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Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma18g27090.4 |
Family | PL4 |
Protein Properties | Length: 636 Molecular Weight: 72413.5 Isoelectric Point: 5.4262 |
Chromosome | Chromosome/Scaffold: 18 Start: 31175206 End: 31183309 |
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 | 614 | 0 |
SNNREQLVVDNGIVAVTFSRPEGYILGISYNGIDNILEEENEDQDRGYLDVVWNTPGKPSNFQRIHGTIFSVIAADENMVELSFSKSWTSSLNGSSVPMN IDIRYILRSGDSGFYSYAIFDRPEGLPAVEIDQIRIVFKLNKDRFNYMAISDERQRSMPTMRDRETGQILAYPEAVLLTRPINPEFRGEVDDKYQYSCEN KVNTVHGWISVDAADAPPVGFWMITPSSEFRNAGPIKQDLTSHVGPITLSMFVSTHYAGKEVTMAFQEGEIYKKVFGPVFAYVNNASNEDDTLSLWSDAV QQQSKEVRSWPYDFPKSVDFIPPNQRGIVLGRLLVQDRYFRGGRLLYANNSYVGLALPGDEGSWQIESKGYQFWTQADTKGFFLINNVVPGDYNLYAWVP GFIGDYRYNATITITPGGVIRLDSLVYVPPRNGPTIWEIGFPDRKAAEFYVPEPYPTLMNKLYNEQRRDKFRQYGLWERYTDLYPNDDLVYTVGISKYRK DWFFAHVTRSTGNKTYQPTTWQIIFEHPNQIIRGNYTLQLALACTADADLQVRVNDPSANPPDFATGKIGGDSAIARHGVHGLYRLFSINVPSDRFVKGT NTIYLRQSRAM |
Full Sequence |
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Protein Sequence Length: 636 Download |
MVNSNNREQL VVDNGIVAVT FSRPEGYILG ISYNGIDNIL EEENEDQDRG YLDVVWNTPG 60 KPSNFQRIHG TIFSVIAADE NMVELSFSKS WTSSLNGSSV PMNIDIRYIL RSGDSGFYSY 120 AIFDRPEGLP AVEIDQIRIV FKLNKDRFNY MAISDERQRS MPTMRDRETG QILAYPEAVL 180 LTRPINPEFR GEVDDKYQYS CENKVNTVHG WISVDAADAP PVGFWMITPS SEFRNAGPIK 240 QDLTSHVGPI TLSMFVSTHY AGKEVTMAFQ EGEIYKKVFG PVFAYVNNAS NEDDTLSLWS 300 DAVQQQSKEV RSWPYDFPKS VDFIPPNQRG IVLGRLLVQD RYFRGGRLLY ANNSYVGLAL 360 PGDEGSWQIE SKGYQFWTQA DTKGFFLINN VVPGDYNLYA WVPGFIGDYR YNATITITPG 420 GVIRLDSLVY VPPRNGPTIW EIGFPDRKAA EFYVPEPYPT LMNKLYNEQR RDKFRQYGLW 480 ERYTDLYPND DLVYTVGISK YRKDWFFAHV TRSTGNKTYQ PTTWQIIFEH PNQIIRGNYT 540 LQLALACTAD ADLQVRVNDP SANPPDFATG KIGGDSAIAR HGVHGLYRLF SINVPSDRFV 600 KGTNTIYLRQ SRAMNPFQGV MYDYIRLERP PLTQI* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.008 | 378 | 426 | 49 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 2.0e-29 | 328 | 428 | 101 | + 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 | 9.0e-48 | 440 | 628 | 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 | 3.0e-73 | 9 | 295 | 293 | + 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 | 3.0e-78 | 9 | 193 | 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 |
GenBank | AAS99719.1 | 0 | 8 | 630 | 60 | 674 | At2g22620 [Arabidopsis thaliana] |
RefSeq | NP_179847.1 | 0 | 8 | 630 | 60 | 674 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002308510.1 | 0 | 2 | 630 | 49 | 671 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002319997.1 | 0 | 10 | 633 | 1 | 620 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527245.1 | 0 | 10 | 633 | 2 | 621 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY969340 | 323 | 225 | 547 | 0 |
EG984401 | 232 | 121 | 347 | 0 |
GW864372 | 316 | 139 | 452 | 0 |
GO374104 | 313 | 322 | 630 | 0 |
EH792178 | 287 | 302 | 587 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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