| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10005788 |
| Family | CBM43 |
| Protein Properties | Length: 1032 Molecular Weight: 115670 Isoelectric Point: 8.0916 |
| Chromosome | Chromosome/Scaffold: 24 Start: 78673 End: 84954 |
| Description | O-Glycosyl hydrolases family 17 protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CBM43 | 396 | 476 | 5.9e-24 |
| WCILNPDASNPVGLDDALGYACAYGDCTSLKPGSPCADLSKSWQASYAFNMYYQINDQDVDACDFNGLAALVKTNASRGNC | |||
| GH17 | 52 | 373 | 0 |
| VGVNWGSITSHPMSPDIVVQMLKDNGFKKLKLFESDSYTVSKFAGTDIEVMLGIPNNQLNDLAKDYDNAKDWVKENVSDHMSNEKDKHVNIKYVAGGNEP FLLSYSDKYTKDLFPAMQNIQKALNEAGYGNTIKATVPLNADVYESNSNKPSDGNFRSNVKDQMKAIIKFLHQNKAPILVNIYPFLSLYQSSNFPSSFAF FDENGRKVYDKNVEYSNVFDANYDTLVYALKKNGYPDLKIIVGEVGWPTAGHKYATPEYAEKFYSGLMKKLAGNKGTPLRPGKLDVYLFALMDEDQKSIE PGPFERHWGLFAFDGKPKFPVD | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1032 Download |
| MIKSTRSPLL IAGDNRRDKI CLWATLLLIV TITNVSPVFS ATNSSLSVVQ GVGVNWGSIT 60 SHPMSPDIVV QMLKDNGFKK LKLFESDSYT VSKFAGTDIE VMLGIPNNQL NDLAKDYDNA 120 KDWVKENVSD HMSNEKDKHV NIKYVAGGNE PFLLSYSDKY TKDLFPAMQN IQKALNEAGY 180 GNTIKATVPL NADVYESNSN KPSDGNFRSN VKDQMKAIIK FLHQNKAPIL VNIYPFLSLY 240 QSSNFPSSFA FFDENGRKVY DKNVEYSNVF DANYDTLVYA LKKNGYPDLK IIVGEVGWPT 300 AGHKYATPEY AEKFYSGLMK KLAGNKGTPL RPGKLDVYLF ALMDEDQKSI EPGPFERHWG 360 LFAFDGKPKF PVDLSGKGND KMLIAAKGVQ YLPAQWCILN PDASNPVGLD DALGYACAYG 420 DCTSLKPGSP CADLSKSWQA SYAFNMYYQI NDQDVDACDF NGLAALVKTN ASRGNCLFPV 480 QIVSGGWRIE SGRGVRLVAS ILVLMGILTN YISWPGMEII TVVITIILSA SFSLYIVRFL 540 HKQIWKPWKT QELLASQGIN GPGYRFLVGN AREIVRLRAE TLGKPMPAIS HDLVLRVLPE 600 VHYWVKQYGK TFVYWIGHQA HLVVTDPDMV KQVLFDKDGN FPKAKWGFVY ASKLMGNGLV 660 TNEGENWSKI KKLANASFHG VKLKSMVPEM IDSADNMLKR WKNKEGVGEE IEVSEEFRML 720 TGEMMLRIAF GTSFDEGRQI FDMIFKMRLL VEKNVFKFRL PIVSKIFKNR DYGEAVRLEQ 780 GIRACVLEIV SKREKSHDVI KDDYLGLLIQ AHRERDESKK ISIDDLVDEF KTLYLAGHET 840 TFILLSWIVL LLAIHQDWQQ EARNEVFSVF GGDKFPDVDG IAKLKVMGMI INETLRLYPP 900 VTALGVRRID VENEATLGNL TLHADIRLQI PILCLHHDPE IWGEDANLFK PERFSEGIAK 960 ATNNNLATFI PFGMGPRNCV GVDIANNIVR VALSMILQRF SFTLSPGYVH SPHPYIPVSP 1020 GKGVQVILHA L* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02936 | PLN02936 | 7.0e-36 | 604 | 1007 | 433 | + epsilon-ring hydroxylase | ||
| COG2124 | CypX | 9.0e-40 | 623 | 1008 | 393 | + Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism] | ||
| pfam00067 | p450 | 1.0e-62 | 606 | 1007 | 414 | + Cytochrome P450. Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures. | ||
| pfam00332 | Glyco_hydro_17 | 1.0e-71 | 52 | 373 | 324 | + Glycosyl hydrolases family 17. | ||
| PLN02290 | PLN02290 | 4.0e-103 | 516 | 1031 | 524 | + cytokinin trans-hydroxylase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005506 | iron ion binding |
| GO:0005975 | carbohydrate metabolic process |
| GO:0009055 | electron carrier activity |
| GO:0016705 | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN62816.1 | 0 | 35 | 489 | 12 | 461 | hypothetical protein [Vitis vinifera] |
| RefSeq | NP_201284.1 | 0 | 32 | 485 | 8 | 458 | glycosyl hydrolase family 17 protein [Arabidopsis thaliana] |
| RefSeq | XP_002275701.1 | 0 | 35 | 489 | 12 | 461 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002310612.1 | 0 | 17 | 503 | 3 | 479 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002530257.1 | 0 | 38 | 488 | 15 | 461 | Glucan endo-1,3-beta-glucosidase precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ur8_B | 0 | 50 | 375 | 1 | 315 | A Chain A, Solution Structure Of Human Sap18 |
| PDB | 3ur8_A | 0 | 50 | 375 | 1 | 315 | A Chain A, Solution Structure Of Human Sap18 |
| PDB | 3ur7_B | 0 | 50 | 375 | 1 | 315 | A Chain A, Higher-density Crystal Structure Of Potato Endo-1,3-beta-glucanase |
| PDB | 3ur7_A | 0 | 50 | 375 | 1 | 315 | A Chain A, Higher-density Crystal Structure Of Potato Endo-1,3-beta-glucanase |
| PDB | 4gzj_A | 0 | 50 | 375 | 1 | 315 | A Chain A, Higher-density Crystal Structure Of Potato Endo-1,3-beta-glucanase |
