Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10036963 |
Family | GH79 |
Protein Properties | Length: 522 Molecular Weight: 57888.9 Isoelectric Point: 8.7696 |
Chromosome | Chromosome/Scaffold: 31 Start: 1415332 End: 1417483 |
Description | glucuronidase 2 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 43 | 516 | 0 |
DNDFICATLDWWPKNKCDYNQCPWGQTSALNLDLKNTNLATAIKAFDPLRIRVGGSLEDLVVYKVGKAIKRFPKFKKLKGGMFGFSRGTLTMDRWDQLNQ LFTKTNAKVIFGLNALVGKRKKDESSTLWIGDWNSQNARDFMNYTVQKGYKIDSYELGNELSGSGVSARVEPEQYAKDTIKVRKAVNELYPDPNSRPLVL GPAGFFDKEWFKKYLQAVGPNVVDGVTHHIYNLGAGVDSKLINKVQDPFFLDKVAQTFKEVQDIVEQSGTAAAPWVGESGGAFNSGGKDVSNTFANGFWY LDQLGMTSTFGHKAYCRQSLVGGNYGLLRSDSFTPNPDYYGALLWHRLMGTIVLRTIHDGSPYLRAYSHCSKKNFGVTLLLINMSNSTTFNVWVTNDLNL YRTTTDSTILTEDREEYHLTPEGGNIQSDVVQLNGTPLKLSCGEIPMMDPKLVPASSTVTVAPDSFVYVNIKDF |
Full Sequence |
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Protein Sequence Length: 522 Download |
MAAAFRAFLV YSLFRSTLSV LCSADTSRIT VTIQSVNSIA KTDNDFICAT LDWWPKNKCD 60 YNQCPWGQTS ALNLDLKNTN LATAIKAFDP LRIRVGGSLE DLVVYKVGKA IKRFPKFKKL 120 KGGMFGFSRG TLTMDRWDQL NQLFTKTNAK VIFGLNALVG KRKKDESSTL WIGDWNSQNA 180 RDFMNYTVQK GYKIDSYELG NELSGSGVSA RVEPEQYAKD TIKVRKAVNE LYPDPNSRPL 240 VLGPAGFFDK EWFKKYLQAV GPNVVDGVTH HIYNLGAGVD SKLINKVQDP FFLDKVAQTF 300 KEVQDIVEQS GTAAAPWVGE SGGAFNSGGK DVSNTFANGF WYLDQLGMTS TFGHKAYCRQ 360 SLVGGNYGLL RSDSFTPNPD YYGALLWHRL MGTIVLRTIH DGSPYLRAYS HCSKKNFGVT 420 LLLINMSNST TFNVWVTNDL NLYRTTTDST ILTEDREEYH LTPEGGNIQS DVVQLNGTPL 480 KLSCGEIPMM DPKLVPASST VTVAPDSFVY VNIKDFKAPA C* |
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-168 | 28 | 347 | 320 | + 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 | CBI27258.1 | 0 | 29 | 521 | 27 | 523 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 29 | 521 | 25 | 521 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 3 | 521 | 2 | 517 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 29 | 520 | 31 | 529 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.0000000005 | 57 | 104 | 540 | 587 | Heparanase precursor, putative [Ricinus communis] |
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 | 0.00004 | 123 | 410 | 107 | 383 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 3vnz_A | 0.00004 | 123 | 410 | 107 | 383 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 3vny_A | 0.00004 | 123 | 410 | 107 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |