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Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.005G151500.1 |
Family | PL4 |
Protein Properties | Length: 646 Molecular Weight: 73539 Isoelectric Point: 5.3098 |
Chromosome | Chromosome/Scaffold: 05 Start: 14236506 End: 14247924 |
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 | 5 | 616 | 0 |
AVRLYIQDHHVVMDNGIVQVTLSKPAGIVTGIRYDGIDNLLEVLNRETNRGYWDLHWNPPGGNGIFDVISGTSFRVVVENDEQVELSFTRMWDSSLEGKY IPLNIDKRFILLRGSSGFYSYAIYEHLQEWPGFDIGETRITFKLRKDKFQYMAIADNRQRLMPLPDDRLPGRCQALAYPEAVILVNPKLPELTGEVDDKY QYSCENKDNQVHGWICFKPPVGFWQITPSDEFRTAGPLKQNLTSHVGPTTLAMFHSSHYAGKDLVLSISPGEPWKKVFGPVFIYLNSASNGEDPLFLWED AKMQMMAEVQSWPYSFPASEDFQKSEQRGNVCGRLLVKDRNISDDYILASGAYVGLAPPGDVGSWQTECKDYQFWTRADENGYFSIKNIRTGDYNLYAWV PGFLGDYRWDAIVNIISGCDMDMGDLVYEPPRDGPTLWEIGIPDRSAAEFYIPGPDPKFMNNLYANHPDRFRQYGLWGRYADLYPDTDLVYTVGLSDYRK DWFFAQVVRRKDDDTQVGTTWQIKFKLDKVDRNSSYKLRVAIASATLAELQVRVNDAKAQRPLFTSGLIGRDNAIARHGIHGLYRLYNVNIPGARLVEGE NTIFLTQPRCTS |
Full Sequence |
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Protein Sequence Length: 646 Download |
MPFQAVRLYI QDHHVVMDNG IVQVTLSKPA GIVTGIRYDG IDNLLEVLNR ETNRGYWDLH 60 WNPPGGNGIF DVISGTSFRV VVENDEQVEL SFTRMWDSSL EGKYIPLNID KRFILLRGSS 120 GFYSYAIYEH LQEWPGFDIG ETRITFKLRK DKFQYMAIAD NRQRLMPLPD DRLPGRCQAL 180 AYPEAVILVN PKLPELTGEV DDKYQYSCEN KDNQVHGWIC FKPPVGFWQI TPSDEFRTAG 240 PLKQNLTSHV GPTTLAMFHS SHYAGKDLVL SISPGEPWKK VFGPVFIYLN SASNGEDPLF 300 LWEDAKMQMM AEVQSWPYSF PASEDFQKSE QRGNVCGRLL VKDRNISDDY ILASGAYVGL 360 APPGDVGSWQ TECKDYQFWT RADENGYFSI KNIRTGDYNL YAWVPGFLGD YRWDAIVNII 420 SGCDMDMGDL VYEPPRDGPT LWEIGIPDRS AAEFYIPGPD PKFMNNLYAN HPDRFRQYGL 480 WGRYADLYPD TDLVYTVGLS DYRKDWFFAQ VVRRKDDDTQ VGTTWQIKFK LDKVDRNSSY 540 KLRVAIASAT LAELQVRVND AKAQRPLFTS GLIGRDNAIA RHGIHGLYRL YNVNIPGARL 600 VEGENTIFLT QPRCTSPFQG LMYDYIRLEG PPFSGSSNEA SSSFK* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 8.0e-31 | 331 | 430 | 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 | 4.0e-55 | 442 | 629 | 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 | 1.0e-78 | 14 | 293 | 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 | 4.0e-99 | 7 | 200 | 194 | + 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 | 5 | 638 | 5 | 651 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 17 | 638 | 1 | 622 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002306520.1 | 0 | 17 | 645 | 1 | 629 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 1 | 631 | 1 | 631 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527353.1 | 0 | 1 | 635 | 1 | 637 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CN523243 | 251 | 315 | 565 | 0 |
GW864372 | 311 | 144 | 454 | 0 |
DW479599 | 294 | 1 | 291 | 0 |
DW479600 | 298 | 1 | 295 | 0 |
DY293973 | 345 | 6 | 344 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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