y
Basic Information | |
---|---|
Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre02.g115950.t1.2 |
Family | GH16 |
Protein Properties | Length: 327 Molecular Weight: 35831.4 Isoelectric Point: 7.4035 |
Chromosome | Chromosome/Scaffold: 2 Start: 6445098 End: 6449097 |
Description | |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH16 | 30 | 322 | 4.3e-36 |
SDEFRAGCKDARVCVNGGIDIRKWSFDLGDGTSFGPNMIGWGNWQRQCHTNSSANARVEAFPGKTDGMLVIQAGYSPLRTCYNENAAPSTTNYTSARLTT RDSAAFKWKGTAGNSTAVRIDVRLQVPMVAGTWPAAWMLPTTDKRWCSGCSEYGDGWCLGGEIDIMEHVNTNNFLISNVHFGGQANASWLDCHEKVGRFR AGSRAASWNVMTLIWDSTYLRFLANGKEVSRLNAGDWYTGGADRAANKFAPFDQDFFLILDMAVGGLYPGFNINDAAIAEGAARYNIDYVRVY |
Full Sequence |
---|
Protein Sequence Length: 327 Download |
MSATVSLSLV ALLLALSHSF THAKQVLRWS DEFRAGCKDA RVCVNGGIDI RKWSFDLGDG 60 TSFGPNMIGW GNWQRQCHTN SSANARVEAF PGKTDGMLVI QAGYSPLRTC YNENAAPSTT 120 NYTSARLTTR DSAAFKWKGT AGNSTAVRID VRLQVPMVAG TWPAAWMLPT TDKRWCSGCS 180 EYGDGWCLGG EIDIMEHVNT NNFLISNVHF GGQANASWLD CHEKVGRFRA GSRAASWNVM 240 TLIWDSTYLR FLANGKEVSR LNAGDWYTGG ADRAANKFAP FDQDFFLILD MAVGGLYPGF 300 NINDAAIAEG AARYNIDYVR VYDLLP* 360 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00413 | Glyco_hydrolase_16 | 2.0e-7 | 99 | 322 | 231 | + glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues. | ||
cd02179 | GH16_beta_GRP | 8.0e-11 | 123 | 297 | 194 | + beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16. Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members. | ||
cd02182 | GH16_Strep_laminarinase_like | 6.0e-22 | 29 | 322 | 308 | + Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel. | ||
cd08024 | GH16_CCF | 2.0e-23 | 67 | 301 | 287 | + Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members. | ||
cd08023 | GH16_laminarinase_like | 5.0e-52 | 29 | 322 | 297 | + Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans. |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001699876.1 | 0 | 67 | 326 | 4 | 228 | hypothetical protein CHLREDRAFT_141622 [Chlamydomonas reinhardtii] |
RefSeq | XP_001703318.1 | 0 | 1 | 326 | 3 | 355 | hypothetical protein CHLREDRAFT_182825 [Chlamydomonas reinhardtii] |
RefSeq | XP_001703464.1 | 2e-36 | 23 | 326 | 45 | 329 | hypothetical protein CHLREDRAFT_168996 [Chlamydomonas reinhardtii] |
RefSeq | XP_001703464.1 | 0.0003 | 47 | 157 | 333 | 436 | hypothetical protein CHLREDRAFT_168996 [Chlamydomonas reinhardtii] |
RefSeq | YP_174203.1 | 1e-31 | 1 | 322 | 1 | 278 | endo-beta-1,3-glucanase [Bacillus clausii KSM-K16] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3atg_A | 9e-22 | 27 | 323 | 5 | 239 | A Chain A, Endo-1,3-Beta-Glucanase From Cellulosimicrobium Cellulans |
PDB | 4dfs_B | 1e-21 | 27 | 323 | 20 | 263 | A Chain A, Structure Of The Catalytic Domain Of An Endo-1,3-Beta-Glucanase (Laminarinase) From Thermotoga Petrophila Rku-1 |
PDB | 4dfs_A | 1e-21 | 27 | 323 | 20 | 263 | A Chain A, Structure Of The Catalytic Domain Of An Endo-1,3-Beta-Glucanase (Laminarinase) From Thermotoga Petrophila Rku-1 |
PDB | 3b01_D | 2e-21 | 27 | 326 | 12 | 259 | A Chain A, Structure Of The Catalytic Domain Of An Endo-1,3-Beta-Glucanase (Laminarinase) From Thermotoga Petrophila Rku-1 |
PDB | 3b01_C | 2e-21 | 27 | 326 | 12 | 259 | A Chain A, Structure Of The Catalytic Domain Of An Endo-1,3-Beta-Glucanase (Laminarinase) From Thermotoga Petrophila Rku-1 |
Signal Peptide | ||||
---|---|---|---|---|
Cleavage Site | ||||
23 |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
BI531129 | 178 | 161 | 327 | 8e-29 |
BU650832 | 166 | 28 | 168 | 3e-21 |
HX142031 | 258 | 77 | 323 | 2e-18 |
HX142007 | 234 | 77 | 299 | 0.000000000000001 |
CU739026 | 284 | 27 | 307 | 0.000000000000005 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|
![]() |