y
Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_002_00770.2 |
Family | GH79 |
Protein Properties | Length: 540 Molecular Weight: 59794.4 Isoelectric Point: 8.987 |
Chromosome | Chromosome/Scaffold: 2 Start: 5902115 End: 5906284 |
Description | glucuronidase 2 |
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 | 39 | 533 | 0 |
DDQFICATLDWWPSDKCNYHDCPWGKSGVPYLDLSHPTFAKAIQAFGHLRIRIGGSLQDKVVYNVGALKYPCHPFKKMDKWLFGFTKGCLYMSRWDELNL LLSKTGAIVTFGLNALYGRHKTGKVAWGGAWDSSNAREFIKYTVSKGYHIDSWELGNELSEPAVGASVSAEQYGKDMIELNAIIKEIYKNSHSRPLILAP GGFFSASWYAKLLEISGPNVVNAVTHHLYNLGPGNDPHLVDRILDPHYLSQSTSDTFQKLQQTIKVHGPWASAWVGESGGAYNSGGRHVSNTFVDSFWYL DQLGMASKYNTKVYCRQTLIGGNYGLLNTTTFTPNPDYYSALFWHRLMGKGVLSVDSKASAHLRVYAHCSKSRAGITVLLINLSNQTSFKILVQNDMSFN LKVEDRIHTGGSFMHGLKKTVSWVGRKASDVTALREEYHLTPDGHLRSQTMLLNGKPLKLTETGDIPTLDPVLVDVRSHISIAPLSISFIAFPKF |
Full Sequence |
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Protein Sequence Length: 540 Download |
MGFVLPLFVF VAYLYGVSAQ GPTYATIIVK SAAKIAETDD QFICATLDWW PSDKCNYHDC 60 PWGKSGVPYL DLSHPTFAKA IQAFGHLRIR IGGSLQDKVV YNVGALKYPC HPFKKMDKWL 120 FGFTKGCLYM SRWDELNLLL SKTGAIVTFG LNALYGRHKT GKVAWGGAWD SSNAREFIKY 180 TVSKGYHIDS WELGNELSEP AVGASVSAEQ YGKDMIELNA IIKEIYKNSH SRPLILAPGG 240 FFSASWYAKL LEISGPNVVN AVTHHLYNLG PGNDPHLVDR ILDPHYLSQS TSDTFQKLQQ 300 TIKVHGPWAS AWVGESGGAY NSGGRHVSNT FVDSFWYLDQ LGMASKYNTK VYCRQTLIGG 360 NYGLLNTTTF TPNPDYYSAL FWHRLMGKGV LSVDSKASAH LRVYAHCSKS RAGITVLLIN 420 LSNQTSFKIL VQNDMSFNLK VEDRIHTGGS FMHGLKKTVS WVGRKASDVT ALREEYHLTP 480 DGHLRSQTML LNGKPLKLTE TGDIPTLDPV LVDVRSHISI APLSISFIAF PKFEAPACL* 540 600 |
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 | 25 | 342 | 318 | + 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 | CAB62595.1 | 0 | 19 | 538 | 2 | 520 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 1 | 538 | 1 | 512 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 1 | 538 | 1 | 542 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 1 | 538 | 1 | 538 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514696.1 | 0 | 17 | 538 | 17 | 538 | Heparanase-2, putative [Ricinus communis] |