Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 32458 |
Family | GH79 |
Protein Properties | Length: 488 Molecular Weight: 53558.3 Isoelectric Point: 6.5776 |
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 | 14 | 483 | 0 |
DEHFVCATIDWWPQGKCNYGSCSWFHSSILNLDLTNRLLAEAVTALAPLLIRLGGSLEDQIFYDVGSSATTTTCKTFTTQNHRFGFSTGCLNMSRWQQLN EFFQRTGSLVAFGLNALHGKERIDNTFQGPWNSSNARDFIAYTASKRYPIKAWGLGNELSSSFSGVTLDSRNYAADVDELQQIIDEIYGTGQKPVLVAPD GFFYAYWYSQVLQQTRTDPALRAVSFHVYDLGPGDGKNIAARILSAAHTDRYQQVQRVLRQYGNGAKAWVGEAGGIYNGGQHLVSDAFVFSFWYLDQLGM AALHNTAVFCRQSLIGGNYGLLDSNFNPNPDFYSALLWKRLMGEVVLNVTSQSLNSSSFHTYAHCLKNARVSSLVWLTPFAYSNVEQGGIAVLVINFSNN TQVVLDLGLKSQKLEYHLSSPDGNVQSQRVALNGQVLEGAKSELKAIAVEGSNPSKVAPLSIAFITLPDA |
Full Sequence |
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Protein Sequence Length: 488 Download |
TLALDASIPV ATVDEHFVCA TIDWWPQGKC NYGSCSWFHS SILNLDLTNR LLAEAVTALA 60 PLLIRLGGSL EDQIFYDVGS SATTTTCKTF TTQNHRFGFS TGCLNMSRWQ QLNEFFQRTG 120 SLVAFGLNAL HGKERIDNTF QGPWNSSNAR DFIAYTASKR YPIKAWGLGN ELSSSFSGVT 180 LDSRNYAADV DELQQIIDEI YGTGQKPVLV APDGFFYAYW YSQVLQQTRT DPALRAVSFH 240 VYDLGPGDGK NIAARILSAA HTDRYQQVQR VLRQYGNGAK AWVGEAGGIY NGGQHLVSDA 300 FVFSFWYLDQ LGMAALHNTA VFCRQSLIGG NYGLLDSNFN PNPDFYSALL WKRLMGEVVL 360 NVTSQSLNSS SFHTYAHCLK NARVSSLVWL TPFAYSNVEQ GGIAVLVINF SNNTQVVLDL 420 GLKSQKLEYH LSSPDGNVQS QRVALNGQVL EGAKSELKAI AVEGSNPSKV APLSIAFITL 480 PDAFVPAC |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 9.0e-118 | 1 | 312 | 318 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | EAY87898.1 | 0 | 10 | 488 | 47 | 540 | hypothetical protein OsI_09318 [Oryza sativa Indica Group] |
GenBank | EAY99897.1 | 0 | 3 | 488 | 30 | 524 | hypothetical protein OsI_21892 [Oryza sativa Indica Group] |
GenBank | EAZ36024.1 | 0 | 3 | 488 | 30 | 524 | hypothetical protein OsJ_20330 [Oryza sativa Japonica Group] |
RefSeq | NP_001048420.1 | 0 | 10 | 488 | 47 | 540 | Os02g0802200 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_001769830.1 | 0 | 2 | 488 | 52 | 556 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 0.005 | 112 | 353 | 124 | 359 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 3vnz_A | 0.005 | 112 | 353 | 124 | 359 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 3vny_A | 0.005 | 112 | 353 | 124 | 359 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GO873410 | 322 | 13 | 328 | 0 |
FE454640 | 96 | 1 | 96 | 0 |
FE454640 | 103 | 103 | 204 | 0 |
GO875320 | 292 | 94 | 378 | 0 |
CK266509 | 303 | 62 | 357 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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