y
Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra038945 |
Family | GH79 |
Protein Properties | Length: 537 Molecular Weight: 59815.8 Isoelectric Point: 6.8846 |
Chromosome | Chromosome/Scaffold: 08 Start: 8432839 End: 8435909 |
Description | glucuronidase 3 |
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 | 46 | 530 | 0 |
DEDFICATLDWWPPQKCDYGTCAWDHASILNLDLNNTIFQNAIREFAPLKIRIGGTLQDLVIYETPDQKQPCLPFTQNTSLLFGYTQGCLPMRRWNQLND FFSKTGAKVIFGLNALSGRSIQSNGEAVGAWDYTNAESFIQYIVQNNHTVDGWELGNELCGSGVGTRVAASQYATDTIALRDIVNRVYKDVSPMPLVIGP GGFFDAAWFTEYLSKTENSLNATTRHIYDLGPGVDQHLIEKILNPSYLDQEAITFRSLKNIINNSSTKAVAWVGEAGGAYNSGRNLVSNAFVYSFWYLDQ LGMASVYDTKTYCRQSLIGGNYGLLNTTNFTPNPDYYSALIWRRLMGRNALFTTFSGTKKIRSYTHCARQSKGITVLLMNLDNTTTVVANVELNNTYKLR HRKTSQKIARTSQMPWVSNGETQREEYHLTAKDANLHSQTMLLNGHALQVNSIGDIPPLEPIHVNSTDPITIAPYSIVFVHMPNV |
Full Sequence |
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Protein Sequence Length: 537 Download |
MGCRQISVIV LFLWVFQFAD KTVVSSAVEE KGTVFVYERA AVGTLDEDFI CATLDWWPPQ 60 KCDYGTCAWD HASILNLDLN NTIFQNAIRE FAPLKIRIGG TLQDLVIYET PDQKQPCLPF 120 TQNTSLLFGY TQGCLPMRRW NQLNDFFSKT GAKVIFGLNA LSGRSIQSNG EAVGAWDYTN 180 AESFIQYIVQ NNHTVDGWEL GNELCGSGVG TRVAASQYAT DTIALRDIVN RVYKDVSPMP 240 LVIGPGGFFD AAWFTEYLSK TENSLNATTR HIYDLGPGVD QHLIEKILNP SYLDQEAITF 300 RSLKNIINNS STKAVAWVGE AGGAYNSGRN LVSNAFVYSF WYLDQLGMAS VYDTKTYCRQ 360 SLIGGNYGLL NTTNFTPNPD YYSALIWRRL MGRNALFTTF SGTKKIRSYT HCARQSKGIT 420 VLLMNLDNTT TVVANVELNN TYKLRHRKTS QKIARTSQMP WVSNGETQRE EYHLTAKDAN 480 LHSQTMLLNG HALQVNSIGD IPPLEPIHVN STDPITIAPY SIVFVHMPNV VVPACA* 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 | 29 | 347 | 320 | + 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 | BAB10787.1 | 0 | 1 | 536 | 1 | 536 | unnamed protein product [Arabidopsis thaliana] |
EMBL | CBI25561.1 | 0 | 11 | 535 | 3 | 532 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_851093.1 | 0 | 1 | 536 | 1 | 536 | AtGUS3 (Arabidopsis thaliana glucuronidase 3); beta-glucuronidase |
RefSeq | XP_002263173.1 | 0 | 11 | 535 | 14 | 558 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324603.1 | 0 | 32 | 536 | 1 | 506 | predicted protein [Populus trichocarpa] |
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 | 0.0000003 | 141 | 387 | 122 | 357 | A Chain A, Bacillus Subtilis Pectate Lyase |
PDB | 3vnz_A | 0.0000003 | 141 | 387 | 122 | 357 | A Chain A, Bacillus Subtilis Pectate Lyase |
PDB | 3vny_A | 0.0000003 | 141 | 387 | 122 | 357 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |