y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s181_80V6.1 |
Family | GH79 |
Protein Properties | Length: 570 Molecular Weight: 62478.9 Isoelectric Point: 4.7948 |
Chromosome | Chromosome/Scaffold: 181 Start: 497412 End: 502003 |
Description | glucuronidase 3 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 107 | 559 | 0 |
LTNYRNGTALYPFRIRLGGTLQDHIVYEIGLNSEESCLPIAKDETYMFGFREGCLSMNRWIALNNLFAKSGTLVAFGLNALYNRLQVGDGWGPWDSSNAR SLIEFSIQQGIQVEAWELGNELSGNGVGTTISAQQYAEDMRELRFIIDTLYVDFDRRPLVVAPDGFLEGQWDTAFLNASGPGVVDVFTRHIYNLGPGVSG DLVDKILNPSYLDNELGNFRAVRDILQTLDPSPSAWVGEAGGAYNSGHHLVTDAFVFSFWYLDQLAMAASFNNKAYCRQSLIGGNYGLLNTTTFRPNPDM YSALLWKRMMGSRVLTTTVDGYPQLRTYSHCQQGTTTGGLTLLLINLSNFTVSVAANLLSHSKDEPKSQGGKNPKYSLIPKSFKTSKALVTRSEYHLTPQ HKDLHSQTAVLNGVPLELTSTGDLPNMEPIVRENFSPVSVAPISIVFVVLPDA |
Full Sequence |
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Protein Sequence Length: 570 Download |
MAALLLCLLL SSMLLSVSTS HSCSNITRVC AEDEDNVLTV DVDASSLLAT TDEAFLCATL 60 DWWPPDKCDY GTCAWGQASL LNLDLDNPLL EKFLKVGEHK VEIACALTNY RNGTALYPFR 120 IRLGGTLQDH IVYEIGLNSE ESCLPIAKDE TYMFGFREGC LSMNRWIALN NLFAKSGTLV 180 AFGLNALYNR LQVGDGWGPW DSSNARSLIE FSIQQGIQVE AWELGNELSG NGVGTTISAQ 240 QYAEDMRELR FIIDTLYVDF DRRPLVVAPD GFLEGQWDTA FLNASGPGVV DVFTRHIYNL 300 GPGVSGDLVD KILNPSYLDN ELGNFRAVRD ILQTLDPSPS AWVGEAGGAY NSGHHLVTDA 360 FVFSFWYLDQ LAMAASFNNK AYCRQSLIGG NYGLLNTTTF RPNPDMYSAL LWKRMMGSRV 420 LTTTVDGYPQ LRTYSHCQQG TTTGGLTLLL INLSNFTVSV AANLLSHSKD EPKSQGGKNP 480 KYSLIPKSFK TSKALVTRSE YHLTPQHKDL HSQTAVLNGV PLELTSTGDL PNMEPIVREN 540 FSPVSVAPIS IVFVVLPDAK VPICSKSDS* 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 | 7.0e-138 | 39 | 371 | 335 | + 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 |
RefSeq | XP_001767170.1 | 0 | 38 | 564 | 35 | 535 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769830.1 | 0 | 4 | 565 | 13 | 557 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001770123.1 | 0 | 25 | 564 | 2 | 525 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001774747.1 | 0 | 33 | 569 | 11 | 528 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002515478.1 | 0 | 39 | 564 | 16 | 522 | heparanase, putative [Ricinus communis] |