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Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10003449m |
Family | GH79 |
Protein Properties | Length: 530 Molecular Weight: 58854.8 Isoelectric Point: 7.4915 |
Chromosome | Chromosome/Scaffold: 18 Start: 3364087 End: 3366979 |
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 | 46 | 522 | 0 |
DEDFICATLDWWPPQKCDYGTCAWDHASILNLDLNNTILQNAIKGGTLQDLVIYETPDQKQPCLPFTQNSSLLFGYTQGCLSLRRWNELNAFFRKTGAKV IFGLNALSGRSIKPNGEAVGAWDYTNAESFIQYIVQNNHTIDGWELGNELCGSGVGARVAANQYAIDTVALRNIVNRVYKNVSPIPLVIGPGGFFEATWF TEYFNKTENSLDATTRHIYNLGPGVDTHLIEKILNPSYLDQEAITFRSLKNIIKNSSTKAVAWVGESGGAYNSGRNLVSNAFVYSFWYLDQLGMASIYDT KTYCRQSLIGGNYGLLNTTNFTPNPDYYSALIWRTLMGRKALFTSFSGIKKIRSYTHCARQSKGITVLLMNLDNTTTVVATVELNNTFSLRHAKHRKSSQ KREISQLPWVSNGEIQREEYHLTAMDGNLHSQTMLLNGNALQISSTGDIPPLEPIHVNSTEPITIAPYSIVFVHMRT |
Full Sequence |
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Protein Sequence Length: 530 Download |
MGYRQISVTV LFLCLFQFSD NTVVSSVVEE KGTVLVYGRA AVGTIDEDFI CATLDWWPPQ 60 KCDYGTCAWD HASILNLDLN NTILQNAIKG GTLQDLVIYE TPDQKQPCLP FTQNSSLLFG 120 YTQGCLSLRR WNELNAFFRK TGAKVIFGLN ALSGRSIKPN GEAVGAWDYT NAESFIQYIV 180 QNNHTIDGWE LGNELCGSGV GARVAANQYA IDTVALRNIV NRVYKNVSPI PLVIGPGGFF 240 EATWFTEYFN KTENSLDATT RHIYNLGPGV DTHLIEKILN PSYLDQEAIT FRSLKNIIKN 300 SSTKAVAWVG ESGGAYNSGR NLVSNAFVYS FWYLDQLGMA SIYDTKTYCR QSLIGGNYGL 360 LNTTNFTPNP DYYSALIWRT LMGRKALFTS FSGIKKIRSY THCARQSKGI TVLLMNLDNT 420 TTVVATVELN NTFSLRHAKH RKSSQKREIS QLPWVSNGEI QREEYHLTAM DGNLHSQTML 480 LNGNALQISS TGDIPPLEPI HVNSTEPITI APYSIVFVHM RTVVVPACA* 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 | 0 | 29 | 338 | 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 |
DDBJ | BAB10787.1 | 0 | 1 | 529 | 1 | 536 | unnamed protein product [Arabidopsis thaliana] |
EMBL | CBI25561.1 | 0 | 31 | 528 | 29 | 532 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_851092.1 | 0 | 128 | 529 | 1 | 401 | AtGUS3 (Arabidopsis thaliana glucuronidase 3); beta-glucuronidase |
RefSeq | NP_851093.1 | 0 | 1 | 529 | 1 | 536 | AtGUS3 (Arabidopsis thaliana glucuronidase 3); beta-glucuronidase |
RefSeq | XP_002324603.1 | 0 | 32 | 529 | 1 | 506 | predicted protein [Populus trichocarpa] |
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 | 0.0000008 | 132 | 378 | 122 | 357 | X Chain X, Crystal Structure Of The Full-Length Autotransporter Esta From Pseudomonas Aeruginosa |
PDB | 3vnz_A | 0.0000008 | 132 | 378 | 122 | 357 | X Chain X, Crystal Structure Of The Full-Length Autotransporter Esta From Pseudomonas Aeruginosa |
PDB | 3vny_A | 0.0000008 | 132 | 378 | 122 | 357 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |