y
Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si013400m |
Family | PL4 |
Protein Properties | Length: 643 Molecular Weight: 73213.1 Isoelectric Point: 4.6819 |
Chromosome | Chromosome/Scaffold: 6 Start: 35479014 End: 35482704 |
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 | 21 | 625 | 0 |
KVEIKNGIFELTLSNPDGIVTGVRYNGVDNLMEILNKEDNRGYWDLVWNPPGQKTGIFDVIKGTEFRIIYHDENQAEVSFTRNWDPSLEGKAVPLNIDKR FIVLRGSSGFYTYGIYEHKEGWPDFGLGETRVAFKLRKDKFHYMALADNRQRIMPMPDDRLPPRGQPLAYPEAVLLVDPINPDLRGEVDDKYQYSCEDQC NNVHGWMSFDPPIGFWQITPSDEFRTGGPLKQNLTSHVGPTTLAMFLSAHYAGDDLSPVFTNGEYWKKVHGPVFMYLNSSWDGSDPTMLWEDAKVQMMIE KESWPYSFALSEDFQKTEQRGCISGRLLVRDRYIDDEDLYASGAYVGLALPGEVGSWQRECKGYQFWCRADVDGSFYIRSIVTGNYNLYAWVPGFIGDYR LDATLTIASGDDIYLGDLVYEPPRDGPTMWEIGVPDRSAAEFYVPDPNPNYINRLYINHPDRFRQYGLWERYAELYPDSDLVYTIGQSDYSTDWFYAQVN RKVDDNTYQPTTWQIKFTLDSVSPGSTYKFRVALASSARAELQVFFNDQNRGVPHFATGLIGRDNAIARHGIHGLYWLFNINVDSAWLVQGMNTIYLKQP RNQSP |
Full Sequence |
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Protein Sequence Length: 643 Download |
MGPPSPAGAG AVDATDGVRV KVEIKNGIFE LTLSNPDGIV TGVRYNGVDN LMEILNKEDN 60 RGYWDLVWNP PGQKTGIFDV IKGTEFRIIY HDENQAEVSF TRNWDPSLEG KAVPLNIDKR 120 FIVLRGSSGF YTYGIYEHKE GWPDFGLGET RVAFKLRKDK FHYMALADNR QRIMPMPDDR 180 LPPRGQPLAY PEAVLLVDPI NPDLRGEVDD KYQYSCEDQC NNVHGWMSFD PPIGFWQITP 240 SDEFRTGGPL KQNLTSHVGP TTLAMFLSAH YAGDDLSPVF TNGEYWKKVH GPVFMYLNSS 300 WDGSDPTMLW EDAKVQMMIE KESWPYSFAL SEDFQKTEQR GCISGRLLVR DRYIDDEDLY 360 ASGAYVGLAL PGEVGSWQRE CKGYQFWCRA DVDGSFYIRS IVTGNYNLYA WVPGFIGDYR 420 LDATLTIASG DDIYLGDLVY EPPRDGPTMW EIGVPDRSAA EFYVPDPNPN YINRLYINHP 480 DRFRQYGLWE RYAELYPDSD LVYTIGQSDY STDWFYAQVN RKVDDNTYQP TTWQIKFTLD 540 SVSPGSTYKF RVALASSARA ELQVFFNDQN RGVPHFATGL IGRDNAIARH GIHGLYWLFN 600 INVDSAWLVQ GMNTIYLKQP RNQSPFQGLM YDYLRLEGPC GC* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 3.0e-29 | 339 | 438 | 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 | 5.0e-56 | 450 | 637 | 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-69 | 24 | 300 | 282 | + 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 | 4.0e-99 | 22 | 208 | 187 | + 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 |
DDBJ | BAD10227.1 | 0 | 3 | 642 | 4 | 645 | putative MYST1 [Oryza sativa Japonica Group] |
GenBank | EEE69123.1 | 0 | 3 | 637 | 663 | 1299 | hypothetical protein OsJ_28233 [Oryza sativa Japonica Group] |
RefSeq | NP_001062464.1 | 0 | 3 | 641 | 17 | 657 | Os08g0554100 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001062465.1 | 0 | 1 | 642 | 1 | 606 | Os08g0554300 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002445711.1 | 0 | 1 | 642 | 14 | 663 | hypothetical protein SORBIDRAFT_07g024560 [Sorghum bicolor] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GO843311 | 278 | 22 | 299 | 0 |
GO850432 | 269 | 22 | 290 | 0 |
FE632882 | 246 | 100 | 345 | 0 |
GO843500 | 255 | 389 | 643 | 0 |
GO850432 | 25 | 291 | 315 | 1.5 |
Sequence Alignments (This image is cropped. Click for full image.) |
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