Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s121_77V6.1 |
Family | GH79 |
Protein Properties | Length: 527 Molecular Weight: 57864.4 Isoelectric Point: 5.9258 |
Chromosome | Chromosome/Scaffold: 121 Start: 532208 End: 535937 |
Description | glucuronidase 3 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 31 | 520 | 0 |
TTYLCATLDWYPQDRCNYGSCSWDHASILYIDLSNSLLEKSLVALSPLRLRLGGTVQDQIVYDTKLGSLAQPCLPLVKDDSFISDYRGGCLSMERWIALT NLFARTGTLPAFGLNALYNRNRSADGVWGPWDPSNAHDFIKFTVDHGIFVEAWELGNELTMNHVVTSIPAKQYAQDVKQLRSIITTLYKGHSQQPLLVAP DSTGNVAGNEYDWYITFLNESGPGVLDGISRHIYNLGPGNSLDLVEKILNYTILDNDLDNYRAVQRLIQTYGPWATAWVGEAGGAYNSGKNLVSNAFVNS FWYLDQLGLAATFNTKAYCRQTLIGGNYGLLNSTTFRPNPDLYSAILWKRLMGRIVLATKLKDAYPQLRSYTHCQAGSKTGGLTVLLINLSNATLSVVVD IKSPFVGEPVSSKNKMSGLIPNKSKVTLRHEYHLSASNGDPHSQTSLLNGTPLELTPLGDLPNLDPVVTENISPVSIRAFSIAFVALPDA |
Full Sequence |
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Protein Sequence Length: 527 Download |
MNSTATQDSH EDGLHLQVEV DGRSVMATTD TTYLCATLDW YPQDRCNYGS CSWDHASILY 60 IDLSNSLLEK SLVALSPLRL RLGGTVQDQI VYDTKLGSLA QPCLPLVKDD SFISDYRGGC 120 LSMERWIALT NLFARTGTLP AFGLNALYNR NRSADGVWGP WDPSNAHDFI KFTVDHGIFV 180 EAWELGNELT MNHVVTSIPA KQYAQDVKQL RSIITTLYKG HSQQPLLVAP DSTGNVAGNE 240 YDWYITFLNE SGPGVLDGIS RHIYNLGPGN SLDLVEKILN YTILDNDLDN YRAVQRLIQT 300 YGPWATAWVG EAGGAYNSGK NLVSNAFVNS FWYLDQLGLA ATFNTKAYCR QTLIGGNYGL 360 LNSTTFRPNP DLYSAILWKR LMGRIVLATK LKDAYPQLRS YTHCQAGSKT GGLTVLLINL 420 SNATLSVVVD IKSPFVGEPV SSKNKMSGLI PNKSKVTLRH EYHLSASNGD PHSQTSLLNG 480 TPLELTPLGD LPNLDPVVTE NISPVSIRAF SIAFVALPDA QVPEYL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 7.0e-135 | 18 | 338 | 324 | + 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_001767170.1 | 0 | 16 | 520 | 35 | 530 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769830.1 | 0 | 4 | 522 | 39 | 553 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001770123.1 | 0 | 1 | 523 | 1 | 523 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001774747.1 | 0 | 3 | 523 | 4 | 521 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002284470.1 | 0 | 18 | 523 | 27 | 536 | PREDICTED: hypothetical protein [Vitis vinifera] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DC935183 | 232 | 43 | 274 | 0 |
BY958882 | 221 | 14 | 231 | 0 |
BY957919 | 206 | 14 | 219 | 0 |
DC949310 | 198 | 326 | 523 | 0 |
DC952372 | 186 | 338 | 523 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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