Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.004G293000.1 |
Family | GH79 |
Protein Properties | Length: 533 Molecular Weight: 57932.8 Isoelectric Point: 8.2308 |
Chromosome | Chromosome/Scaffold: 04 Start: 62070377 End: 62073071 |
Description | glucuronidase 3 |
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 | 48 | 524 | 0 |
DDNFICATLDWWAPNKCDYGTCSWERSSLLNLIRMGGTLQDKVIYETKDDKSPCAPFVKNSSEMFGFSKGCLPMSRWDQLNVFFKKAGAMVVFGLNALNG KAIGSDGSATGAWNSSNAESLIRYTVNKGYSIHGWELGNELCGTGVGAKVAPDQYASDVKSLENIVQNIYRGFEVKPLVIAPGGFIDTNWFAQFIQRTPK SLQVVTQHIYNLGPGTRAKSSYLKVPSNKAAFQITLNVGYVGNDNQLINNILDPSYLDGGAQPFRDLEAILKNSATPAVAWVGEAGGAYNSGQNLVTNSF VNAFWYLGQLGMASSYDTKTYCRQTLIGGNYGLLDTATFVPNPDYYGALLWHRLMGSNVLSTSFSGTTGVRAYAHCSKQSQGISLLLINFNANISVNVRV VTDGEQAPRVKLGNTSREEYHFTAKDENLHSQKVVLNGKILALNSSGGIPPMEPVNRSMTDPIIVAPFSYVFSHISS |
Full Sequence |
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Protein Sequence Length: 533 Download |
MCMLFKLVLL YLWVHWVNQG SDFVTGRSGN VTSGTVFVNG TASIGKTDDN FICATLDWWA 60 PNKCDYGTCS WERSSLLNLI RMGGTLQDKV IYETKDDKSP CAPFVKNSSE MFGFSKGCLP 120 MSRWDQLNVF FKKAGAMVVF GLNALNGKAI GSDGSATGAW NSSNAESLIR YTVNKGYSIH 180 GWELGNELCG TGVGAKVAPD QYASDVKSLE NIVQNIYRGF EVKPLVIAPG GFIDTNWFAQ 240 FIQRTPKSLQ VVTQHIYNLG PGTRAKSSYL KVPSNKAAFQ ITLNVGYVGN DNQLINNILD 300 PSYLDGGAQP FRDLEAILKN SATPAVAWVG EAGGAYNSGQ NLVTNSFVNA FWYLGQLGMA 360 SSYDTKTYCR QTLIGGNYGL LDTATFVPNP DYYGALLWHR LMGSNVLSTS FSGTTGVRAY 420 AHCSKQSQGI SLLLINFNAN ISVNVRVVTD GEQAPRVKLG NTSREEYHFT AKDENLHSQK 480 VVLNGKILAL NSSGGIPPME PVNRSMTDPI IVAPFSYVFS HISSIILPAC IN* 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 | 3.0e-164 | 34 | 358 | 344 | + 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 | CBI25561.1 | 0 | 25 | 530 | 21 | 532 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283254.1 | 0 | 1 | 530 | 1 | 536 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002283260.1 | 0 | 1 | 530 | 1 | 545 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324878.1 | 0 | 34 | 530 | 1 | 504 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002515478.1 | 0 | 17 | 531 | 1 | 523 | heparanase, putative [Ricinus communis] |