Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.113020.1 |
Family | GH79 |
Protein Properties | Length: 537 Molecular Weight: 60014.4 Isoelectric Point: 8.1935 |
Chromosome | Chromosome/Scaffold: 00953 Start: 1319068 End: 1323977 |
Description | glucuronidase 2 |
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 | 41 | 530 | 0 |
NFICATLDWWPHDKCDYNQCPWGYSSVINLNLSHPLLSKAIQAFHNLRIRIGGSLQDQVLYDVESLKTPCRPFQKISSGLFGFSKGCLHLYRWDELNHLF SRTGAIVTFGLNALYGRHKIGRIQWGGDWDSSNARDFMKYTISKGYVIESWEFGNELSGSGVAASVGAVQYGKDLIRLKSIINELYQDSNSKPSLIAPGG FFEQDWYAKLLQVSGSNVVDVITHHIYNLGPGIDPNLVKKILDPQYLSRVSETFSKLDQTIQTYGPWASAWIGESGGAYNSGGRNISNTFVNSFWYLDQL GMAAKYRTKVYCRQTLIGGNYGLLNTGTFVPNPDFYSALLWHRLMGTGVLDVNSDASPFLRSYAHCSKERAGVTALFINLSNQTRFVVSVRNSLTIKLRR VHKGSSFMQGIKKTVSWVGNKASDLSISREEYHLTPKDGFLQSQTMVLNDIPLELTEDGNIPQLNPVLNDVNSPIVIAPLSIAFIVFPNF |
Full Sequence |
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Protein Sequence Length: 537 Download |
MDVRSFLLLF VVSLPAIWAQ DIEHARIIIN ANEKVAETDY NFICATLDWW PHDKCDYNQC 60 PWGYSSVINL NLSHPLLSKA IQAFHNLRIR IGGSLQDQVL YDVESLKTPC RPFQKISSGL 120 FGFSKGCLHL YRWDELNHLF SRTGAIVTFG LNALYGRHKI GRIQWGGDWD SSNARDFMKY 180 TISKGYVIES WEFGNELSGS GVAASVGAVQ YGKDLIRLKS IINELYQDSN SKPSLIAPGG 240 FFEQDWYAKL LQVSGSNVVD VITHHIYNLG PGIDPNLVKK ILDPQYLSRV SETFSKLDQT 300 IQTYGPWASA WIGESGGAYN SGGRNISNTF VNSFWYLDQL GMAAKYRTKV YCRQTLIGGN 360 YGLLNTGTFV PNPDFYSALL WHRLMGTGVL DVNSDASPFL RSYAHCSKER AGVTALFINL 420 SNQTRFVVSV RNSLTIKLRR VHKGSSFMQG IKKTVSWVGN KASDLSISRE EYHLTPKDGF 480 LQSQTMVLND IPLELTEDGN IPQLNPVLND VNSPIVIAPL SIAFIVFPNF EAPTCK* 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 | 0 | 23 | 341 | 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 | CAB62595.1 | 0 | 19 | 535 | 2 | 520 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 12 | 535 | 12 | 512 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 6 | 535 | 11 | 542 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 12 | 535 | 12 | 538 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514696.1 | 0 | 15 | 535 | 15 | 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 | 0.002 | 259 | 429 | 235 | 409 | L Chain L, Crystal Structure Of Rsv-neutralizing Human Antibody D25 |
PDB | 3vnz_A | 0.002 | 259 | 429 | 235 | 409 | L Chain L, Crystal Structure Of Rsv-neutralizing Human Antibody D25 |
PDB | 3vny_A | 0.002 | 259 | 429 | 235 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |