Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 879190 |
Family | PL4 |
Protein Properties | Length: 665 Molecular Weight: 76174.5 Isoelectric Point: 5.4107 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 23 | 640 | 0 |
VLQLHYQDQHVVVENGIFQLTLSNPEGFVTGIRYNGIENVLAYTGKEYDRGYWDLVWNFPGKKAKKTKGTLDRIEATKMEVITQNDEQIELSFTRTWNTS STTAVPVNIDKRFVMLRNSSGFYSYAIFERLQGWPAVELDNMRLVFKLNKDKFHYMAISDDRQRYMPLPDDRIPPRGQPLAYPEAVQLLDPIEPEFKGEV DDKYEYSMESKDIKVHGWISTNDSVGFWQITPSNEFRSAGPLKQFLGSHVGPTNLAIFHSTHYVGAELIMSFKNGEAWKKVFGPVFIYLNSFPKGVDPLL LWHEAKNQTKIEEEKWPYNFTASDDFPESDQRGSVSGRLVVRDRFISSEDIPANGSYVGLAAPGDVGSWQRECKGYQFWSKADENGYFSINNVRSGRYHL YAFAPGFIGDYHNDTVFDISPGSKISLGDLVYEPPRDGSTLWEIGVPDRSAAEFYIPDPNPSFVNKLYLNHSDKFRQYGLWERYSELYPDEDMVYNVDAD DYSKKWFFMQVTRKHANGGYNGTTWQIRFQFDDKMKNLTGNFKLRIALATSNVAELQVRVNDLSADPPLFTTGQIGRDNTIARHGIHGLYWLYNVNVPAA SLHLGNNTIYLTQPLATS |
Full Sequence |
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Protein Sequence Length: 665 Download |
MFISVFEIAF CQNQTPEPES TQVLQLHYQD QHVVVENGIF QLTLSNPEGF VTGIRYNGIE 60 NVLAYTGKEY DRGYWDLVWN FPGKKAKKTK GTLDRIEATK MEVITQNDEQ IELSFTRTWN 120 TSSTTAVPVN IDKRFVMLRN SSGFYSYAIF ERLQGWPAVE LDNMRLVFKL NKDKFHYMAI 180 SDDRQRYMPL PDDRIPPRGQ PLAYPEAVQL LDPIEPEFKG EVDDKYEYSM ESKDIKVHGW 240 ISTNDSVGFW QITPSNEFRS AGPLKQFLGS HVGPTNLAIF HSTHYVGAEL IMSFKNGEAW 300 KKVFGPVFIY LNSFPKGVDP LLLWHEAKNQ TKIEEEKWPY NFTASDDFPE SDQRGSVSGR 360 LVVRDRFISS EDIPANGSYV GLAAPGDVGS WQRECKGYQF WSKADENGYF SINNVRSGRY 420 HLYAFAPGFI GDYHNDTVFD ISPGSKISLG DLVYEPPRDG STLWEIGVPD RSAAEFYIPD 480 PNPSFVNKLY LNHSDKFRQY GLWERYSELY PDEDMVYNVD ADDYSKKWFF MQVTRKHANG 540 GYNGTTWQIR FQFDDKMKNL TGNFKLRIAL ATSNVAELQV RVNDLSADPP LFTTGQIGRD 600 NTIARHGIHG LYWLYNVNVP AASLHLGNNT IYLTQPLATS PFQGLMYDYI RLEYPDSINY 660 ITKS* |
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-32 | 353 | 452 | 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 | 464 | 653 | 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 | 8.0e-71 | 29 | 313 | 287 | + 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-105 | 25 | 222 | 198 | + 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 | 35 | 664 | 1 | 631 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002527353.1 | 0 | 22 | 655 | 4 | 633 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527356.1 | 0 | 32 | 663 | 127 | 754 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527356.1 | 7.00649e-44 | 96 | 222 | 1 | 128 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 20 | 655 | 2 | 634 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FY443137 | 262 | 402 | 662 | 0 |
DW479599 | 295 | 21 | 314 | 0 |
DW479600 | 295 | 21 | 314 | 0 |
EX058229 | 224 | 28 | 251 | 0 |
DT552229 | 295 | 35 | 327 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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