0 |
DW479599 | 294 | 45 | 335 | 0 |
DW479600 | 296 | 45 | 337 | 0 |
DT552229 | 293 | 61 | 349 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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