Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.N021000.1 |
Family | GH79 |
Protein Properties | Length: 502 Molecular Weight: 56076.8 Isoelectric Point: 6.5094 |
Chromosome | Chromosome/Scaffold: 357 Start: 2409 End: 4932 |
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 | 495 | 0 |
DDNFVCATLDWWPTEKCNYNQCPWGKAGLLNLDLKRKVLINAIKAFNSLRIKVGGSLQDQVVDGVGEVKNCPNFMKKEGSLFGFSQGCLPVERWDELNNF FNQTGWVTFGLNALLGRNESQSEKCLWVGDWNSQNARDFMKYTISRGYKVDSYEFGNQLSGARMGARVEAEQYGKDVIVLKNMVKELHPDPKTQPKVLGP SGFYDEKWFNSFLEVLGQEVVDGVTHHIYNLGPGDDLNLITKIQDPSCLNQVAQTYRGVFNIVNKFKPQSGAWVSESGGALQGGAKDVSPTFADGFWQTL IGGNYALLDTTTFIPNPDYYGALLWHRLMGSIVLAVTQESNPNLRVYAHSRDFYIFINLSNDSTFDVTLSSYEHRRRNLRPTDAAKPKFEFRSHLNREEY HLTALGGNIQGQIVLLNDVPMVLTDIFDIPAMDPKLVNASTPISVAAHSIVYLTIRDF |
Full Sequence |
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Protein Sequence Length: 502 Download |
MDLKCIFGLV IIVSRISLSF TQNVNVVIQG SKSVAEIDDN FVCATLDWWP TEKCNYNQCP 60 WGKAGLLNLD LKRKVLINAI KAFNSLRIKV GGSLQDQVVD GVGEVKNCPN FMKKEGSLFG 120 FSQGCLPVER WDELNNFFNQ TGWVTFGLNA LLGRNESQSE KCLWVGDWNS QNARDFMKYT 180 ISRGYKVDSY EFGNQLSGAR MGARVEAEQY GKDVIVLKNM VKELHPDPKT QPKVLGPSGF 240 YDEKWFNSFL EVLGQEVVDG VTHHIYNLGP GDDLNLITKI QDPSCLNQVA QTYRGVFNIV 300 NKFKPQSGAW VSESGGALQG GAKDVSPTFA DGFWQTLIGG NYALLDTTTF IPNPDYYGAL 360 LWHRLMGSIV LAVTQESNPN LRVYAHSRDF YIFINLSNDS TFDVTLSSYE HRRRNLRPTD 420 AAKPKFEFRS HLNREEYHLT ALGGNIQGQI VLLNDVPMVL TDIFDIPAMD PKLVNASTPI 480 SVAAHSIVYL TIRDFHAPVC V* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 3.0e-155 | 22 | 334 | 315 | + 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 | 501 | 9 | 524 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 6 | 501 | 7 | 522 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 8 | 501 | 3 | 518 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 24 | 499 | 31 | 529 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.0000000000005 | 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 | 0.0006 | 129 | 407 | 119 | 409 | A Chain A, Distal Heme Pocket Mutant (r38s/h42e) Of Recombinant Horseradish Peroxidase C (hrp |
PDB | 3vnz_A | 0.0006 | 129 | 407 | 119 | 409 | A Chain A, Distal Heme Pocket Mutant (r38s/h42e) Of Recombinant Horseradish Peroxidase C (hrp |
PDB | 3vny_A | 0.0006 | 129 | 407 | 119 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |