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Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_93036g0020 |
Family | GH79 |
Protein Properties | Length: 542 Molecular Weight: 60389.4 Isoelectric Point: 8.3893 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 73 | 533 | 0 |
DESFICATLDWWPPEKCDYGRCSWVDASLLNMDLENPTFAKAVKAFSPLKIRLGGTLQDKLIYDVGPLSQPCHPFVRDVSKMFGFSKGCLTMDRWDKLNK FIAKTGSMVAFGLNALYGRYQMSTDGLWGGPWNSSNARSLIQYTVDHGYKIYAWEFGNELSGSGIGARVSATQYAADVIELNKVLKDIYKHSREKPLTVA PDGFFDPTWFQEILQQTGPNVLNAVTRHIYNLGAGVDKHLTQKILSPGYLSREATKFRQMQAILQKYGPWSSSWVGEAGGAYNSGKHRVSDAFVNSFWYL DQLGMSSTFDTKVYCRQSLVGGNYGLLNTTXXXXXXXXXXXXLHPILIIIVHCFGIGPPYVRTYAHCAKNDTGITLLLINLSNDTNVDILVSSYPNSTMY KRSLNAKESFMHKIKKFLAWAGSKTSELTEDGNIPSLDPVMVDAGLPIPVAPLSIAFVSLP |
Full Sequence |
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Protein Sequence Length: 542 Download |
MHVALDTKFE ADWRAYAVRR KIFLSHWKSE VRWDAEVLNQ ISSAIVVFCC LKACNGQFVT 60 LVVNASAKIA ETDESFICAT LDWWPPEKCD YGRCSWVDAS LLNMDLENPT FAKAVKAFSP 120 LKIRLGGTLQ DKLIYDVGPL SQPCHPFVRD VSKMFGFSKG CLTMDRWDKL NKFIAKTGSM 180 VAFGLNALYG RYQMSTDGLW GGPWNSSNAR SLIQYTVDHG YKIYAWEFGN ELSGSGIGAR 240 VSATQYAADV IELNKVLKDI YKHSREKPLT VAPDGFFDPT WFQEILQQTG PNVLNAVTRH 300 IYNLGAGVDK HLTQKILSPG YLSREATKFR QMQAILQKYG PWSSSWVGEA GGAYNSGKHR 360 VSDAFVNSFW YLDQLGMSST FDTKVYCRQS LVGGNYGLLN TTXXXXXXXX XXXXLHPILI 420 IIVHCFGIGP PYVRTYAHCA KNDTGITLLL INLSNDTNVD ILVSSYPNST MYKRSLNAKE 480 SFMHKIKKFL AWAGSKTSEL TEDGNIPSLD PVMVDAGLPI PVAPLSIAFV SLPGLDIPAC 540 LK 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 0 | 59 | 376 | 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 | ACG27548.1 | 0 | 60 | 540 | 27 | 538 | heparanase-like protein 2 precursor [Zea mays] |
GenBank | ACR10240.1 | 0 | 59 | 542 | 25 | 539 | heparanase [Oryza sativa Indica Group] |
EMBL | CBI15157.1 | 0 | 63 | 540 | 29 | 512 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001067122.1 | 0 | 59 | 542 | 25 | 539 | Os12g0578400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002284470.1 | 0 | 63 | 540 | 29 | 538 | PREDICTED: hypothetical protein [Vitis vinifera] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EX353120 | 286 | 179 | 462 | 0 |
CX647951 | 267 | 107 | 373 | 0 |
EX390283 | 251 | 254 | 502 | 0 |
EX933244 | 258 | 79 | 336 | 0 |
EX390283 | 23 | 499 | 521 | 0.011 |
Sequence Alignments (This image is cropped. Click for full image.) |
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