y
Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.252720.2 |
Family | GH79 |
Protein Properties | Length: 493 Molecular Weight: 54998.1 Isoelectric Point: 5.1376 |
Chromosome | Chromosome/Scaffold: 02229 Start: 1590179 End: 1592558 |
Description | glucuronidase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 16 | 486 | 0 |
DENYICMTIDYWPFNECSTLPCLWDGNASALILNLSLPTLTKAVQAFKTLRIRVGGSLQDKLVYDVGSFKGNCPQFARNSSALFQISDGCLSMERWDDLN QFFNKTGAIVTFGLNALLGRHHTTGLQWEGDWNCTNAEAFIQYTIEKNYRINSWEFGNEMVGHNSIGANVTSAQYEKDLIKLREIIDRLYNNSQQKASIA APSAFFYAPWYKDFVNGTGPGIVDILTHHIYNMGAGDDPKVINNFVDPNYLSKESKDFQQLKNIVENDAPWSVAWVGEAGGTFHGGSPYISNTFVDGFWY IDQLAMAALYNTKVYCRQTLVGGFYGILLPHTLAPSPDYYGALLFHRLMGSGVLKVDNNVSSYLRTYAHCSKERSGVTMLFINLSNETEFTVDIENNMMS TSLADKASQREEYHLIPNNGLVRSSTVLLNGNLLETTEDGDLPDLTPIYRDSNSSITIATWSIVFVVIPHF |
Full Sequence |
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Protein Sequence Length: 493 Download |
MGKIVVDLTI RKAQTDENYI CMTIDYWPFN ECSTLPCLWD GNASALILNL SLPTLTKAVQ 60 AFKTLRIRVG GSLQDKLVYD VGSFKGNCPQ FARNSSALFQ ISDGCLSMER WDDLNQFFNK 120 TGAIVTFGLN ALLGRHHTTG LQWEGDWNCT NAEAFIQYTI EKNYRINSWE FGNEMVGHNS 180 IGANVTSAQY EKDLIKLREI IDRLYNNSQQ KASIAAPSAF FYAPWYKDFV NGTGPGIVDI 240 LTHHIYNMGA GDDPKVINNF VDPNYLSKES KDFQQLKNIV ENDAPWSVAW VGEAGGTFHG 300 GSPYISNTFV DGFWYIDQLA MAALYNTKVY CRQTLVGGFY GILLPHTLAP SPDYYGALLF 360 HRLMGSGVLK VDNNVSSYLR TYAHCSKERS GVTMLFINLS NETEFTVDIE NNMMSTSLAD 420 KASQREEYHL IPNNGLVRSS TVLLNGNLLE TTEDGDLPDL TPIYRDSNSS ITIATWSIVF 480 VVIPHFEASA CK* 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 | 9.0e-141 | 2 | 319 | 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 |
DDBJ | BAB08480.1 | 0 | 4 | 491 | 6 | 515 | unnamed protein product [Arabidopsis thaliana] |
EMBL | CAB62595.1 | 0 | 4 | 491 | 10 | 520 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 4 | 491 | 27 | 512 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_200933.2 | 0 | 4 | 491 | 29 | 538 | AtGUS1 (Arabidopsis thaliana glucuronidase 1); beta-glucuronidase |
RefSeq | XP_002514696.1 | 0 | 4 | 491 | 27 | 538 | 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 | 0.00000001 | 105 | 407 | 115 | 408 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vnz_A | 0.00000001 | 105 | 407 | 115 | 408 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vny_A | 0.00000001 | 105 | 407 | 115 | 408 | 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 | 370 | 150 | 491 | 0 |
CK266509 | 314 | 61 | 374 | 0 |
GO875320 | 325 | 88 | 412 | 0 |
GO873410 | 323 | 14 | 336 | 0 |
FQ430098 | 279 | 120 | 398 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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