Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.011G284500.1 |
Family | GH79 |
Protein Properties | Length: 479 Molecular Weight: 53642.3 Isoelectric Point: 8.3719 |
Chromosome | Chromosome/Scaffold: 11 Start: 61696410 End: 61698735 |
Description | glucuronidase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 38 | 235 | 0 |
DEDFICVTLDWWPTNKCDYDQCPWGQAGLFNSDLKNKILEKAVKAFHPLRIRVGGSLQDQNCQPFQKQDKGFLFGFSIGCLDMKRWDELNEFFNQTRAKV TFGLNALIGRKESKTEKTLWVGDWYSHNARDLMSYTISKGYKIDSYELGNELCGVGVSARIEAKQYAKDMATLKNLVKEMYPNPKTQPKILGPGGNNP | |||
GH79 | 237 | 471 | 0 |
VVRRVQDPFFLTQIAQTFKDVSNAIDKFAPWSGAWVSESGGAYNSGGQLVSYTFAFGFWYLDQLGMTSVYNHKVYCRQALTGGNYALLKTTTFVPNPDYY GALLWHRVMGSKVLSVTHKGSPYLRVYSHCAKKEPGVSFVFINLSKNTSFEINLYHDQNLNGGSPNFEFKGHKKREEYHLTPKDGNILSSIVLLNGTPLE LSDSLEIPELKPKLVDGLKTISIATHSIAFVTIID |
Full Sequence |
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Protein Sequence Length: 479 Download |
MNFKSITFFV VFLSCLLVSK AEKVEVVVEG ATPNAQTDED FICVTLDWWP TNKCDYDQCP 60 WGQAGLFNSD LKNKILEKAV KAFHPLRIRV GGSLQDQNCQ PFQKQDKGFL FGFSIGCLDM 120 KRWDELNEFF NQTRAKVTFG LNALIGRKES KTEKTLWVGD WYSHNARDLM SYTISKGYKI 180 DSYELGNELC GVGVSARIEA KQYAKDMATL KNLVKEMYPN PKTQPKILGP GGNNPDVVRR 240 VQDPFFLTQI AQTFKDVSNA IDKFAPWSGA WVSESGGAYN SGGQLVSYTF AFGFWYLDQL 300 GMTSVYNHKV YCRQALTGGN YALLKTTTFV PNPDYYGALL WHRVMGSKVL SVTHKGSPYL 360 RVYSHCAKKE PGVSFVFINL SKNTSFEINL YHDQNLNGGS PNFEFKGHKK REEYHLTPKD 420 GNILSSIVLL NGTPLELSDS LEIPELKPKL VDGLKTISIA THSIAFVTII DFNAPACS* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 1.0e-136 | 30 | 301 | 314 | + 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 | 10 | 477 | 13 | 523 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 10 | 477 | 11 | 521 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 5 | 478 | 7 | 518 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 21 | 476 | 28 | 529 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.0000000000005 | 51 | 97 | 539 | 585 | Heparanase precursor, putative [Ricinus communis] |