Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_010_00069.4 |
Family | PL4 |
Protein Properties | Length: 626 Molecular Weight: 70721.6 Isoelectric Point: 4.5392 |
Chromosome | Chromosome/Scaffold: 10 Start: 477795 End: 487266 |
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 | 1 | 607 | 0 |
MDNGILQVTLSNPGGLVTGIRFNGIDNLLEVRNEENNRGYWDLVWAEPGSTGTKGTFDLIQGTSFKVIVEDEDQVEISFTRSWEPSLQGKQVPLNTDIRF IMLRGCSGFYSYGIYEHLQDWPGFNMPNTRIAFKLNKDKFQYMAMADNRQRIMPMPDDRLQGHCQPLAYPEAVLLTNPINPDLKGEVDDKYQYSCESKDN RVHGWICTNPPVGLWQITPSSEFRTGGPVKQILTSHVGPTTLAMFVSAHYSGEDLVPKIQDKEPWKKVFGPVFIYLNWAMESDDPLSLWEDAKAQMAIEV ESWPYSFPASEDFPTTDERGSVSGTLLVKDPYIDEDYMSADSAYIGLALPGDAGSWQRESKGYQFWTRTDEDGNFTISDIRAGNYNLYAWVPGFIGDYKY DVDISITPGCDIDLGGIVYEPPRDGPTLWEIGIPDRSAAEFFVPDPDPKYINKVLVNKPDLRFRQYGLWDRYAELYPNTDLVYTVGVSDFRKDWFFAQVN RKKDSKTYQGTTWQIVFNLDEVDQSGTFKLRLALASATVAELQVRVNDPKANPPLFSSGVIGKDNSLARHGIHGLYWLYTVDVPGSLLVKGNNTIFLTQP RAATPWQ |
Full Sequence |
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Protein Sequence Length: 626 Download |
MDNGILQVTL SNPGGLVTGI RFNGIDNLLE VRNEENNRGY WDLVWAEPGS TGTKGTFDLI 60 QGTSFKVIVE DEDQVEISFT RSWEPSLQGK QVPLNTDIRF IMLRGCSGFY SYGIYEHLQD 120 WPGFNMPNTR IAFKLNKDKF QYMAMADNRQ RIMPMPDDRL QGHCQPLAYP EAVLLTNPIN 180 PDLKGEVDDK YQYSCESKDN RVHGWICTNP PVGLWQITPS SEFRTGGPVK QILTSHVGPT 240 TLAMFVSAHY SGEDLVPKIQ DKEPWKKVFG PVFIYLNWAM ESDDPLSLWE DAKAQMAIEV 300 ESWPYSFPAS EDFPTTDERG SVSGTLLVKD PYIDEDYMSA DSAYIGLALP GDAGSWQRES 360 KGYQFWTRTD EDGNFTISDI RAGNYNLYAW VPGFIGDYKY DVDISITPGC DIDLGGIVYE 420 PPRDGPTLWE IGIPDRSAAE FFVPDPDPKY INKVLVNKPD LRFRQYGLWD RYAELYPNTD 480 LVYTVGVSDF RKDWFFAQVN RKKDSKTYQG TTWQIVFNLD EVDQSGTFKL RLALASATVA 540 ELQVRVNDPK ANPPLFSSGV IGKDNSLARH GIHGLYWLYT VDVPGSLLVK GNNTIFLTQP 600 RAATPWQNIM YDYIRLEAPP PSPSK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.0008 | 357 | 394 | 38 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 6.0e-34 | 318 | 417 | 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 | 8.0e-56 | 429 | 617 | 191 | + 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 | 5.0e-67 | 1 | 288 | 291 | + 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 | 1.0e-88 | 1 | 187 | 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 |
EMBL | CBI19298.1 | 0 | 1 | 620 | 17 | 645 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 1 | 620 | 1 | 616 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 1 | 618 | 1 | 613 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002301114.1 | 0 | 1 | 625 | 17 | 637 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 622 | 17 | 636 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DT729214 | 263 | 55 | 317 | 0 |
GW864372 | 311 | 131 | 441 | 0 |
DR937930 | 227 | 394 | 620 | 0 |
DT552229 | 293 | 1 | 292 | 0 |
DT729214 | 32 | 319 | 350 | 0.00001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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