y
Basic Information | |
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Species | Volvox carteri |
Cazyme ID | Vocar20009711m |
Family | GH16 |
Protein Properties | Length: 334 Molecular Weight: 36988.1 Isoelectric Point: 4.5753 |
Chromosome | Chromosome/Scaffold: 1 Start: 7504432 End: 7506778 |
Description | |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH16 | 71 | 329 | 0 |
WSDEFDAATLDTSSWNYFTGTAYNNELEYYTSRPENVRLENGSLVIEARAEAYGGMNYTSARIDTRLKRAFYPGVSVNGTVVPKIRYEARMKLPKGQGMW PAFWLAPNSQVCDACGPYGSWPYSGEIYILEAINNMTYAFGTVHYGGFRSDGQTFNNQGHYRPTSFNLGLEWHTYAFEWSYNQMWWFIDDVLYYTTHSYF LSDEGWWTSSQTTTPTGPNSPFDAPFYIILNLAVGGDWPRAPDASTVFPSQLLVDYVRV |
Full Sequence |
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Protein Sequence Length: 334 Download |
MLLSLSNTDW TVSAARAPKP TASPSPPPSS SPPPSPSPAP SPAPSPSPSA PPPSPAAPYS 60 PEVCTSPTLL WSDEFDAATL DTSSWNYFTG TAYNNELEYY TSRPENVRLE NGSLVIEARA 120 EAYGGMNYTS ARIDTRLKRA FYPGVSVNGT VVPKIRYEAR MKLPKGQGMW PAFWLAPNSQ 180 VCDACGPYGS WPYSGEIYIL EAINNMTYAF GTVHYGGFRS DGQTFNNQGH YRPTSFNLGL 240 EWHTYAFEWS YNQMWWFIDD VLYYTTHSYF LSDEGWWTSS QTTTPTGPNS PFDAPFYIIL 300 NLAVGGDWPR APDASTVFPS QLLVDYVRVL GYW* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG2273 | SKN1 | 3.0e-23 | 71 | 332 | 263 | + Beta-glucanase/Beta-glucan synthetase [Carbohydrate transport and metabolism] | ||
cd00413 | Glyco_hydrolase_16 | 7.0e-25 | 73 | 329 | 258 | + 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. | ||
cd08024 | GH16_CCF | 7.0e-27 | 69 | 307 | 289 | + 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. | ||
cd02182 | GH16_Strep_laminarinase_like | 4.0e-43 | 68 | 329 | 286 | + 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. | ||
cd08023 | GH16_laminarinase_like | 5.0e-77 | 71 | 329 | 266 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAC06195.1 | 0 | 69 | 329 | 33 | 259 | 1,3-(1,3;1,4)-beta-D-glucan 3(4)-glucanohydrolase [Bacillus circulans] |
RefSeq | YP_001309932.1 | 0 | 69 | 329 | 35 | 262 | glycoside hydrolase family protein [Clostridium beijerinckii NCIMB 8052] |
RefSeq | YP_001634695.1 | 0 | 68 | 329 | 39 | 267 | glycoside hydrolase family protein [Chloroflexus aurantiacus J-10-fl] |
RefSeq | ZP_01617124.1 | 0 | 25 | 329 | 35 | 311 | Beta-glucanase/Beta-glucan synthetase [marine gamma proteobacterium HTCC2143] |
RefSeq | ZP_04850748.1 | 0 | 69 | 329 | 36 | 262 | 1,3-(1,3;1,4)-beta-D-glucan 3(4)-glucanohydrolase [Paenibacillus sp. oral taxon 786 str. D14] |
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 | 3b01_D | 7.00649e-43 | 69 | 329 | 12 | 253 | A Chain A, Crystal Structure Of Wild-Type E.Coli Gs In Complex With Adp And Glucose(Wtgsb) |
PDB | 3b01_C | 7.00649e-43 | 69 | 329 | 12 | 253 | A Chain A, Crystal Structure Of Wild-Type E.Coli Gs In Complex With Adp And Glucose(Wtgsb) |
PDB | 3b01_B | 7.00649e-43 | 69 | 329 | 12 | 253 | A Chain A, Crystal Structure Of Wild-Type E.Coli Gs In Complex With Adp And Glucose(Wtgsb) |
PDB | 3b01_A | 7.00649e-43 | 69 | 329 | 12 | 253 | A Chain A, Crystal Structure Of Wild-Type E.Coli Gs In Complex With Adp And Glucose(Wtgsb) |
PDB | 3b00_D | 7.00649e-43 | 69 | 329 | 12 | 253 | A Chain A, Crystal Structure Of Wild-Type E.Coli Gs In Complex With Adp And Glucose(Wtgsb) |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO408828 | 276 | 69 | 329 | 6e-34 |
DR473838 | 271 | 63 | 329 | 2e-31 |
CU739026 | 261 | 65 | 313 | 2e-29 |
CU738731 | 258 | 65 | 310 | 4e-25 |
HX142031 | 251 | 95 | 329 | 5e-24 |
Sequence Alignments (This image is cropped. Click for full image.) |
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