Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 133100 |
Family | GH79 |
Protein Properties | Length: 544 Molecular Weight: 59536.9 Isoelectric Point: 8.9777 |
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 | 60 | 534 | 0 |
EGFLCATLDWWPAEKCDYGTCSWKDASLLTMARNSSSQPPKFWFFLAALYPLTLRLGGSLQDRMFYKVGRSAQRPCSNFVKQQNSIFGFSEGCLNMSRWL ELNSLFQRTGASVAFGLNALNGRQRVSKGVYSGSWDSTNAEDFIKFTHDSKIAIAAWELGNELSANGVGTTINSRQYATDVKSLREIIDGIYGDQIDRPM VVAPDGFFVAAWYQQLLQSTGPRVLDAVTRHIYNLGAGVDRHLIQKILSPTYLSQEAGAFKQMRDTVSRYGPWAQAWIGEAGGAYNSGQHLVNDAFVSSF WYLDQLGMAASHSTAVYCRQSLVGGNYALLRTNSYNPNPDYYSALLWKQVMGNDVLPATVVSETYLRAYAHCAKSNSGGLAVLVINMSNSTVYSVSLKLS GFAKSSKGSSRTPRLEYHLSAPLTDLQSQSIHLNGKLLDVTPDGNIPVLKPISVDSKQPITIAPLSIAFVVLPDA |
Full Sequence |
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Protein Sequence Length: 544 Download |
MGRALLFLSC WIFLLGWVHK CGSAAAAAVP GRSKFLAEKI VARAAVVEIN TSNTIWRVSE 60 GFLCATLDWW PAEKCDYGTC SWKDASLLTM ARNSSSQPPK FWFFLAALYP LTLRLGGSLQ 120 DRMFYKVGRS AQRPCSNFVK QQNSIFGFSE GCLNMSRWLE LNSLFQRTGA SVAFGLNALN 180 GRQRVSKGVY SGSWDSTNAE DFIKFTHDSK IAIAAWELGN ELSANGVGTT INSRQYATDV 240 KSLREIIDGI YGDQIDRPMV VAPDGFFVAA WYQQLLQSTG PRVLDAVTRH IYNLGAGVDR 300 HLIQKILSPT YLSQEAGAFK QMRDTVSRYG PWAQAWIGEA GGAYNSGQHL VNDAFVSSFW 360 YLDQLGMAAS HSTAVYCRQS LVGGNYALLR TNSYNPNPDY YSALLWKQVM GNDVLPATVV 420 SETYLRAYAH CAKSNSGGLA VLVINMSNST VYSVSLKLSG FAKSSKGSSR TPRLEYHLSA 480 PLTDLQSQSI HLNGKLLDVT PDGNIPVLKP ISVDSKQPIT IAPLSIAFVV LPDAKLQACT 540 IVE* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 2.0e-144 | 42 | 366 | 329 | + 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. |