y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma02g12760.1 |
Family | GH79 |
Protein Properties | Length: 514 Molecular Weight: 57331.2 Isoelectric Point: 7.0943 |
Chromosome | Chromosome/Scaffold: 02 Start: 11028207 End: 11031465 |
Description | glucuronidase 1 |
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 | 37 | 505 | 0 |
DENFICATLDWWPPNKCDYNDCPWGNAGILNLDLYNDIFLNAVKAFNPLRIRLGGSLEDWLVYQFGKQRECPLFQKKNDGLFGFSKGCLPKKKWDEINHF FNKTGVKLTFGLNALSGKKPSKEDKKNWKGDWDPTNAIDLMEYTISKGYNIDSYELGNELCADGVSARIDSVQYAKDITQLRKTVNLLYQDANTRPKVLG PAGFYGKEWFDSFLQNVGHGVVDGVTHHIYNLGSGNDKDLINKIQDPYYLSQVAQTFKDVSDAVKEFEPSSGPWVGESGGAYNSGGKDVSNTFVNGFWYL DQLGMTSTFNHKVYCRQALVGGNYGLLDTTTFIPNPDYYGALLWHRLMGSKVLSVSHEGSPYLRAYVHCSKTESGIAVLLINMSNSTTFEVSLLNDMNLY PEVVFKNTQREEYHLTPKDGNIQSKVVLLNGTPLVLTQSLHIPEMKPKLVDPSSPVKVKHDSIVFVHSK |
Full Sequence |
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Protein Sequence Length: 514 Download |
MNVKTTICCV LLLLFSTSSA KDVDLRVKGV TSIATTDENF ICATLDWWPP NKCDYNDCPW 60 GNAGILNLDL YNDIFLNAVK AFNPLRIRLG GSLEDWLVYQ FGKQRECPLF QKKNDGLFGF 120 SKGCLPKKKW DEINHFFNKT GVKLTFGLNA LSGKKPSKED KKNWKGDWDP TNAIDLMEYT 180 ISKGYNIDSY ELGNELCADG VSARIDSVQY AKDITQLRKT VNLLYQDANT RPKVLGPAGF 240 YGKEWFDSFL QNVGHGVVDG VTHHIYNLGS GNDKDLINKI QDPYYLSQVA QTFKDVSDAV 300 KEFEPSSGPW VGESGGAYNS GGKDVSNTFV NGFWYLDQLG MTSTFNHKVY CRQALVGGNY 360 GLLDTTTFIP NPDYYGALLW HRLMGSKVLS VSHEGSPYLR AYVHCSKTES GIAVLLINMS 420 NSTTFEVSLL NDMNLYPEVV FKNTQREEYH LTPKDGNIQS KVVLLNGTPL VLTQSLHIPE 480 MKPKLVDPSS PVKVKHDSIV FVHSKSFNAP ACM* 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 | 9.0e-165 | 20 | 340 | 322 | + 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 | CBI27258.1 | 0 | 1 | 513 | 3 | 524 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 1 | 513 | 1 | 522 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 12 | 512 | 15 | 517 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 20 | 511 | 28 | 529 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.00000000002 | 51 | 98 | 540 | 587 | Heparanase precursor, 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 | 0.00000005 | 87 | 429 | 75 | 408 | A Chain A, The Crystal Structure Of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase |
PDB | 3vnz_A | 0.00000005 | 87 | 429 | 75 | 408 | A Chain A, The Crystal Structure Of Udp-Galnac: Polypeptide Alpha-N- Acetylgalactosaminyltransferase |
PDB | 3vny_A | 0.00000005 | 87 | 429 | 75 | 408 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |