Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g038979m |
Family | PL4 |
Protein Properties | Length: 607 Molecular Weight: 69435.1 Isoelectric Point: 10.3987 |
Chromosome | Chromosome/Scaffold: 00004 Start: 2562504 End: 2567129 |
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 | 2 | 584 | 0 |
AAGVQLHEQNNHVVMNNGILQVSISTPQGFVIGIQYKGNKNLLNVQNEEDNRGIEATNYKVIMRTKEQVELSFTRMWQPYTNGTIAPVNIDKRFLMLRGS SGFYSYAIYKRLKGWPGFQLFNNRMVFKPNPDKFHYMIISGNRQREMPLQQDRERGHKLAYEEAVLLPNGEVDDKYQYSMDAKDIRVHGWISTDSTVGFW QILPSSESRSFGPLKQFLTSHTGPISINTFHSTHYVGENFGMKFKDGEAWKKIFGPFLVYVNSVAGKGDRQMLWRDANRQFMNEVKSWPYKFPASKDFAR SNKRGSISGRLIVKDRYVSRAGIAAKGAYVGLAKPGRAGSWQTECKGYQFWTVANEGGNFSIKNVLIGNYNLYAWIPGFIGDFKYHAAIRITAGSAKQIG NLVYKAPRNGPTLWEIGIPDRSAAEFYIPNPNPKYINKLYVKHDRFRQYGLWERYAELHRKRDLVYEVWANNYRKDWYFAQNTRKKGNKYEGSTWQIQFK LEGVVKKATYKLRVAVAAAHGAELQVRVNSRSARRPLFSSGSVGRENAIARHGIHGVYKLFNVDVPGKVLRKGNNTIYLSQPR |
Full Sequence |
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Protein Sequence Length: 607 Download |
SAAGVQLHEQ NNHVVMNNGI LQVSISTPQG FVIGIQYKGN KNLLNVQNEE DNRGIEATNY 60 KVIMRTKEQV ELSFTRMWQP YTNGTIAPVN IDKRFLMLRG SSGFYSYAIY KRLKGWPGFQ 120 LFNNRMVFKP NPDKFHYMII SGNRQREMPL QQDRERGHKL AYEEAVLLPN GEVDDKYQYS 180 MDAKDIRVHG WISTDSTVGF WQILPSSESR SFGPLKQFLT SHTGPISINT FHSTHYVGEN 240 FGMKFKDGEA WKKIFGPFLV YVNSVAGKGD RQMLWRDANR QFMNEVKSWP YKFPASKDFA 300 RSNKRGSISG RLIVKDRYVS RAGIAAKGAY VGLAKPGRAG SWQTECKGYQ FWTVANEGGN 360 FSIKNVLIGN YNLYAWIPGF IGDFKYHAAI RITAGSAKQI GNLVYKAPRN GPTLWEIGIP 420 DRSAAEFYIP NPNPKYINKL YVKHDRFRQY GLWERYAELH RKRDLVYEVW ANNYRKDWYF 480 AQNTRKKGNK YEGSTWQIQF KLEGVVKKAT YKLRVAVAAA HGAELQVRVN SRSARRPLFS 540 SGSVGRENAI ARHGIHGVYK LFNVDVPGKV LRKGNNTIYL SQPRKLDAFT GIMYDYLRFE 600 GPDPNS* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam13620 | CarboxypepD_reg | 0.005 | 307 | 400 | 94 | + Carboxypeptidase regulatory-like domain. |
cd10316 | RGL4_M | 1.0e-28 | 304 | 403 | 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-44 | 415 | 600 | 188 | + 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-56 | 7 | 270 | 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 | 3.0e-61 | 1 | 170 | 189 | + 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 | 606 | 2 | 649 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 16 | 606 | 1 | 620 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002301113.1 | 0 | 5 | 604 | 50 | 678 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527353.1 | 0 | 4 | 602 | 5 | 633 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 1 | 602 | 2 | 634 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EL409069 | 278 | 320 | 594 | 0 |
DY922281 | 278 | 244 | 518 | 0 |
GW864372 | 311 | 126 | 427 | 0 |
DY969340 | 318 | 206 | 520 | 0 |
FY792769 | 268 | 306 | 571 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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