y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_032464m |
Family | GH79 |
Protein Properties | Length: 549 Molecular Weight: 60299.2 Isoelectric Point: 8.1 |
Chromosome | Chromosome/Scaffold: 08686 Start: 908587 End: 911301 |
Description | glucuronidase 3 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 52 | 541 | 0 |
DEDFICATLDWWPPEKCDYGTCSWDHASLINLDINSNIFLNAVKAFSPLKIRLGGTLQDKVIYDTEDNKEPCKQFVKNTTEMFGFTQGCLPMYRWDELNA FFKKSGAKIIFGLNALAGRSIQSDGSATGTWNYTNAESFISYTVKKNYSIHGWELGNELSGSGVGTRIAAKQYAADTISLYKIVQNIYSGVEPKPLVLAP GGFFDANWFKEFIDKTGNSLDVITHHIYNLGPGVDEHLVEKILNPSYLDGEANTFSGLQNSLKSSATSATAWVGEAGGAYNSGRNLVSNAFVYSFWYLDQ LGMASAYDTKTYCRQSLIGGNYGLLNTTTFVPNPDYYSALLWHRLMGRNVLSTKFSGTKKIRAYAHCTKESKGITLLLINLDNSTNVEVKVAFNGTATLH HQQKHHRSHKYQRSHRTRNIKLPQGSESSTREEYHLTAKDGNLHSQTMLLNGNILTVNSSGDIPALEPVSVNLSKPISVAPFSVVFVHLP |
Full Sequence |
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Protein Sequence Length: 549 Download |
MGSQIFLKGF CFLACIFSYS FVSLSSQAAA AGDGSVKGTV FIDGKTSIGK IDEDFICATL 60 DWWPPEKCDY GTCSWDHASL INLDINSNIF LNAVKAFSPL KIRLGGTLQD KVIYDTEDNK 120 EPCKQFVKNT TEMFGFTQGC LPMYRWDELN AFFKKSGAKI IFGLNALAGR SIQSDGSATG 180 TWNYTNAESF ISYTVKKNYS IHGWELGNEL SGSGVGTRIA AKQYAADTIS LYKIVQNIYS 240 GVEPKPLVLA PGGFFDANWF KEFIDKTGNS LDVITHHIYN LGPGVDEHLV EKILNPSYLD 300 GEANTFSGLQ NSLKSSATSA TAWVGEAGGA YNSGRNLVSN AFVYSFWYLD QLGMASAYDT 360 KTYCRQSLIG GNYGLLNTTT FVPNPDYYSA LLWHRLMGRN VLSTKFSGTK KIRAYAHCTK 420 ESKGITLLLI NLDNSTNVEV KVAFNGTATL HHQQKHHRSH KYQRSHRTRN IKLPQGSESS 480 TREEYHLTAK DGNLHSQTML LNGNILTVNS SGDIPALEPV SVNLSKPISV APFSVVFVHL 540 PYVVPACS* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 0 | 36 | 353 | 319 | + 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 | CAN81917.1 | 0 | 1 | 547 | 1 | 554 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002263173.1 | 0 | 1 | 547 | 5 | 558 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324603.1 | 0 | 38 | 548 | 1 | 506 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331013.1 | 0 | 9 | 548 | 2 | 547 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533671.1 | 0 | 1 | 547 | 1 | 550 | 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 | 0.000000003 | 147 | 449 | 122 | 413 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 3vnz_A | 0.000000003 | 147 | 449 | 122 | 413 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 3vny_A | 0.000000003 | 147 | 449 | 122 | 413 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |