Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.006G004300.1 |
Family | GH79 |
Protein Properties | Length: 516 Molecular Weight: 57368.6 Isoelectric Point: 8.1378 |
Chromosome | Chromosome/Scaffold: 06 Start: 888644 End: 891069 |
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 | 509 | 0 |
DDNFVCATLDWWPTEKCNYNQCPWGKAGLLNLDLKKKVLINAIKAFNSLRIKVGGSLQDQVVYGVGEVKNCPNFMKKEGSLFGFSQGCLPVERWDELNNY FNQTGVKVTFGLNALLGRNESQSEKGLWVGDWNSQNARNLMKYTISRGYKVDSYEFGNQLSGAGMGARVEAEQYGKDVIVLKNMVKELHPDPKTQPKVLG PSGFYDEKWFNSLLKVSVQEVVDRVTHHIYNLGPGDDLNLITKIQDPSGVFNIVNKFKPQSGAWVSESGGALQGGAKDVSPTFADGFWYFDQLGIASTYN HKVFCRQTLIGGNYALLDTTTFIPNPDYYGALLWHRLMGSIVLAVTQESNPNLRVYAHCAKKKLGISIIFINLSNDSTFDVTLSSYEHRRRNLRPTDAAK PKFEFRSHLNREEYHLTALGGNIQGQIVLLNDVPMVLTDTFDIPAMDPKLVNASTPISVAAHSIVYVTIRDF |
Full Sequence |
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Protein Sequence Length: 516 Download |
MDLKCIFGLV IIVSRISLSF TQNVNVVIQG SKSVAEIDDN FVCATLDWWP TEKCNYNQCP 60 WGKAGLLNLD LKKKVLINAI KAFNSLRIKV GGSLQDQVVY GVGEVKNCPN FMKKEGSLFG 120 FSQGCLPVER WDELNNYFNQ TGVKVTFGLN ALLGRNESQS EKGLWVGDWN SQNARNLMKY 180 TISRGYKVDS YEFGNQLSGA GMGARVEAEQ YGKDVIVLKN MVKELHPDPK TQPKVLGPSG 240 FYDEKWFNSL LKVSVQEVVD RVTHHIYNLG PGDDLNLITK IQDPSGVFNI VNKFKPQSGA 300 WVSESGGALQ GGAKDVSPTF ADGFWYFDQL GIASTYNHKV FCRQTLIGGN YALLDTTTFI 360 PNPDYYGALL WHRLMGSIVL AVTQESNPNL RVYAHCAKKK LGISIIFINL SNDSTFDVTL 420 SSYEHRRRNL RPTDAAKPKF EFRSHLNREE YHLTALGGNI QGQIVLLNDV PMVLTDTFDI 480 PAMDPKLVNA STPISVAAHS IVYVTIRDFH APVCV* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam03662 | Glyco_hydro_79n | 4.0e-156 | 22 | 331 | 321 | + 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 | 6 | 515 | 9 | 524 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 6 | 515 | 7 | 522 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 8 | 515 | 3 | 518 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 24 | 513 | 31 | 529 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.0000000000004 | 51 | 99 | 539 | 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 | 0.0008 | 129 | 413 | 119 | 403 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 3vnz_A | 0.0008 | 129 | 413 | 119 | 403 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
PDB | 3vny_A | 0.0008 | 129 | 413 | 119 | 403 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |