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Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma04g09680.1 |
Family | PL4 |
Protein Properties | Length: 628 Molecular Weight: 71888.9 Isoelectric Point: 5.1357 |
Chromosome | Chromosome/Scaffold: 04 Start: 7955340 End: 7961008 |
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 | 1 | 610 | 0 |
MDNGIVQVNLSNPEGIVTGIQYNGIDNLLEVLNDESNRGYWDIVWDEGGKKRTKKGAKGKGRFDRMEATNFTVIVESEEQVELSFSRTWNDSLEGKLPPL NIDKRFIMLSGSSGFYTYAIYEHLKEWPAFDLDNTRIAFKPRKDKFHYMVVADNRQRFMPLPDDRSPPRGQVLAYPEAVRLVDPLEPEFKGEVDDKYQYA CESRYNRVHGWICIDPVNSTGFWLITPSYEFRSAGPLKQYLTSHVGPTTLSVFHSTHYSGADLIMQFGPNEPWKKVYGPIFIYLNSLSNGFSPIGLWEDA KQQMVNEVESWPYTFPASEDFLSSDQRGKVEGRLLVRDRYISDAFIPVSGAYVGLAAIGEVGSWQRECKGYQFWTITDDKGYFSIINIRPGGYNLYSWVN GFIGDYQFDSVIYVTSGCETNVGELVYEAPRDGPTLWEIGIPDRSAAEFYVPDPNPMCINRLYVNHPDRFRQYGLWERYAELYPNEDLVYTVGISDYRKD WFFAQVNRKKDNGTYIGTTWQINFKLDSVNTNGTYTLQVALASVHSAELEIRINNLEANPPLFSSGVIGKENTIARHGIHGLYWLFSIHIQGTLLVQGNN TIFLTQTRDT |
Full Sequence |
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Protein Sequence Length: 628 Download |
MDNGIVQVNL SNPEGIVTGI QYNGIDNLLE VLNDESNRGY WDIVWDEGGK KRTKKGAKGK 60 GRFDRMEATN FTVIVESEEQ VELSFSRTWN DSLEGKLPPL NIDKRFIMLS GSSGFYTYAI 120 YEHLKEWPAF DLDNTRIAFK PRKDKFHYMV VADNRQRFMP LPDDRSPPRG QVLAYPEAVR 180 LVDPLEPEFK GEVDDKYQYA CESRYNRVHG WICIDPVNST GFWLITPSYE FRSAGPLKQY 240 LTSHVGPTTL SVFHSTHYSG ADLIMQFGPN EPWKKVYGPI FIYLNSLSNG FSPIGLWEDA 300 KQQMVNEVES WPYTFPASED FLSSDQRGKV EGRLLVRDRY ISDAFIPVSG AYVGLAAIGE 360 VGSWQRECKG YQFWTITDDK GYFSIINIRP GGYNLYSWVN GFIGDYQFDS VIYVTSGCET 420 NVGELVYEAP RDGPTLWEIG IPDRSAAEFY VPDPNPMCIN RLYVNHPDRF RQYGLWERYA 480 ELYPNEDLVY TVGISDYRKD WFFAQVNRKK DNGTYIGTTW QINFKLDSVN TNGTYTLQVA 540 LASVHSAELE IRINNLEANP PLFSSGVIGK ENTIARHGIH GLYWLFSIHI QGTLLVQGNN 600 TIFLTQTRDT SPFIGIMYDY IRLEYKR* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG1429 | CobN | 0.004 | 370 | 501 | 143 | + Cobalamin biosynthesis protein CobN and related Mg-chelatases [Coenzyme metabolism] | ||
cd10316 | RGL4_M | 2.0e-27 | 326 | 425 | 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 | 5.0e-51 | 437 | 624 | 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-62 | 1 | 286 | 288 | + 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-91 | 1 | 193 | 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 |
EMBL | CBI19298.1 | 0 | 1 | 624 | 17 | 642 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 1 | 624 | 1 | 613 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301112.1 | 0 | 1 | 624 | 1 | 612 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 1 | 624 | 17 | 631 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527356.1 | 0 | 1 | 624 | 130 | 744 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FF401051 | 261 | 338 | 598 | 0 |
DT552229 | 301 | 1 | 300 | 0 |
DW479600 | 289 | 2 | 290 | 0 |
DW479599 | 287 | 1 | 287 | 0 |
EG983669 | 225 | 174 | 398 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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