y
Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi3g42610.1 |
Family | PL4 |
Protein Properties | Length: 634 Molecular Weight: 72646.5 Isoelectric Point: 4.8495 |
Chromosome | Chromosome/Scaffold: 3 Start: 44109240 End: 44112797 |
Description | Rhamnogalacturonate lyase family protein |
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 | 4 | 616 | 0 |
VKVKVTDRYVEIKNGIFGLTLSNPDGIVTGVRYNGVDNLMEILNKEDNRGYWDVVWNPPGQRTGIFDVIKGTEFRIIYHDDNQAEVSFTRSWDPSLEGKA VPLIIDKRFIVLRGSSGFYTYGIYEHKEGWPDFGLGETRVAFKLRKDKFHYMAMADNRQRIMPMPDDRLPPRGQPLAYPEAVLLVDPINPELKGEVDDKY QYSCEDQYNNVHGWISSDPPIGFWQITPSDEFRTGGPLKQNLTSHVGPTMLAMFLSAHYAGDDLSPKFTNGEYWKKVHGPVFLYLNSSWDGSDPSLLWED AKVQTVIEKESWPYSFALSEDFQKTEQRGCVSGRLLVRDRYIDAEDLYATSAYVGLALPGEAGSWQRECKGYQFWCRADADGSFYIRNIVTGNYNLYAWV PGFIGDYKFSATLTISSGDDIYLGDLVYEPPRDGPTMWEIGIPDRSAAEFYVPDPNPNYVNRLFINHPDRFRQYGLWERYAELYPDRDLVYTIGESDYRT DWFYAQVTRRTDENTYQPTTWQIRFDLDNVPPNSTYKFRVALASSAIAELQIRFNDQDRGAPHFSSGLIGRDNTIARHGIHGLYWLFTVDVSGAWLVQGM NTVYLKQPRSQSP |
Full Sequence |
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Protein Sequence Length: 634 Download |
MDVVKVKVTD RYVEIKNGIF GLTLSNPDGI VTGVRYNGVD NLMEILNKED NRGYWDVVWN 60 PPGQRTGIFD VIKGTEFRII YHDDNQAEVS FTRSWDPSLE GKAVPLIIDK RFIVLRGSSG 120 FYTYGIYEHK EGWPDFGLGE TRVAFKLRKD KFHYMAMADN RQRIMPMPDD RLPPRGQPLA 180 YPEAVLLVDP INPELKGEVD DKYQYSCEDQ YNNVHGWISS DPPIGFWQIT PSDEFRTGGP 240 LKQNLTSHVG PTMLAMFLSA HYAGDDLSPK FTNGEYWKKV HGPVFLYLNS SWDGSDPSLL 300 WEDAKVQTVI EKESWPYSFA LSEDFQKTEQ RGCVSGRLLV RDRYIDAEDL YATSAYVGLA 360 LPGEAGSWQR ECKGYQFWCR ADADGSFYIR NIVTGNYNLY AWVPGFIGDY KFSATLTISS 420 GDDIYLGDLV YEPPRDGPTM WEIGIPDRSA AEFYVPDPNP NYVNRLFINH PDRFRQYGLW 480 ERYAELYPDR DLVYTIGESD YRTDWFYAQV TRRTDENTYQ PTTWQIRFDL DNVPPNSTYK 540 FRVALASSAI AELQIRFNDQ DRGAPHFSSG LIGRDNTIAR HGIHGLYWLF TVDVSGAWLV 600 QGMNTVYLKQ PRSQSPFQGL MYDYLRLEGP CGC* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 2.0e-31 | 330 | 429 | 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-55 | 441 | 628 | 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-71 | 4 | 299 | 301 | + 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 | 5.0e-98 | 7 | 199 | 193 | + 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 | 4 | 632 | 16 | 644 | putative MYST1 [Oryza sativa Japonica Group] |
GenBank | EEE69123.1 | 0 | 4 | 628 | 675 | 1299 | hypothetical protein OsJ_28233 [Oryza sativa Japonica Group] |
RefSeq | NP_001062464.1 | 0 | 4 | 632 | 29 | 657 | Os08g0554100 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001062465.1 | 0 | 4 | 633 | 17 | 606 | Os08g0554300 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002445711.1 | 0 | 4 | 633 | 33 | 663 | hypothetical protein SORBIDRAFT_07g024560 [Sorghum bicolor] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GO850432 | 281 | 1 | 281 | 0 |
GO843311 | 290 | 1 | 290 | 0 |
GO843500 | 255 | 380 | 634 | 0 |
FE632882 | 246 | 91 | 336 | 0 |
GO850432 | 25 | 282 | 306 | 3.8 |
Sequence Alignments (This image is cropped. Click for full image.) |
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