Basic Information | |
---|---|
Species | Cucumis sativus |
Cazyme ID | Cucsa.201230.1 |
Family | GH79 |
Protein Properties | Length: 507 Molecular Weight: 56954.9 Isoelectric Point: 8.1944 |
Chromosome | Chromosome/Scaffold: 01374 Start: 160503 End: 163007 |
Description | glucuronidase 2 |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH79 | 16 | 500 | 0 |
DENFICFTLDIWPHDECSQPNLCVWDSHASVLNVDLSLPIINKAVQAFKTLRIRVGGTLQDRLIYNIGEGFKGNCHPFEADDSLLFDFTEGCLYMERWDD LNNFFNNTGAIVTFGLNALLGKYHTQGMQWEGNWNYTNAEALIKYTVDKNYQINSWEFGNELAGRNSIGASISASQYAKDLLKLREIVDRLYKNSQQKPL IVAPGAFFDDKWYHELVTKTGPKVVSVLTHHIYNMGAGDDPKLIYRFVNPTYLSQVSNTFKQLKNIVQKHAPWSSAWVGEAGGAYQGGAYRISDSFINSF WYLDQLGMAAFYNTKVYCRQTLIGGFYSVLKAKTLVPTPDYYGALLFHRLMGPGVLKVHNKVSTYLRTYAHCSRERSGISMLFINLSNTTEFAINVKDHM TLSLHKRRKPKHGSSSINNLGTPREEYHLTPQNGLLRSSNVLLNGKALQLTSEGELPNLTPIYKDSNSSINIATWSIAFVVIPDF |
Full Sequence |
---|
Protein Sequence Length: 507 Download |
MGKIVVEGIT KIAETDENFI CFTLDIWPHD ECSQPNLCVW DSHASVLNVD LSLPIINKAV 60 QAFKTLRIRV GGTLQDRLIY NIGEGFKGNC HPFEADDSLL FDFTEGCLYM ERWDDLNNFF 120 NNTGAIVTFG LNALLGKYHT QGMQWEGNWN YTNAEALIKY TVDKNYQINS WEFGNELAGR 180 NSIGASISAS QYAKDLLKLR EIVDRLYKNS QQKPLIVAPG AFFDDKWYHE LVTKTGPKVV 240 SVLTHHIYNM GAGDDPKLIY RFVNPTYLSQ VSNTFKQLKN IVQKHAPWSS AWVGEAGGAY 300 QGGAYRISDS FINSFWYLDQ LGMAAFYNTK VYCRQTLIGG FYSVLKAKTL VPTPDYYGAL 360 LFHRLMGPGV LKVHNKVSTY LRTYAHCSRE RSGISMLFIN LSNTTEFAIN VKDHMTLSLH 420 KRRKPKHGSS SINNLGTPRE EYHLTPQNGL LRSSNVLLNG KALQLTSEGE LPNLTPIYKD 480 SNSSINIATW SIAFVVIPDF VAIGCN* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 2.0e-151 | 2 | 322 | 321 | + 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 | |
---|---|
GO Term | Description |
GO:0016020 | membrane |
GO:0016798 | hydrolase activity, acting on glycosyl bonds |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAB62595.1 | 0 | 4 | 506 | 10 | 521 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 4 | 505 | 27 | 512 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 4 | 506 | 32 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 4 | 505 | 27 | 538 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514696.1 | 0 | 4 | 505 | 27 | 538 | Heparanase-2, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vo0_A | 0.0000002 | 68 | 410 | 75 | 409 | A Chain A, Pectin Methylesterase From Yersinia Enterocolitica |
PDB | 3vnz_A | 0.0000002 | 68 | 410 | 75 | 409 | A Chain A, Pectin Methylesterase From Yersinia Enterocolitica |
PDB | 3vny_A | 0.0000002 | 68 | 410 | 75 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
CK266509 | 314 | 62 | 375 | 0 |
HO797031 | 370 | 152 | 505 | 0 |
GO873410 | 325 | 14 | 338 | 0 |
EC920863 | 289 | 47 | 335 | 0 |
FQ430098 | 278 | 123 | 400 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|