y
Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa003804m |
Family | GH79 |
Protein Properties | Length: 548 Molecular Weight: 60830.4 Isoelectric Point: 9.537 |
Chromosome | Chromosome/Scaffold: 5 Start: 16130335 End: 16133452 |
Description | glucuronidase 2 |
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 | 45 | 539 | 0 |
DNNFICATIDWWNHEKCDYNQCPWGSASALNLNLSHPLLAKSIQAFNQLRIRIGGSLEDQLLYDVGNLKYPCHPFRKKSHGLFGFSRGCLPMSRWDELNQ FFSKTRPIVTFSLNALSGRHHKSGGVWVGDWDSSNAYDFINYTVLKGYQIDSWEFGNELSGRGIGASVGAEQYGKDLIKLKHIINQLYNKSRTKPALVAP GGFYDQGWFAKLLQVSGSGIVNVITQHMYNLGAGVDPKLVSRILNPGYLDLASGTFHDLEQTVKKNGPWASIWVGESGGAYNSGGRNVSDTFVNSFWYLD QLGMSAKYNTRVYCRQSLVGGNYGLLNRTSFVPNPDYYSALLWHRLMGQGVLAVNSNASADLRTYAHCARGRAGVTVVLINLSNDTDFIVNVENILDFNL GAHERNISKESYFKRSLKKTVSWVGRKALDKPVYREEYHLTPKNRNLRSKTMVLNGAPLEITKDGNIPELEPARVLANSPLTISPLSIKFVVLPY |
Full Sequence |
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Protein Sequence Length: 548 Download |
MEFRLSLVLI LVSLPAILAQ DVGNTKKAGN VKVVVNGILA IARVDNNFIC ATIDWWNHEK 60 CDYNQCPWGS ASALNLNLSH PLLAKSIQAF NQLRIRIGGS LEDQLLYDVG NLKYPCHPFR 120 KKSHGLFGFS RGCLPMSRWD ELNQFFSKTR PIVTFSLNAL SGRHHKSGGV WVGDWDSSNA 180 YDFINYTVLK GYQIDSWEFG NELSGRGIGA SVGAEQYGKD LIKLKHIINQ LYNKSRTKPA 240 LVAPGGFYDQ GWFAKLLQVS GSGIVNVITQ HMYNLGAGVD PKLVSRILNP GYLDLASGTF 300 HDLEQTVKKN GPWASIWVGE SGGAYNSGGR NVSDTFVNSF WYLDQLGMSA KYNTRVYCRQ 360 SLVGGNYGLL NRTSFVPNPD YYSALLWHRL MGQGVLAVNS NASADLRTYA HCARGRAGVT 420 VVLINLSNDT DFIVNVENIL DFNLGAHERN ISKESYFKRS LKKTVSWVGR KALDKPVYRE 480 EYHLTPKNRN LRSKTMVLNG APLEITKDGN IPELEPARVL ANSPLTISPL SIKFVVLPYF 540 DAQYACA* 600 |
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 | 40 | 347 | 308 | + 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 |
EMBL | CBI15157.1 | 0 | 12 | 547 | 12 | 513 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 1 | 547 | 1 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 12 | 547 | 12 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002321464.1 | 0 | 1 | 547 | 1 | 541 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514696.1 | 0 | 15 | 547 | 15 | 539 | Heparanase-2, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vo0_A | 0.00002 | 265 | 439 | 235 | 411 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 3vnz_A | 0.00002 | 265 | 439 | 235 | 411 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 3vny_A | 0.00002 | 265 | 439 | 235 | 411 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |