y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.B03174.1 |
Family | GH79 |
Protein Properties | Length: 523 Molecular Weight: 57371.8 Isoelectric Point: 8.1529 |
Chromosome | Chromosome/Scaffold: 2 Start: 56846238 End: 56850054 |
Description | glucuronidase 1 |
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 | 43 | 515 | 0 |
DDSFICATLDWWPSDKCDYGQCPWGLAGVLNLVSLSSRIAAFNPLRIRVGGSLQDQVVYEHTHLYNKKCSEFKKEDGGMFGFSEGCLRTERWDQLNHLFN QTGALVTFGLNALNGRMRSKQSDNLYVGKWKNGNAHHLVRYTHHKGYKIDSYELGNELCGSGVSGRLTAEQYTEDIVKMKKFLTKLYPDQASRPKVLGPA GFYDRKWFETFLKATGPGVVDGVTHHIYNLGAGVDPTLINKVQDPSYLDQIDTTYKDVSDTVQKFGPWTAPWVGEAGGAYNSGGKGVSNTFANGFWYLDQ LGMTSRFNHKVFCRQALIGGNYALLNTTTFIPNPDFYGALLWHRLMGKEVLSTTHSGSPYLRAYAHCSRNTPGVTVVLINMSNSTSFDVSIVDDPNWSPS KQKKIASGSHAQREEYHLTPKDGNIRSDVLLLNGTPLKLTDSSDIPELNPTTVDPSQPIHVVADSIVFARLQG |
Full Sequence |
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Protein Sequence Length: 523 Download |
MESKVGLGWV SLLLLSSLLS SSSSSADNVK VAVKGGASIA ATDDSFICAT LDWWPSDKCD 60 YGQCPWGLAG VLNLVSLSSR IAAFNPLRIR VGGSLQDQVV YEHTHLYNKK CSEFKKEDGG 120 MFGFSEGCLR TERWDQLNHL FNQTGALVTF GLNALNGRMR SKQSDNLYVG KWKNGNAHHL 180 VRYTHHKGYK IDSYELGNEL CGSGVSGRLT AEQYTEDIVK MKKFLTKLYP DQASRPKVLG 240 PAGFYDRKWF ETFLKATGPG VVDGVTHHIY NLGAGVDPTL INKVQDPSYL DQIDTTYKDV 300 SDTVQKFGPW TAPWVGEAGG AYNSGGKGVS NTFANGFWYL DQLGMTSRFN HKVFCRQALI 360 GGNYALLNTT TFIPNPDFYG ALLWHRLMGK EVLSTTHSGS PYLRAYAHCS RNTPGVTVVL 420 INMSNSTSFD VSIVDDPNWS PSKQKKIASG SHAQREEYHL TPKDGNIRSD VLLLNGTPLK 480 LTDSSDIPEL NPTTVDPSQP IHVVADSIVF ARLQGFKAPA CN* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 4.0e-165 | 26 | 344 | 323 | + 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 | CBI27258.1 | 0 | 26 | 521 | 24 | 523 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 26 | 521 | 22 | 521 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 4 | 521 | 5 | 517 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 26 | 522 | 28 | 531 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.000002 | 56 | 100 | 539 | 587 | Heparanase precursor, 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 | 0.000003 | 89 | 433 | 75 | 408 | A Chain A, Human Liver Glycogen Phosphorylase- Gl Complex |
PDB | 3vnz_A | 0.000003 | 89 | 433 | 75 | 408 | A Chain A, Human Liver Glycogen Phosphorylase- Gl Complex |
PDB | 3vny_A | 0.000003 | 89 | 433 | 75 | 408 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |