Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.006G062200.2 |
Family | GH79 |
Protein Properties | Length: 555 Molecular Weight: 61112.2 Isoelectric Point: 8.1599 |
Chromosome | Chromosome/Scaffold: 06 Start: 4563968 End: 4567475 |
Description | glucuronidase 3 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 48 | 547 | 0 |
DEDFICATLDWWPPEKCDYGTCSWDRASLINLDLNNNILLNAIKAFSPLKIRLGGTLQDKVIYDTEDNKQPCVQFVKNTSEMFGFTQGCLPMYRWDELNA FFKKSGAEIIFGLNALAGRSITSDGSAVGAWNYTNAESFISYTVKKNYSIYGWELGNELSGSGVGTRVAAAQYASDTISLYNTVKKIYSSIEPKPLVIAP GGFFDANWFKEFVDKTGNSVNAITHHIYNLGPGVDTHLIEKILDPSYLDGEADTFNSLQSTIKSSATSAVAWVGESGGAYNSGRNLVTNAFVFSFWYLDQ LGMASAYDTKTYCRQSLIGGNYGLLNTSTFVPNPDYYSALLWHRLMGRNVLSTSFSGTKKIRAYTHCAKQSKGITLLLINLDNSTTVEVTVTFNSTRRLH QKHKPHRSHKLHKPHRSHRSHKSHKSKVIQQPQRSTSGITREEYHLTAKDGDLHSQTMLLNGNILTVNSSGDIPSLEPLHVNSSKPIMVAPFSIVFVQMP |
Full Sequence |
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Protein Sequence Length: 555 Download |
MGLCLLVCII CCSFIYVSSQ SAVAGNDNSS VSEGTVFIDG KSSIGKIDED FICATLDWWP 60 PEKCDYGTCS WDRASLINLD LNNNILLNAI KAFSPLKIRL GGTLQDKVIY DTEDNKQPCV 120 QFVKNTSEMF GFTQGCLPMY RWDELNAFFK KSGAEIIFGL NALAGRSITS DGSAVGAWNY 180 TNAESFISYT VKKNYSIYGW ELGNELSGSG VGTRVAAAQY ASDTISLYNT VKKIYSSIEP 240 KPLVIAPGGF FDANWFKEFV DKTGNSVNAI THHIYNLGPG VDTHLIEKIL DPSYLDGEAD 300 TFNSLQSTIK SSATSAVAWV GESGGAYNSG RNLVTNAFVF SFWYLDQLGM ASAYDTKTYC 360 RQSLIGGNYG LLNTSTFVPN PDYYSALLWH RLMGRNVLST SFSGTKKIRA YTHCAKQSKG 420 ITLLLINLDN STTVEVTVTF NSTRRLHQKH KPHRSHKLHK PHRSHRSHKS HKSKVIQQPQ 480 RSTSGITREE YHLTAKDGDL HSQTMLLNGN ILTVNSSGDI PSLEPLHVNS SKPIMVAPFS 540 IVFVQMPYVL PACS* |
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 | 33 | 349 | 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 | CAN81917.1 | 0 | 1 | 553 | 8 | 554 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002263173.1 | 0 | 1 | 553 | 12 | 558 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324603.1 | 0 | 34 | 554 | 1 | 506 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331013.1 | 0 | 1 | 554 | 1 | 547 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533671.1 | 0 | 2 | 553 | 9 | 550 | 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 | 0.0000002 | 143 | 439 | 122 | 409 | A Chain A, Crystal Structure Of Human Aflatoxin B1 Aldehyde Reductase Member 3 |
PDB | 3vnz_A | 0.0000002 | 143 | 439 | 122 | 409 | A Chain A, Crystal Structure Of Human Aflatoxin B1 Aldehyde Reductase Member 3 |
PDB | 3vny_A | 0.0000002 | 143 | 439 | 122 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |