| Basic Information | |
|---|---|
| Species | Picea abies |
| Cazyme ID | MA_854085g0010 |
| Family | GH79 |
| Protein Properties | Length: 369 Molecular Weight: 41074.8 Isoelectric Point: 9.5869 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH79 | 4 | 361 | 0 |
| TSVAFGLNALNGRQMKPSGITGPWDSSNARDFIQYTVDHGYKIEAWEFGNELSGRDVGSNVPAEQYSADVIELHGILKEVYKNQIAKPLLVAPDGYFDAD WFKELIQRTGPKILDVVTHHIYNLGAGVDKSLVEKILDPSFLSQEAFTFKSLQSILKNYGPWAKAWVGESGGAYNSGRNLVTNAFVCSFWYLDQLGMSSK FNTTSYCRQSLIGGNYGLLNTTTFVPNPDYYSALLWHRLMGTRVLATTSEGTKYLRAYAHCAKNAKGVTLLLINFSNHTRVSVRAFTGSGTSTQRKSRFE YHLTAKDGDLHSQTILLNGKILDITAEGEIPSLKAVRIRARRRIYLAPLSIAFVHLPH | |||
| Full Sequence |
|---|
| Protein Sequence Length: 369 Download |
| GYFTSVAFGL NALNGRQMKP SGITGPWDSS NARDFIQYTV DHGYKIEAWE FGNELSGRDV 60 GSNVPAEQYS ADVIELHGIL KEVYKNQIAK PLLVAPDGYF DADWFKELIQ RTGPKILDVV 120 THHIYNLGAG VDKSLVEKIL DPSFLSQEAF TFKSLQSILK NYGPWAKAWV GESGGAYNSG 180 RNLVTNAFVC SFWYLDQLGM SSKFNTTSYC RQSLIGGNYG LLNTTTFVPN PDYYSALLWH 240 RLMGTRVLAT TSEGTKYLRA YAHCAKNAKG VTLLLINFSN HTRVSVRAFT GSGTSTQRKS 300 RFEYHLTAKD GDLHSQTILL NGKILDITAE GEIPSLKAVR IRARRRIYLA PLSIAFVHLP 360 HVRIPACSR 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03662 | Glyco_hydro_79n | 1.0e-104 | 6 | 199 | 195 | + 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 | 6 | 368 | 18 | 381 | unknown [Picea sitchensis] |
| EMBL | CBI25561.1 | 0 | 6 | 367 | 152 | 532 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002263173.1 | 0 | 6 | 367 | 163 | 558 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002324603.1 | 0 | 6 | 368 | 123 | 506 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002533671.1 | 0 | 6 | 367 | 161 | 550 | heparanase, putative [Ricinus communis] |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EX309526 | 298 | 68 | 365 | 0 |
| GR954317 | 252 | 117 | 368 | 0 |
| EX428547 | 252 | 6 | 256 | 0 |
| EX353120 | 283 | 6 | 286 | 0 |
| EX428547 | 39 | 248 | 286 | 0.00002 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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