y
Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.003G171800.2 |
Family | GH79 |
Protein Properties | Length: 513 Molecular Weight: 56466.7 Isoelectric Point: 8.6669 |
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 | 506 | 0 |
DNDFICATLDWWPPQKCDYGKCSWGQASLLNLDLNSKTLLNAIKAFSSLKLRLGGTLQDKVIYGTEDNRQPCTPFVKADEMFGFTGGCLPMSRVKAIFGL NALAGKSIKSGFAVGPWNYTNAESLIRYTVRKKYHIHGWELGNELCGNGIGVSVTADQYASDVVALRNIVQSAYRGIEPKPLVVAPGGFFEFNWFKEFIS KYNKSADVITHHIYNLGPGVDDHITERILDPFYLDGEANTFNRLKGILQSSSSHKVKSWVGESGGAYNSGHHLVSDAFVNSFWYLDQLGMSAVYDTTTYC RQTLIGGNYGLLNTSTFMPNPDYYSALLWHRLMGGRVLSTTFYGTKKIRSYAHCAKESKGITILLLNLDNSTSVQVNVDLTFNKLPHHRVDEPARREYHL TAPDRNIHSQIMLLNGKALSVNSAGEIPPLEPVYVDSTKPITVGPLSIVFAHIPNV |
Full Sequence |
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Protein Sequence Length: 513 Download |
MGCQIRLLGL CLWMYLASLS FIGVGAVYGR GGAVEKGIVL VHGKSAIGRI DNDFICATLD 60 WWPPQKCDYG KCSWGQASLL NLDLNSKTLL NAIKAFSSLK LRLGGTLQDK VIYGTEDNRQ 120 PCTPFVKADE MFGFTGGCLP MSRVKAIFGL NALAGKSIKS GFAVGPWNYT NAESLIRYTV 180 RKKYHIHGWE LGNELCGNGI GVSVTADQYA SDVVALRNIV QSAYRGIEPK PLVVAPGGFF 240 EFNWFKEFIS KYNKSADVIT HHIYNLGPGV DDHITERILD PFYLDGEANT FNRLKGILQS 300 SSSHKVKSWV GESGGAYNSG HHLVSDAFVN SFWYLDQLGM SAVYDTTTYC RQTLIGGNYG 360 LLNTSTFMPN PDYYSALLWH RLMGGRVLST TFYGTKKIRS YAHCAKESKG ITILLLNLDN 420 STSVQVNVDL TFNKLPHHRV DEPARREYHL TAPDRNIHSQ IMLLNGKALS VNSAGEIPPL 480 EPVYVDSTKP ITVGPLSIVF AHIPNVLLSA CR* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 1.0e-162 | 35 | 339 | 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 | 511 | 1 | 524 | unknown [Glycine max] |
EMBL | CAN81917.1 | 0 | 1 | 512 | 1 | 555 | hypothetical protein [Vitis vinifera] |
EMBL | CBI25561.1 | 0 | 8 | 512 | 1 | 533 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263173.1 | 0 | 1 | 512 | 5 | 559 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002533671.1 | 0 | 1 | 512 | 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 | 0.000001 | 145 | 427 | 134 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vnz_A | 0.000001 | 145 | 427 | 134 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vny_A | 0.000001 | 145 | 427 | 134 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |