y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29818.m000393 |
Family | GT47 |
Protein Properties | Length: 512 Molecular Weight: 58585 Isoelectric Point: 8.2881 |
Chromosome | Chromosome/Scaffold: 29818 Start: 21572 End: 24169 |
Description | exostosin family protein |
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 |
GT47 | 108 | 424 | 0 |
EPLKVFMYDLPPEFHFELLDWKAQGDSVWPDLRTKIPGYPGGLNLQHSIEYWLTLDLLASEISGIPRAGSAIRVRNSSEADVIFVPFFSSLSYNRYSKVN PHQKRSKNKLLQEKLVRYVTSQMEWKRSQGQDHIILAHHPNSMLDARMKLWPALFILADFGRYPPNIANVDKDLIAPYKHVIRSYADDSSTFDSRPTLLY FQGAIYRKDGGFARQELFYLLKDEKDVHFQFGSVQKDGINKASQGMHTSKFCLNIAGDTPSSNRLFDAIASHCVPVIISDDIELPYEDVLDYSQFCIFVR TSDAIKEKFLINLIRGI |
Full Sequence |
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Protein Sequence Length: 512 Download |
MAEKHSSSLV VISRKSLFGL FSFVLVLFIL SWFFVLRSTG RPNFIDGSLI NNPLYSIIDN 60 GSDAPSIGSR ATLADSRGEG QEEAEETPQE KVDVKDVKCN TPLENRKEPL KVFMYDLPPE 120 FHFELLDWKA QGDSVWPDLR TKIPGYPGGL NLQHSIEYWL TLDLLASEIS GIPRAGSAIR 180 VRNSSEADVI FVPFFSSLSY NRYSKVNPHQ KRSKNKLLQE KLVRYVTSQM EWKRSQGQDH 240 IILAHHPNSM LDARMKLWPA LFILADFGRY PPNIANVDKD LIAPYKHVIR SYADDSSTFD 300 SRPTLLYFQG AIYRKDGGFA RQELFYLLKD EKDVHFQFGS VQKDGINKAS QGMHTSKFCL 360 NIAGDTPSSN RLFDAIASHC VPVIISDDIE LPYEDVLDYS QFCIFVRTSD AIKEKFLINL 420 IRGIGKDEWT QMWQKLKEVE RFFEFQYPSK EGDAVQMIWQ AVARKVPAIR MKINKSMRFS 480 RSFGHNIREL RGIPTPGISA WTSLAFEERI IL 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03016 | Exostosin | 2.0e-51 | 106 | 424 | 329 | + Exostosin family. The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear. |
Gene Ontology | |
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GO Term | Description |
GO:0016020 | membrane |