Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.006G004500.1 |
Family | GH79 |
Protein Properties | Length: 481 Molecular Weight: 53298.6 Isoelectric Point: 7.3218 |
Chromosome | Chromosome/Scaffold: 06 Start: 898274 End: 900700 |
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 | 43 | 474 | 0 |
GLLNLDLKKKVLINAIKAFNSLRIKVGGSLQDQVVYGVGEVKNCPNFMKKEGSLFGFSQGCLPVERWDELNNFFNQTGVKVTFGLNALLGRNESQSEKGL WVGDWNSQNARDLMKYTISRGYKVDSYEFGNQLSGAGMGARVEAEQYGKDVIVLKNMVKELHPDPKTQPKFNSFLEVSGQEVVDGVTHHIYNLRPDPSYL NQVAQTYRGVFNIVNKFKPQSGAWVSESGGALQGGAKDVSPTFADGFWYFDQLGMASTYNHKVFCRQTLIGGNYALLDTTTFIPNPDYYGALLWHRLMGS IVLAVTQESNPNLCVYAHCAKKKPGISIIFINLSNDSTFDVTLSSYEHRRRNLRPTDAAKPNFEFTSHLNREEYHLTALGGNIQGQIVLLNDVPMVLTDT FDIPAMDPKLVNASTPISVAAHSIVYVTIRDF |
Full Sequence |
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Protein Sequence Length: 481 Download |
MDLKYIFSLV IIVSRISLSF TQNVNVVIQG STSVAETDDN FAGLLNLDLK KKVLINAIKA 60 FNSLRIKVGG SLQDQVVYGV GEVKNCPNFM KKEGSLFGFS QGCLPVERWD ELNNFFNQTG 120 VKVTFGLNAL LGRNESQSEK GLWVGDWNSQ NARDLMKYTI SRGYKVDSYE FGNQLSGAGM 180 GARVEAEQYG KDVIVLKNMV KELHPDPKTQ PKFNSFLEVS GQEVVDGVTH HIYNLRPDPS 240 YLNQVAQTYR GVFNIVNKFK PQSGAWVSES GGALQGGAKD VSPTFADGFW YFDQLGMAST 300 YNHKVFCRQT LIGGNYALLD TTTFIPNPDY YGALLWHRLM GSIVLAVTQE SNPNLCVYAH 360 CAKKKPGISI IFINLSNDST FDVTLSSYEH RRRNLRPTDA AKPNFEFTSH LNREEYHLTA 420 LGGNIQGQIV LLNDVPMVLT DTFDIPAMDP KLVNASTPIS VAAHSIVYVT IRDFHAPVCV 480 * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 4.0e-123 | 22 | 296 | 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 | |
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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 | CBI27258.1 | 0 | 20 | 480 | 23 | 524 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 20 | 480 | 21 | 522 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 17 | 480 | 19 | 518 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 24 | 478 | 31 | 529 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.00001 | 42 | 77 | 552 | 587 | Heparanase precursor, putative [Ricinus communis] |