Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.010G032900.2 |
Family | PL4 |
Protein Properties | Length: 635 Molecular Weight: 71976.8 Isoelectric Point: 4.8098 |
Chromosome | Chromosome/Scaffold: 10 Start: 2951786 End: 2958614 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 1 | 606 | 0 |
MIDNGLLQLTLLNPDGIVTGIRYNGIDNLLEVLNGEDNRGYWDLVWNSPGTPGTTGSFDVIKGTSFKVIVENEDQVEVSFTRTWDSSQEGKLVPLNIDKR FIVLRGCSGFYTYAIYEHLKDWPGFNLAETRIAFKLRKDKFHYMAMADNRQRYMPLPDDRLSGRGQALAYPEAVLLVNPVEPDFKGEVDDKYQYSCDNKD SQVHGWICTTDQPAVGFWMVTPSNEFRSGGPVKQNLTSHVGPTTLAVFLSAHYTGEDLVPKFSAGEAWKKVFGPVFIYLNCTMDGDEPLSLWEDAKQQMI IEVQSWPYTFPASDDFPKSNQRGNVNGRLLVNDRYASDDNIPANGAYIGLVPPGNVGSWQRECKDYQFWTKTDINGYFLINDIRPGDYNLYAWVPGFIGD YQYSAAITITPGSEIEVGDLVYKPPRNGPTLWEIGIPDRSAAEFYVPDPNPKYINKVYVNHPDRFRQYGLWERYAELYPNEDLVYTVGTSDYKKDWFFAQ VTRKIDTNKYQGTTWQIRFKLDNVDQGSSYKLRVAIASATFSELQVQINDPKTNPLFSSGLIGRDNSIARHGIHGLYWLYNVDVPGKLLVQGDNTIFLTQ PRSSSP |
Full Sequence |
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Protein Sequence Length: 635 Download |
MIDNGLLQLT LLNPDGIVTG IRYNGIDNLL EVLNGEDNRG YWDLVWNSPG TPGTTGSFDV 60 IKGTSFKVIV ENEDQVEVSF TRTWDSSQEG KLVPLNIDKR FIVLRGCSGF YTYAIYEHLK 120 DWPGFNLAET RIAFKLRKDK FHYMAMADNR QRYMPLPDDR LSGRGQALAY PEAVLLVNPV 180 EPDFKGEVDD KYQYSCDNKD SQVHGWICTT DQPAVGFWMV TPSNEFRSGG PVKQNLTSHV 240 GPTTLAVFLS AHYTGEDLVP KFSAGEAWKK VFGPVFIYLN CTMDGDEPLS LWEDAKQQMI 300 IEVQSWPYTF PASDDFPKSN QRGNVNGRLL VNDRYASDDN IPANGAYIGL VPPGNVGSWQ 360 RECKDYQFWT KTDINGYFLI NDIRPGDYNL YAWVPGFIGD YQYSAAITIT PGSEIEVGDL 420 VYKPPRNGPT LWEIGIPDRS AAEFYVPDPN PKYINKVYVN HPDRFRQYGL WERYAELYPN 480 EDLVYTVGTS DYKKDWFFAQ VTRKIDTNKY QGTTWQIRFK LDNVDQGSSY KLRVAIASAT 540 FSELQVQIND PKTNPLFSSG LIGRDNSIAR HGIHGLYWLY NVDVPGKLLV QGDNTIFLTQ 600 PRSSSPFQGI MYDYIRLEGP SKLSSNEEYM SSTL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.001 | 370 | 417 | 48 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 4.0e-30 | 321 | 420 | 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 | 1.0e-56 | 432 | 618 | 189 | + 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-73 | 1 | 291 | 294 | + 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 | 1 | 188 | 188 | + 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 | 626 | 16 | 650 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_172460.6 | 0 | 2 | 621 | 1 | 617 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002285626.1 | 0 | 2 | 626 | 1 | 621 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 2 | 619 | 1 | 613 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 627 | 16 | 640 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DT552229 | 295 | 2 | 295 | 0 |
DW479600 | 283 | 3 | 285 | 0 |
DW479599 | 281 | 1 | 281 | 0 |
GW864372 | 313 | 132 | 444 | 0 |
DT729214 | 265 | 56 | 320 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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