Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr4g116040.1 |
Family | GH79 |
Protein Properties | Length: 344 Molecular Weight: 37576.8 Isoelectric Point: 9.0512 |
Chromosome | Chromosome/Scaffold: 4 Start: 40187501 End: 40189421 |
Description | glucuronidase 3 |
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 |
GH79 | 18 | 336 | 0 |
NFANAKSFIRYTVSKNYTIHGWELGNELCGKGIGISISPYQYANDATILRNIVQEVYREVVQKPLIIAPGGFFDANWFKKFLNRSEKLADVVTHHIYNLG PGVDDHITEKILDPTYLDGVAGTFSSLKNVLQRSSTTAKAWVGEAGGAWNSGHHLVSDAFVNSFWYFDQLGMSATYSTKTYCRQTLIGGTTRSSLALTHG RTRPVMSTTFNGTKKIRTYAHCKGITMLFLNFDNSTTVQATVASNYATKPSPSLVVESQRRDHLTAKDGDLHSQIMLLNGNILSVNSAGDIPPLNPIYVD SSKPITLDPLSIVFVQIQD |
Full Sequence |
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Protein Sequence Length: 344 Download |
MLLLGRSLKP GSVVAACNFA NAKSFIRYTV SKNYTIHGWE LGNELCGKGI GISISPYQYA 60 NDATILRNIV QEVYREVVQK PLIIAPGGFF DANWFKKFLN RSEKLADVVT HHIYNLGPGV 120 DDHITEKILD PTYLDGVAGT FSSLKNVLQR SSTTAKAWVG EAGGAWNSGH HLVSDAFVNS 180 FWYFDQLGMS ATYSTKTYCR QTLIGGTTRS SLALTHGRTR PVMSTTFNGT KKIRTYAHCK 240 GITMLFLNFD NSTTVQATVA SNYATKPSPS LVVESQRRDH LTAKDGDLHS QIMLLNGNIL 300 SVNSAGDIPP LNPIYVDSSK PITLDPLSIV FVQIQDTAIT ICS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 3.0e-97 | 3 | 188 | 188 | + Glycosyl hydrolase family 79, N-terminal domain. Family of endo-beta-N-glucuronidase, or heparanase. Heparan sulfate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulfate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular micro-environment. Heparanase degrades HS at specific intra-chain sites. The enzyme is synthesised as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularization, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity. |
Gene Ontology | |
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GO Term | Description |
GO:0016020 | membrane |
GO:0016798 | hydrolase activity, acting on glycosyl bonds |
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 | ACU20377.1 | 0 | 3 | 343 | 166 | 525 | unknown [Glycine max] |
EMBL | CBI25561.1 | 0 | 3 | 342 | 159 | 532 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002324603.1 | 0 | 3 | 334 | 130 | 498 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331013.1 | 0 | 3 | 334 | 156 | 539 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533671.1 | 0 | 3 | 334 | 168 | 543 | heparanase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vo0_A | 0.008 | 18 | 187 | 148 | 313 | A Chain A, Crystal Structure Of The Cellulase Cel9m Of C. Cellulolyticum |
PDB | 3vnz_A | 0.008 | 18 | 187 | 148 | 313 | A Chain A, Crystal Structure Of The Cellulase Cel9m Of C. Cellulolyticum |
PDB | 3vny_A | 0.008 | 18 | 187 | 148 | 313 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO799886 | 308 | 58 | 344 | 0 |
CX636465 | 263 | 18 | 262 | 0 |
CA990302 | 260 | 107 | 344 | 0 |
CO982074 | 265 | 93 | 336 | 0 |
FK019336 | 230 | 24 | 239 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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