Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.006G021700.1 |
Family | GH79 |
Protein Properties | Length: 398 Molecular Weight: 44742 Isoelectric Point: 8.1103 |
Chromosome | Chromosome/Scaffold: 06 Start: 5567844 End: 5570261 |
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 | 269 | 391 | 8.8e-21 |
NQNLRVYAHCAKKKPGISIIFINLSKDSSFNVTLSNYEHQSRNLRTTDVVKPNYEFRGYQNREEYHLAALAGNIQGQIVLLNDIQMVPTKTFDIPAIEPK LVNASTPISVAAYSIVYVTIRDF | |||
GH79 | 57 | 271 | 0 |
INGCLPMERWDELNKFFNQTGWQSQNARDFMKYTISKGYKVDSYEFGHQLSRAGMGASIEAEQYGKDIVVLKNLVKELHLDPKTQPKVLGPSGYYDEKWF NSFLEVSRQEVVDGVTHHIYNLGPGDDPNMITKIQDPSYLNQVAQTYKGVLDIVNKFKPQSRAWVFKSGRALHGGAKDVSQTFANGFWYFDQLGMASTYN HKVFCRQTLIESNQN |
Full Sequence |
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Protein Sequence Length: 398 Download |
MDLKCVFSLA ILVSQISLLL TQNVNIVIQG ATSIAETDDN FVCATWIGSL LKNATTINGC 60 LPMERWDELN KFFNQTGWQS QNARDFMKYT ISKGYKVDSY EFGHQLSRAG MGASIEAEQY 120 GKDIVVLKNL VKELHLDPKT QPKVLGPSGY YDEKWFNSFL EVSRQEVVDG VTHHIYNLGP 180 GDDPNMITKI QDPSYLNQVA QTYKGVLDIV NKFKPQSRAW VFKSGRALHG GAKDVSQTFA 240 NGFWYFDQLG MASTYNHKVF CRQTLIESNQ NLRVYAHCAK KKPGISIIFI NLSKDSSFNV 300 TLSNYEHQSR NLRTTDVVKP NYEFRGYQNR EEYHLAALAG NIQGQIVLLN DIQMVPTKTF 360 DIPAIEPKLV NASTPISVAA YSIVYVTIRD FQAPLCA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 0.0006 | 22 | 45 | 24 | + 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. | ||
pfam03662 | Glyco_hydro_79n | 4.0e-87 | 59 | 250 | 216 | + 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 |
RefSeq | XP_002274743.1 | 0 | 59 | 396 | 126 | 521 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 59 | 397 | 127 | 518 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 59 | 394 | 134 | 528 | Heparanase precursor, putative [Ricinus communis] |