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Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G098397_T03 |
Family | GH79 |
Protein Properties | Length: 541 Molecular Weight: 59643.5 Isoelectric Point: 5.6808 |
Chromosome | Chromosome/Scaffold: 3 Start: 124642507 End: 124646867 |
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 | 40 | 533 | 0 |
SDEFVCATIDWWPPEKCNYDQCPWERASVLNLDLTNPLLAKAIQAFSPLRIRVGGSLQDQVLYGTPNLGLPCDPFTKVSSGLFGFSQGCITLERWDDIND MFLKTGAVVTFGLNALRGRQQTRKGVWGGPWNSSNAREFIEYTVLKNYPIDSWEFGNELSGSGVGASVSAEQYGKDLVELQTIISELYGDSNKPLVVAPG GFYDQKWFAQLLDVSGPNVLNAMTHHIYNLGAGNDPQVPNRILNPQYLSRTSDTFRSLQLTIQRHGPWSAPWVGESGGAYNSGSRLVSNTFLNSFWYLDQ LGQSAKYDTKVYCRQTLIGGNYGLLDTETFVPNPDYYSALLWHQLMGTGVLSVDISGSSYLRAYVHCAKQKGGVTLLLLNLHRTMGFMVSVRNDLNVNLA EGQGIRRDSAFVHGLKRTVSWVGSKASDGFSKREEYHLSSKDGNPFARTMLLNGAPLELTEDGGIPSLYPVEVSVNSPIYVAPLTIAFVVFPDF |
Full Sequence |
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Protein Sequence Length: 541 Download |
MRLWSLFLLP LLCLPARVRS EDYADATVIV RGSETIASTS DEFVCATIDW WPPEKCNYDQ 60 CPWERASVLN LDLTNPLLAK AIQAFSPLRI RVGGSLQDQV LYGTPNLGLP CDPFTKVSSG 120 LFGFSQGCIT LERWDDINDM FLKTGAVVTF GLNALRGRQQ TRKGVWGGPW NSSNAREFIE 180 YTVLKNYPID SWEFGNELSG SGVGASVSAE QYGKDLVELQ TIISELYGDS NKPLVVAPGG 240 FYDQKWFAQL LDVSGPNVLN AMTHHIYNLG AGNDPQVPNR ILNPQYLSRT SDTFRSLQLT 300 IQRHGPWSAP WVGESGGAYN SGSRLVSNTF LNSFWYLDQL GQSAKYDTKV YCRQTLIGGN 360 YGLLDTETFV PNPDYYSALL WHQLMGTGVL SVDISGSSYL RAYVHCAKQK GGVTLLLLNL 420 HRTMGFMVSV RNDLNVNLAE GQGIRRDSAF VHGLKRTVSW VGSKASDGFS KREEYHLSSK 480 DGNPFARTML LNGAPLELTE DGGIPSLYPV EVSVNSPIYV APLTIAFVVF PDFEAEACGR 540 * 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 | 24 | 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 |
GenBank | ACG27548.1 | 0 | 1 | 540 | 1 | 540 | heparanase-like protein 2 precursor [Zea mays] |
GenBank | ACR34666.1 | 0 | 1 | 540 | 36 | 575 | unknown [Zea mays] |
GenBank | EEC69565.1 | 0 | 1 | 540 | 671 | 1237 | hypothetical protein OsI_38868 [Oryza sativa Indica Group] |
RefSeq | NP_001130921.1 | 0 | 1 | 540 | 27 | 566 | hypothetical protein LOC100192026 [Zea mays] |
RefSeq | XP_002442385.1 | 0 | 16 | 540 | 16 | 540 | hypothetical protein SORBIDRAFT_08g019250 [Sorghum bicolor] |
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 | 0.0001 | 128 | 404 | 115 | 383 | A Chain A, Crystal Structure Of Class V Chitinase (E115q Mutant) From Nicotiana Tobaccum In Complex With Nag4 |
PDB | 3vnz_A | 0.0001 | 128 | 404 | 115 | 383 | A Chain A, Crystal Structure Of Class V Chitinase (E115q Mutant) From Nicotiana Tobaccum In Complex With Nag4 |
PDB | 3vny_A | 0.0001 | 128 | 404 | 115 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |