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Basic Information | |
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Species | Arabidopsis thaliana |
Cazyme ID | AT4G24430.1 |
Family | PL4 |
Protein Properties | Length: 647 Molecular Weight: 73608.8 Isoelectric Point: 4.8207 |
Chromosome | Chromosome/Scaffold: 4 Start: 12630018 End: 12633075 |
Description | rhamnogalacturonate lyase, putative, expressed |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 6 | 624 | 0 |
SVQLDVQESHVVMGNGKVKVTISKPDGFVTGISYQGVDNLLETHNEDFNRGYWDLVWSDEGTPGTTGKSERIKGTSFEVVVENEELVEISFSRKWDSSLQ DSIAPINVDKRFIMRKDVTGFYSYAIFEHLAEWPAFNLPQTRIVYKLRKDKFKYMAIADNRQRKMPLPEDRLGKRGRPLAYPEAVLLVHPVEDEFKGEVD DKYEYSSENKDLKVHGWISHNLDLGCWQIIPSNEFRSGGLSKQNLTSHVGPISLAMFLSAHYAGEDMVMKVKAGDSWKKVFGPVFTYLNCLPDKTSDPLS LWQDAKNQMLTEVQSWPYDFPASEDFPVSDKRGCISGRLLVCDKFLSDDFLPANGAFVGLAPPGEVGSWQLESKGYQFWTEADSDGYFAINDIREGEYNL NGYVTGWIGDYQYEQLINITAGCDIDVGNIVYEPPRDGPTVWEIGIPDRSAAEFFVPDPNPKYINKLYIGHPDRFRQYGLWERYTELYPKEDLVFTIGVS DYKKDWFFAHVTRKMGDDTYQKTTWQIKFKLENVQKSCTYKIRIALATANVAELQVRMNDDDTEKTTPIFTTGVIGHDNAIARHGIHGIYRLYNVDVPSE KLVEGDNTLFLTQTMTTTG |
Full Sequence |
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Protein Sequence Length: 647 Download |
MSNQDSVQLD VQESHVVMGN GKVKVTISKP DGFVTGISYQ GVDNLLETHN EDFNRGYWDL 60 VWSDEGTPGT TGKSERIKGT SFEVVVENEE LVEISFSRKW DSSLQDSIAP INVDKRFIMR 120 KDVTGFYSYA IFEHLAEWPA FNLPQTRIVY KLRKDKFKYM AIADNRQRKM PLPEDRLGKR 180 GRPLAYPEAV LLVHPVEDEF KGEVDDKYEY SSENKDLKVH GWISHNLDLG CWQIIPSNEF 240 RSGGLSKQNL TSHVGPISLA MFLSAHYAGE DMVMKVKAGD SWKKVFGPVF TYLNCLPDKT 300 SDPLSLWQDA KNQMLTEVQS WPYDFPASED FPVSDKRGCI SGRLLVCDKF LSDDFLPANG 360 AFVGLAPPGE VGSWQLESKG YQFWTEADSD GYFAINDIRE GEYNLNGYVT GWIGDYQYEQ 420 LINITAGCDI DVGNIVYEPP RDGPTVWEIG IPDRSAAEFF VPDPNPKYIN KLYIGHPDRF 480 RQYGLWERYT ELYPKEDLVF TIGVSDYKKD WFFAHVTRKM GDDTYQKTTW QIKFKLENVQ 540 KSCTYKIRIA LATANVAELQ VRMNDDDTEK TTPIFTTGVI GHDNAIARHG IHGIYRLYNV 600 DVPSEKLVEG DNTLFLTQTM TTTGAFNGLM YDYIRLEGPP LDSYSH* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 6.0e-31 | 336 | 435 | 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 | 6.0e-46 | 447 | 637 | 193 | + 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 | 14 | 295 | 285 | + 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-90 | 3 | 204 | 202 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0005886 | plasma membrane |
GO:0008150 | biological_process |
GO:0016829 | lyase activity |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAL15345.1 | 0 | 160 | 646 | 1 | 487 | AT4g24430/T22A6_260 [Arabidopsis thaliana] |
GenBank | AAU90065.1 | 0 | 160 | 646 | 1 | 487 | At4g24430 [Arabidopsis thaliana] |
RefSeq | NP_567703.4 | 0 | 1 | 646 | 1 | 646 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002527353.1 | 0 | 7 | 640 | 6 | 634 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 7 | 640 | 6 | 635 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CD813831 | 254 | 2 | 255 | 0 |
FD941014 | 256 | 388 | 643 | 0 |
DY293973 | 327 | 7 | 331 | 0 |
FY792769 | 271 | 338 | 608 | 0 |
BP562256 | 186 | 131 | 316 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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