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Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10008518m |
Family | PL4 |
Protein Properties | Length: 666 Molecular Weight: 76225.8 Isoelectric Point: 5.9262 |
Chromosome | Chromosome/Scaffold: 1 Start: 3280593 End: 3283777 |
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 | 26 | 641 | 0 |
LQLHYQDQHVVMDNGILQLTLSNPEGFVTGIRYNGIENVLATGKEYDRGYWDLVWNFPGKKTKKTKGTLDRIEATKMEVKTQNEDLIELSFSRTWNTSSS TAVPVNIDKRFVMLRNSSGFYSYAIFERLQGWPAVELDNIRLAIKLNKDKFHYMAISDDRQRYMPLPDDRIPPRGQPLAYPEAVKLLDPIEPEFKGEVDD KYEYSMESKDIKVHGWISTNDSVGFWQITPSNEFRSSGPLKQFLGSHVGPTNLAIFHSTHYVGAELIMNFKQGEAWKKVFGPVFIYLNSFPKGVDPLLLW HEAKNQTKIEEEKWPYKFIASDDFPASDQRGSVSGRLLVRDRFISSVDIPANGSYVGLAAPGDVGSWQRECKGYQFWSKAEENGYFSINNVRSGRYNLYA FAPGFIGDYHNDTIFDISPGSKINLGDLVYEPPRDGSTLWEIGVPDRTAAEFYIPDPNPSFVNHLYLNHSDKYRQYGLWERYSELYPSEDMVYNADVDDH SKQWFFMQVTRKQANGGYNGTTWQIRFQLDDKMKNLTGNFKLRIALATSNVAELQVRVNDLSANPPLFTTEQIGRDNTIARHGIHGLYWLYNVNVPDSSL RLGNNTIYLTQPLATS |
Full Sequence |
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Protein Sequence Length: 666 Download |
MFMSLFQIAI SQNQTPEPEP ESTKVLQLHY QDQHVVMDNG ILQLTLSNPE GFVTGIRYNG 60 IENVLATGKE YDRGYWDLVW NFPGKKTKKT KGTLDRIEAT KMEVKTQNED LIELSFSRTW 120 NTSSSTAVPV NIDKRFVMLR NSSGFYSYAI FERLQGWPAV ELDNIRLAIK LNKDKFHYMA 180 ISDDRQRYMP LPDDRIPPRG QPLAYPEAVK LLDPIEPEFK GEVDDKYEYS MESKDIKVHG 240 WISTNDSVGF WQITPSNEFR SSGPLKQFLG SHVGPTNLAI FHSTHYVGAE LIMNFKQGEA 300 WKKVFGPVFI YLNSFPKGVD PLLLWHEAKN QTKIEEEKWP YKFIASDDFP ASDQRGSVSG 360 RLLVRDRFIS SVDIPANGSY VGLAAPGDVG SWQRECKGYQ FWSKAEENGY FSINNVRSGR 420 YNLYAFAPGF IGDYHNDTIF DISPGSKINL GDLVYEPPRD GSTLWEIGVP DRTAAEFYIP 480 DPNPSFVNHL YLNHSDKYRQ YGLWERYSEL YPSEDMVYNA DVDDHSKQWF FMQVTRKQAN 540 GGYNGTTWQI RFQLDDKMKN LTGNFKLRIA LATSNVAELQ VRVNDLSANP PLFTTEQIGR 600 DNTIARHGIH GLYWLYNVNV PDSSLRLGNN TIYLTQPLAT SPFQGLMYDY IRLECPDSIN 660 YITRS* 720 |
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-33 | 354 | 453 | 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-48 | 465 | 654 | 192 | + 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 | 4.0e-68 | 31 | 314 | 286 | + 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-97 | 5 | 223 | 220 | + 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 |
RefSeq | NP_172459.1 | 0 | 37 | 665 | 1 | 631 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002527353.1 | 0 | 26 | 656 | 6 | 633 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527356.1 | 0 | 34 | 664 | 127 | 754 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527356.1 | 3.99931e-42 | 97 | 223 | 1 | 128 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 22 | 656 | 2 | 634 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FY443137 | 262 | 403 | 663 | 0 |
DK542563 | 214 | 450 | 663 | 0 |
DW479599 | 292 | 26 | 315 | 0 |
DK542563 | 25 | 425 | 449 | 0.0006 |
DK542563 | 12 | 415 | 426 | 0.0006 |
Sequence Alignments (This image is cropped. Click for full image.) |
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