y
Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.015G049100.5 |
Family | GH79 |
Protein Properties | Length: 477 Molecular Weight: 52826 Isoelectric Point: 8.4292 |
Chromosome | Chromosome/Scaffold: 15 Start: 5225569 End: 5231168 |
Description | glucuronidase 2 |
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 | 23 | 470 | 0 |
NLRIRIGGSLQDQVLYDVESLKAPCHPFRKMKGGLFGFSKGCLHMNRWDELNHLFSRTGAIVTFGLNALYGRHQIRKGVWGGAWDSSNACDFMNYTVLKG YKIDSWEYGNELSGSGVSASVSAELYGKDLIKLKDVVNNLYKNSDLKPSLVAPGGFFDKQWYAKLLQVTGSGIVNFVTHHIYNLGAGMDPNLVNKILDPH YLSKVSETFSNLSQTIQQNGPWASAWVGESGGAYNSGGRHVSDTFVNSFWYLDQLGMASRYNTKVYCRQTLVGGHYGLLNTTTLVPNPDYYSALLWHRLM GKGVLAVGSNASPFLRSYAHCSKGRAGITLLLINLSNQTDFIISVQNSMDMRLTVEENISGENSFVRGLKRSVSWVGSRASDEPLYREEYHLTAKDGNLQ SRTMVLNGIPLELTEDENIPSLDPVRLDVNSPLYINPLSISFIVFPNF |
Full Sequence |
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Protein Sequence Length: 477 Download |
MELFIRNKLG LISSSSCQSH PRNLRIRIGG SLQDQVLYDV ESLKAPCHPF RKMKGGLFGF 60 SKGCLHMNRW DELNHLFSRT GAIVTFGLNA LYGRHQIRKG VWGGAWDSSN ACDFMNYTVL 120 KGYKIDSWEY GNELSGSGVS ASVSAELYGK DLIKLKDVVN NLYKNSDLKP SLVAPGGFFD 180 KQWYAKLLQV TGSGIVNFVT HHIYNLGAGM DPNLVNKILD PHYLSKVSET FSNLSQTIQQ 240 NGPWASAWVG ESGGAYNSGG RHVSDTFVNS FWYLDQLGMA SRYNTKVYCR QTLVGGHYGL 300 LNTTTLVPNP DYYSALLWHR LMGKGVLAVG SNASPFLRSY AHCSKGRAGI TLLLINLSNQ 360 TDFIISVQNS MDMRLTVEEN ISGENSFVRG LKRSVSWVGS RASDEPLYRE EYHLTAKDGN 420 LQSRTMVLNG IPLELTEDEN IPSLDPVRLD VNSPLYINPL SISFIVFPNF DAPACA* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 2.0e-143 | 22 | 278 | 257 | + 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 |
EMBL | CAB62595.1 | 0 | 22 | 476 | 68 | 521 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 22 | 476 | 85 | 513 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284470.1 | 0 | 22 | 476 | 85 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002321464.1 | 0 | 22 | 476 | 85 | 541 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514696.1 | 0 | 22 | 476 | 85 | 539 | Heparanase-2, 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 | 0.00009 | 22 | 366 | 71 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vnz_A | 0.00009 | 22 | 366 | 71 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vny_A | 0.00009 | 22 | 366 | 71 | 409 | 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 |
HO797031 | 371 | 109 | 476 | 0 |
DT521895 | 242 | 236 | 477 | 0 |
EG664145 | 271 | 161 | 431 | 0 |
CB968811 | 284 | 183 | 465 | 0 |
HO781548 | 336 | 148 | 476 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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