y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.011G285000.1 |
Family | GH79 |
Protein Properties | Length: 521 Molecular Weight: 58498.7 Isoelectric Point: 7.5518 |
Chromosome | Chromosome/Scaffold: 11 Start: 61752467 End: 61754716 |
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 | 514 | 0 |
DEDFICVTLDWWPTNKCDYDQCPWGQAGLFNLDLKNKILEKAVKAFHPLRIRVGGSLQDQVVYNVRNNIENCQPFQKQDKGFLFGFSIGCLDMKRWDELN EFFNQTRAKVTFGLNALIGRKESETEKTLWVGDWYSHNARDLMSYTISKGYKIDSYELGNELCGVGVSARIEAKQYAKDMATLKNLVKEMYPNPKTQPKV LGPGGFYDKKWFDTFLDASGHDVIDGVTHHIYNLGPGNNPDVVRRVQDPFFLTQIAQTFKDVSNAIVKFAPWSGAWVSESGGAYNSGGQLVSYTFAFGFW YLDQLGMTSVYNHKVYCRQALIGGNYALLNTTTFVPNPDYYGALLWHRVMGSKVLSVTHKGSPYLRVYSHCAKKEPGVSFVFINLSKNTSFEIDLFHDLN LNGGSPNFEFKGHKKREEYHLTPKDGNILSSIVLLNGTPLELSDSLEIPELKPKLVDGLKPISIAAHSIAFVTIRDF |
Full Sequence |
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Protein Sequence Length: 521 Download |
MNFKSITFFV VFLSCLLVSK AEKVEVVVEG ATSIAQTDED FICVTLDWWP TNKCDYDQCP 60 WGQAGLFNLD LKNKILEKAV KAFHPLRIRV GGSLQDQVVY NVRNNIENCQ PFQKQDKGFL 120 FGFSIGCLDM KRWDELNEFF NQTRAKVTFG LNALIGRKES ETEKTLWVGD WYSHNARDLM 180 SYTISKGYKI DSYELGNELC GVGVSARIEA KQYAKDMATL KNLVKEMYPN PKTQPKVLGP 240 GGFYDKKWFD TFLDASGHDV IDGVTHHIYN LGPGNNPDVV RRVQDPFFLT QIAQTFKDVS 300 NAIVKFAPWS GAWVSESGGA YNSGGQLVSY TFAFGFWYLD QLGMTSVYNH KVYCRQALIG 360 GNYALLNTTT FVPNPDYYGA LLWHRVMGSK VLSVTHKGSP YLRVYSHCAK KEPGVSFVFI 420 NLSKNTSFEI DLFHDLNLNG GSPNFEFKGH KKREEYHLTP KDGNILSSIV LLNGTPLELS 480 DSLEIPELKP KLVDGLKPIS IAAHSIAFVT IRDFNAPAFS * 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 | 4.0e-172 | 30 | 343 | 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 | 517 | 13 | 521 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 10 | 517 | 11 | 519 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 5 | 518 | 7 | 516 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 21 | 519 | 28 | 530 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.00000000000002 | 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 | 0.00000002 | 134 | 406 | 122 | 383 | A Chain A, The Structure Of Alpha-N-Acetylgalactosaminidase |
PDB | 3vnz_A | 0.00000002 | 134 | 406 | 122 | 383 | A Chain A, The Structure Of Alpha-N-Acetylgalactosaminidase |
PDB | 3vny_A | 0.00000002 | 134 | 406 | 122 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |