Basic Information | |
---|---|
Species | Capsella rubella |
Cazyme ID | Carubv10000369m |
Family | GH85 |
Protein Properties | Length: 688 Molecular Weight: 77104.5 Isoelectric Point: 6.439 |
Chromosome | Chromosome/Scaffold: 6 Start: 1589631 End: 1593146 |
Description | Glycosyl hydrolase family 85 |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH85 | 78 | 359 | 0 |
MKGGYVDDKWVQGCGNNAGYAIWNWYLMDVFVYFSHSLVTLPPPCWTNTAHRHGVKVLGTFITEWDEGKATCKELLATKESAQMYAERLAELAAALGFDG WLINIENVIDEVQIPNLLVFVSHLTKVMHSSVPGGLVIWYDSVTVHGLLEWQDQLTDNNKPFFDICDGIFMNYTWKENYPKASAKIAGDRKYDVYMGIDV FGRGTYGGGQWTANVALDLLKRNNVSAAVFAPGWVYETEQPPDFHTAQNKWWSLVEKSWGIVQTYPQVLPFYSDFNQGLGSH |
Full Sequence |
---|
Protein Sequence Length: 688 Download |
MSKSNEAAML VAPSPPPPPF DPTKPSTPIS FPIKTLQDLK SRSYFDSFHF SFNRSSVALR 60 RNIGVLPDRS RLLVCHDMKG GYVDDKWVQG CGNNAGYAIW NWYLMDVFVY FSHSLVTLPP 120 PCWTNTAHRH GVKVLGTFIT EWDEGKATCK ELLATKESAQ MYAERLAELA AALGFDGWLI 180 NIENVIDEVQ IPNLLVFVSH LTKVMHSSVP GGLVIWYDSV TVHGLLEWQD QLTDNNKPFF 240 DICDGIFMNY TWKENYPKAS AKIAGDRKYD VYMGIDVFGR GTYGGGQWTA NVALDLLKRN 300 NVSAAVFAPG WVYETEQPPD FHTAQNKWWS LVEKSWGIVQ TYPQVLPFYS DFNQGLGSHI 360 SLGGKILSDA PWYNISCQSL QPLLEFHEGK NSDIMQVTVD GGEASYNGGG NVSFRGKLQR 420 NAHFTARLFK PHLELPASPI SISFSVKSDK RSELSILLHF SSPSHEKKSF LMAPNESSNR 480 FGDMFLPCHV TSTQTTSDWM VHETNLVLDG HTLSEISAFC SRPDDLTEET NTLEYFALLG 540 HISIKSQQKT KLFPLASSWV IEAHHIKFVP GDSGSKTLSC KLEWRLKHPE EDIAFTRYNV 600 YAENLKSSEY RARKVMEEPR SEKVFLGTAH VDAYYVSGLV VGSDLKGVRF VVQTCGEDGT 660 WQELDHSPNL LVEVERPSSK LCCCGLI* |
Functional Domains Download unfiltered results here | ||||||
---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
cd00598 | GH18_chitinase-like | 0.0004 | 80 | 250 | 184 | + The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model. |
COG4724 | COG4724 | 2.0e-32 | 52 | 519 | 514 | + Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism] |
pfam03644 | Glyco_hydro_85 | 4.0e-119 | 78 | 359 | 301 | + Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates. |
cd06547 | GH85_ENGase | 6.0e-135 | 73 | 386 | 334 | + Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model. |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0005737 | cytoplasm |
GO:0033925 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAB09989.1 | 0 | 23 | 676 | 16 | 620 | unnamed protein product [Arabidopsis thaliana] |
RefSeq | NP_187715.1 | 0 | 1 | 675 | 1 | 694 | glycosyl hydrolase family 85 protein [Arabidopsis thaliana] |
RefSeq | NP_196165.3 | 0 | 23 | 687 | 16 | 680 | hydrolase, acting on glycosyl bonds / mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [Arabidopsis thaliana] |
RefSeq | XP_002273683.1 | 0 | 10 | 675 | 6 | 688 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520784.1 | 0 | 1 | 675 | 1 | 685 | endo beta n-acetylglucosaminidase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3fha_D | 2e-30 | 102 | 657 | 84 | 604 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fha_C | 2e-30 | 102 | 657 | 84 | 604 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fha_B | 2e-30 | 102 | 657 | 84 | 604 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fha_A | 2e-30 | 102 | 657 | 84 | 604 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fhq_F | 2e-30 | 102 | 657 | 84 | 604 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
EV118225 | 237 | 106 | 342 | 0 |
EV160308 | 245 | 120 | 364 | 0 |
JG621224 | 271 | 122 | 391 | 0 |
EL437937 | 257 | 97 | 353 | 0 |
GE541456 | 268 | 191 | 458 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|