y
Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10013186m |
Family | GH79 |
Protein Properties | Length: 544 Molecular Weight: 60185.7 Isoelectric Point: 8.6731 |
Chromosome | Chromosome/Scaffold: 2 Start: 2505148 End: 2508689 |
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 | 43 | 537 | 0 |
DENFVCATLDWWPHDKCNYDNCPWGYSSVINMDLSRPLLAKAVQAFKPLRIRIGGSLQDQVIYDVGNLKTPCRPFRKMNSGLFGFSKGCLHMKRWDELNS FLTETGAIVTFGLNALHGRHKLRGNAWGGAWNHINTQDFINYTVSKGYAIDSWEFGNELSGNGVGASVSAELYGKDLIVLREVINKVYKDSQLTKPSLVA PGGFYEQQWYSKLLQISGPGVVDVVTHHIYNLGSGNDPELVKKILNPSYLSKISETFKNVNQTIQEHGPWASPWVGESGGAYNSGGRHVSDTFIDSFWYL DQLGMSSKHNTKVYCRQTLVGGFYGLLEKGTFVPNPDYYSALLWHRLMGKGVLAVRSDGPPHLRVYAHCSKGRAGVTMLLINLSNQTCFTVSVSNGVNIV LNAESKQRKKSLLDTLKKPFSWIGSKASDGYLNREEYHLTPENGDFRSKTMNLNGKPLKPTATGDIPNLEPVLRGVNSPVNVLPLSMSFIVLPNF |
Full Sequence |
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Protein Sequence Length: 544 Download |
MGFKVCFFVF LSCLLLVPET TMAQDVKHAS IVIEGASRIS ETDENFVCAT LDWWPHDKCN 60 YDNCPWGYSS VINMDLSRPL LAKAVQAFKP LRIRIGGSLQ DQVIYDVGNL KTPCRPFRKM 120 NSGLFGFSKG CLHMKRWDEL NSFLTETGAI VTFGLNALHG RHKLRGNAWG GAWNHINTQD 180 FINYTVSKGY AIDSWEFGNE LSGNGVGASV SAELYGKDLI VLREVINKVY KDSQLTKPSL 240 VAPGGFYEQQ WYSKLLQISG PGVVDVVTHH IYNLGSGNDP ELVKKILNPS YLSKISETFK 300 NVNQTIQEHG PWASPWVGES GGAYNSGGRH VSDTFIDSFW YLDQLGMSSK HNTKVYCRQT 360 LVGGFYGLLE KGTFVPNPDY YSALLWHRLM GKGVLAVRSD GPPHLRVYAH CSKGRAGVTM 420 LLINLSNQTC FTVSVSNGVN IVLNAESKQR KKSLLDTLKK PFSWIGSKAS DGYLNREEYH 480 LTPENGDFRS KTMNLNGKPL KPTATGDIPN LEPVLRGVNS PVNVLPLSMS FIVLPNFDAS 540 ACS* 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 | 29 | 346 | 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 |
DDBJ | BAB08480.1 | 0 | 26 | 543 | 1 | 516 | unnamed protein product [Arabidopsis thaliana] |
EMBL | CAB62595.1 | 0 | 22 | 543 | 1 | 521 | putative protein [Arabidopsis thaliana] |
RefSeq | NP_196400.2 | 0 | 1 | 543 | 1 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | NP_200933.2 | 0 | 1 | 543 | 1 | 539 | AtGUS1 (Arabidopsis thaliana glucuronidase 1); beta-glucuronidase |
RefSeq | XP_002514696.1 | 0 | 22 | 543 | 18 | 539 | Heparanase-2, putative [Ricinus communis] |