| Basic Information | |
|---|---|
| Species | Picea abies |
| Cazyme ID | MA_77698g0010 |
| Family | GH79 |
| Protein Properties | Length: 517 Molecular Weight: 57022.9 Isoelectric Point: 6.5632 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH79 | 46 | 509 | 0 |
| DEDFICATLDWWPPEKCDYGTCSWGHASLLNLDLENPLLATAIKAFHPLKIRLGGSLQDKVIYDVGKLKQPCHPFVKNASRMFGFSNGCLPMSRWDALNA FFNKTGAVVAFGLNALNGKRWKSNGATDGPWDSSNARDFIQYTVDHGHKIKAWELGNELSGSGVGTSISVEQYAADIIELHGILDGIYKDYEEKPLLIAP DGFFVADWFKEFLNLTGPNIMNVVTHHFYNLGAGVDNDLVEKILNPSYLSQEASTFKGLQAVLQNYGPWSKAWVGETGGAYNSGHNLITNAFVMSFWYLD QLGMASAFSTKSFCRQSLIGGNYGLLNTTTFLPNPDYYSALLWHRLMGTRVLATNSTGTEYLRAYAHCTKSYRGVTLLLINLSRDTGISVQVSTGSGTST DRNSRLEYHLTAKDGDLHSQTVLLNGNILNITPDGEIPSLSAVTVPANRPILVAPLSIAFVNLP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 517 Download |
| MASWFPRLWV WTLLLCCKCI RCENGFNKTV TAEVRVEGVF AIGETDEDFI CATLDWWPPE 60 KCDYGTCSWG HASLLNLDLE NPLLATAIKA FHPLKIRLGG SLQDKVIYDV GKLKQPCHPF 120 VKNASRMFGF SNGCLPMSRW DALNAFFNKT GAVVAFGLNA LNGKRWKSNG ATDGPWDSSN 180 ARDFIQYTVD HGHKIKAWEL GNELSGSGVG TSISVEQYAA DIIELHGILD GIYKDYEEKP 240 LLIAPDGFFV ADWFKEFLNL TGPNIMNVVT HHFYNLGAGV DNDLVEKILN PSYLSQEAST 300 FKGLQAVLQN YGPWSKAWVG ETGGAYNSGH NLITNAFVMS FWYLDQLGMA SAFSTKSFCR 360 QSLIGGNYGL LNTTTFLPNP DYYSALLWHR LMGTRVLATN STGTEYLRAY AHCTKSYRGV 420 TLLLINLSRD TGISVQVSTG SGTSTDRNSR LEYHLTAKDG DLHSQTVLLN GNILNITPDG 480 EIPSLSAVTV PANRPILVAP LSIAFVNLPY VQFPACS 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03662 | Glyco_hydro_79n | 2.0e-177 | 32 | 348 | 317 | + 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. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ABR16706.1 | 0 | 137 | 517 | 1 | 381 | unknown [Picea sitchensis] |
| EMBL | CBI25561.1 | 0 | 8 | 516 | 5 | 532 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002283254.1 | 0 | 32 | 517 | 38 | 537 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002324603.1 | 0 | 34 | 517 | 3 | 506 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002515478.1 | 0 | 27 | 516 | 10 | 522 | heparanase, 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 | 0.000002 | 143 | 443 | 124 | 417 | A Chain A, Crystal Structure Of Hypothetical Protein Ph1004 From Pyrococcus Horikoshii Ot3 |
| PDB | 3vnz_A | 0.000002 | 143 | 443 | 124 | 417 | A Chain A, Crystal Structure Of Hypothetical Protein Ph1004 From Pyrococcus Horikoshii Ot3 |
| PDB | 3vny_A | 0.000002 | 143 | 443 | 124 | 417 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
