| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.006G004200.1 |
| Family | GH79 |
| Protein Properties | Length: 464 Molecular Weight: 51456.2 Isoelectric Point: 7.1001 |
| Chromosome | Chromosome/Scaffold: 06 Start: 883846 End: 886252 |
| 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 | 37 | 307 | 0 |
| TDDNFDLKKKVLINAIKAFNSLRIKVGGSLQDQVVYGVGEVKNCPNFMKKEGSLFGFSQGCLPVERWDELNNFFNQTGVNVTFGLNALLGRNESQNEKGL WVGDWNSQNARDLMKYTISRGYKVDSYEFGNQLSGAGMGARVEAEQYGKDVIVLKNMVKELHPYPKTQPKVLGPSGFYDEKWFNSFLEVSGQEVVDGVTH HIYNLGPGDDLNLITKIQDPSYLNQVAQTYRGVFNIVHKFKPQSGAWVSKSGGALQGGAKDVSPTFADGFW | |||
| Full Sequence |
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| Protein Sequence Length: 464 Download |
| MDLKCIFSLV IIVSRISLSF TQNVNVVIQG STSVAETDDN FDLKKKVLIN AIKAFNSLRI 60 KVGGSLQDQV VYGVGEVKNC PNFMKKEGSL FGFSQGCLPV ERWDELNNFF NQTGVNVTFG 120 LNALLGRNES QNEKGLWVGD WNSQNARDLM KYTISRGYKV DSYEFGNQLS GAGMGARVEA 180 EQYGKDVIVL KNMVKELHPY PKTQPKVLGP SGFYDEKWFN SFLEVSGQEV VDGVTHHIYN 240 LGPGDDLNLI TKIQDPSYLN QVAQTYRGVF NIVHKFKPQS GAWVSKSGGA LQGGAKDVSP 300 TFADGFWFSA GKLSFGGNYA LLKTTTFISN PDYYGSLLWH RLMENIVLAV TQESQESNPK 360 KKPGNSIIFV NLLKDSSFDV TLSSYEHHRC NLRSTDAAKP NFEFKSYLHR EEYHLTALGG 420 NIQDTFDIPA MDPKLVNAST AISVAAHSIV YETIRDFHAP VCV* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03662 | Glyco_hydro_79n | 9.0e-131 | 22 | 308 | 316 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0016020 | membrane |
| GO:0016798 | hydrolase activity, acting on glycosyl bonds |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI27258.1 | 0 | 20 | 463 | 23 | 524 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002274743.1 | 0 | 20 | 463 | 21 | 522 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315010.1 | 0 | 17 | 463 | 19 | 518 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002512114.1 | 0 | 24 | 461 | 31 | 529 | Heparanase precursor, putative [Ricinus communis] |
| RefSeq | XP_002512114.1 | 0.0007 | 41 | 71 | 557 | 587 | Heparanase precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vo0_A | 0.002 | 101 | 359 | 119 | 377 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 3vnz_A | 0.002 | 101 | 359 | 119 | 377 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 3vny_A | 0.002 | 101 | 359 | 119 | 377 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
