Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.003G171800.1 |
Family | GH79 |
Protein Properties | Length: 525 Molecular Weight: 57890.3 Isoelectric Point: 8.5566 |
Chromosome | Chromosome/Scaffold: 03 Start: 38277301 End: 38280551 |
Description | glucuronidase 3 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 51 | 518 | 0 |
DNDFICATLDWWPPQKCDYGKCSWGQASLLNLDLNSKTLLNAIKAFSSLKLRLGGTLQDKVIYGTEDNRQPCTPFVKADEMFGFTGGCLPMSRWDELNSF FQKAGVKAIFGLNALAGKSIKSGFAVGPWNYTNAESLIRYTVRKKYHIHGWELGNELCGNGIGVSVTADQYASDVVALRNIVQSAYRGIEPKPLVVAPGG FFEFNWFKEFISKYNKSADVITHHIYNLGPGVDDHITERILDPFYLDGEANTFNRLKGILQSSSSHKVKSWVGESGGAYNSGHHLVSDAFVNSFWYLDQL GMSAVYDTTTYCRQTLIGGNYGLLNTSTFMPNPDYYSALLWHRLMGGRVLSTTFYGTKKIRSYAHCAKESKGITILLLNLDNSTSVQVNVDLTFNKLPHH RVDEPARREYHLTAPDRNIHSQIMLLNGKALSVNSAGEIPPLEPVYVDSTKPITVGPLSIVFAHIPNV |
Full Sequence |
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Protein Sequence Length: 525 Download |
MGCQIRLLGL CLWMYLASLS FIGVGAVYGR GGAVEKGIVL VHGKSAIGRI DNDFICATLD 60 WWPPQKCDYG KCSWGQASLL NLDLNSKTLL NAIKAFSSLK LRLGGTLQDK VIYGTEDNRQ 120 PCTPFVKADE MFGFTGGCLP MSRWDELNSF FQKAGVKAIF GLNALAGKSI KSGFAVGPWN 180 YTNAESLIRY TVRKKYHIHG WELGNELCGN GIGVSVTADQ YASDVVALRN IVQSAYRGIE 240 PKPLVVAPGG FFEFNWFKEF ISKYNKSADV ITHHIYNLGP GVDDHITERI LDPFYLDGEA 300 NTFNRLKGIL QSSSSHKVKS WVGESGGAYN SGHHLVSDAF VNSFWYLDQL GMSAVYDTTT 360 YCRQTLIGGN YGLLNTSTFM PNPDYYSALL WHRLMGGRVL STTFYGTKKI RSYAHCAKES 420 KGITILLLNL DNSTSVQVNV DLTFNKLPHH RVDEPARREY HLTAPDRNIH SQIMLLNGKA 480 LSVNSAGEIP PLEPVYVDST KPITVGPLSI VFAHIPNVLL SACR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 3.0e-175 | 35 | 351 | 320 | + 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 |
GenBank | ACU20377.1 | 0 | 1 | 523 | 1 | 524 | unknown [Glycine max] |
EMBL | CAN81917.1 | 0 | 1 | 524 | 1 | 555 | hypothetical protein [Vitis vinifera] |
EMBL | CBI25561.1 | 0 | 8 | 524 | 1 | 533 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263173.1 | 0 | 1 | 524 | 5 | 559 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002533671.1 | 0 | 1 | 524 | 1 | 551 | heparanase, 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 | 0.000000005 | 145 | 439 | 122 | 409 | A Chain A, Higher-density Crystal Structure Of Potato Endo-1,3-beta-glucanase |
PDB | 3vnz_A | 0.000000005 | 145 | 439 | 122 | 409 | A Chain A, Higher-density Crystal Structure Of Potato Endo-1,3-beta-glucanase |
PDB | 3vny_A | 0.000000005 | 145 | 439 | 122 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |