Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000253529 |
Family | PL4 |
Protein Properties | Length: 761 Molecular Weight: 86923.5 Isoelectric Point: 6.5167 |
Chromosome | Chromosome/Scaffold: 02594441 Start: 17281 End: 23563 |
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 | 95 | 724 | 0 |
TSGLQLHIRDKEVVVENGILQMTLSKPGGVVTGLQYNGVDNLLEVLNEAPNRGYWDLVWTAPGITRKKGAFDRIEGTNFSVIVETEDQIELSFTRMWDPS LEGKLVPLNIDIRFVMLRNSSGFYTYAIYEHLKEWPAFNLTNTRTVFKLRKEKFHYMAISDKRQRYMPLPDDRLQGRGQALAYPEAVLLVNPVEPQFKGE VDDKYLYSIENKENRVHGWISTEPPVGFWQITPSQEFKSGGPFKQCLTSHVGPTTLAIFHSTHYSGAELIIEFKPSEPWKKVLGPIFIYLNSLVTEDDPL QQLWEDAKQQMKTEVQSWPYDFPSSEDFLSSDQRGTVTGRLLVRDGYINTEDIFGDGTQVGLAAPGDAGSWQLECKGYQFWTKANDKGFFSISGIRPGIY NVYAWVPGFIGDYRHDAEVIITPGCNVDVGTLVYEPPRSGPTFWEIGIPDRTAAEFYIPDPNPNHINKLYVNHTDRFRQYGLWERYAELYPYNDLVYTVG VNDYRKDFYFAQVTRKTGNNTYQGSTWQIRFTLDTVGKNNTYTLRIALATAHVSELQKCHYIFTEKILFDYLIVKVRINDLEASNPLFSTGQIGNDNTIA RHGIHGLYRLYTVDIPGAQLLEGNNTIFLT |
Full Sequence |
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Protein Sequence Length: 761 Download |
MLVWFTKHKE WRRGDKVKKS QENILFTETW PQIDVPITGR RFTVHMSTFH VRLGWAPTGN 60 VFWASESTCH CLAKLCTIIL FIQAMNFLAA AQNSTSGLQL HIRDKEVVVE NGILQMTLSK 120 PGGVVTGLQY NGVDNLLEVL NEAPNRGYWD LVWTAPGITR KKGAFDRIEG TNFSVIVETE 180 DQIELSFTRM WDPSLEGKLV PLNIDIRFVM LRNSSGFYTY AIYEHLKEWP AFNLTNTRTV 240 FKLRKEKFHY MAISDKRQRY MPLPDDRLQG RGQALAYPEA VLLVNPVEPQ FKGEVDDKYL 300 YSIENKENRV HGWISTEPPV GFWQITPSQE FKSGGPFKQC LTSHVGPTTL AIFHSTHYSG 360 AELIIEFKPS EPWKKVLGPI FIYLNSLVTE DDPLQQLWED AKQQMKTEVQ SWPYDFPSSE 420 DFLSSDQRGT VTGRLLVRDG YINTEDIFGD GTQVGLAAPG DAGSWQLECK GYQFWTKAND 480 KGFFSISGIR PGIYNVYAWV PGFIGDYRHD AEVIITPGCN VDVGTLVYEP PRSGPTFWEI 540 GIPDRTAAEF YIPDPNPNHI NKLYVNHTDR FRQYGLWERY AELYPYNDLV YTVGVNDYRK 600 DFYFAQVTRK TGNNTYQGST WQIRFTLDTV GKNNTYTLRI ALATAHVSEL QKCHYIFTEK 660 ILFDYLIVKV RINDLEASNP LFSTGQIGND NTIARHGIHG LYRLYTVDIP GAQLLEGNNT 720 IFLTRALSIS PFQGIMYDYI RLEGPASSNN ESLGSSSWGY K |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 2.0e-28 | 427 | 526 | 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 | 2.0e-51 | 538 | 743 | 207 | + 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-72 | 104 | 386 | 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 | 9.0e-98 | 78 | 295 | 218 | + 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 | 94 | 752 | 2 | 651 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 109 | 752 | 1 | 622 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002527356.1 | 0 | 106 | 749 | 127 | 750 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527356.1 | 0 | 168 | 295 | 1 | 128 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527357.1 | 0 | 94 | 750 | 2 | 639 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DW479599 | 293 | 95 | 387 | 0 |
DW479600 | 293 | 95 | 387 | 0 |
DT552229 | 293 | 109 | 401 | 0 |
DY293973 | 331 | 94 | 422 | 0 |
DR999573 | 200 | 452 | 651 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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