Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.C02740.1 |
Family | GH79 |
Protein Properties | Length: 489 Molecular Weight: 53083.1 Isoelectric Point: 7.0507 |
Chromosome | Chromosome/Scaffold: 3 Start: 52482150 End: 52485355 |
Description | glucuronidase 3 |
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 |
GH79 | 118 | 481 | 0 |
KCRAIVTFGLNALYGRTVNSDGSVHGPWDSSNAEILLRYTVNKGYTIHGWELGNELSGQGIGAQISAQQYASDIKTLQNLLDDIYGGFEVKPLILAPGGF FDANWFKDFVDHTTQMFQVVTHHVYSLGAGYDDNLTSRILDPSYLNGMAQTFSSLESILKNSGTSAVAWVGEAGGAYGGGHHLVTDAFVSSFWYLDQLAM AATYNTKTYCRQTLIGGGYGLLNSSTFQPNPDYYSALLWHRLMGNNVLFTNFTGTNKLRAYSHCSKNSVNGAGNGTLILQPQIRSRKSKFSRISKGLIFD ANIREEYHLTAKDRDLHSQVTLLNGKILSVDSSGNIPALNPIQVRMSDPILVASFSVAFARFPS |
Full Sequence |
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Protein Sequence Length: 489 Download |
MGSLLVLVGV CFLVVWLHHY SVDSQTTGLS GIVVDGSVFI NGSASIASID DDFICATLDY 60 GPPDVCHQGT CWGNATLFTL DLSNPILLNA IKAFSPLKIR MGGTLQDKLI YHSVNSVKCR 120 AIVTFGLNAL YGRTVNSDGS VHGPWDSSNA EILLRYTVNK GYTIHGWELG NELSGQGIGA 180 QISAQQYASD IKTLQNLLDD IYGGFEVKPL ILAPGGFFDA NWFKDFVDHT TQMFQVVTHH 240 VYSLGAGYDD NLTSRILDPS YLNGMAQTFS SLESILKNSG TSAVAWVGEA GGAYGGGHHL 300 VTDAFVSSFW YLDQLAMAAT YNTKTYCRQT LIGGGYGLLN SSTFQPNPDY YSALLWHRLM 360 GNNVLFTNFT GTNKLRAYSH CSKNSVNGAG NGTLILQPQI RSRKSKFSRI SKGLIFDANI 420 REEYHLTAKD RDLHSQVTLL NGKILSVDSS GNIPALNPIQ VRMSDPILVA SFSVAFARFP 480 SMNVTACR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 6.0e-111 | 34 | 315 | 318 | + 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 | CBI21126.1 | 0 | 22 | 467 | 8 | 516 | unnamed protein product [Vitis vinifera] |
EMBL | CBI21126.1 | 0 | 22 | 488 | 432 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283254.1 | 0 | 1 | 487 | 1 | 536 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002283260.1 | 0 | 1 | 488 | 1 | 546 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324878.1 | 0 | 36 | 487 | 1 | 504 | predicted protein [Populus trichocarpa] |