Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr3g071610.1 |
Family | GH85 |
Protein Properties | Length: 740 Molecular Weight: 82806.2 Isoelectric Point: 5.283 |
Chromosome | Chromosome/Scaffold: 3 Start: 22833031 End: 22839126 |
Description | Glycosyl hydrolase family 85 |
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 |
GH85 | 109 | 419 | 0 |
MAGGYSDDKWIQGGDNVNAYSIWHWHLIDVFVYFSHDLVTLPPVCWINTAHRHGVKVLGTFITEWDEGKANCDVLLSTKESAQMYAERLAELAVDLGFDG WLINMEVELDPAQISNLKEFVDHLSSTMHSSVPGSQVLWYDSVTIDGKLNWQDQLNESNKPFFDICDGIFVNYTWKEDYPRISAAVAGDRKFDVYMGIDV FGRNTYGGGQWNANVALDVIRKNDVSAAIFAPGWVYETKQPPDFETAQNRIPDLLHAPVLSYGIAINCRLITSVSVSSFWWGLVEKSWGILRNFSGPLPL YTNFDQGRGYH |
Full Sequence |
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Protein Sequence Length: 740 Download |
MNPRHLEPYI NRQFLIKIRN ILRFISQTTQ NLTMSTPNPN SSSSPSPSPP FDPKQPSIPI 60 SYPIKTLQEL ESRSYFDSFH YPFNKASVPI SSSSSKLPDR RRLLVCHDMA GGYSDDKWIQ 120 GGDNVNAYSI WHWHLIDVFV YFSHDLVTLP PVCWINTAHR HGVKVLGTFI TEWDEGKANC 180 DVLLSTKESA QMYAERLAEL AVDLGFDGWL INMEVELDPA QISNLKEFVD HLSSTMHSSV 240 PGSQVLWYDS VTIDGKLNWQ DQLNESNKPF FDICDGIFVN YTWKEDYPRI SAAVAGDRKF 300 DVYMGIDVFG RNTYGGGQWN ANVALDVIRK NDVSAAIFAP GWVYETKQPP DFETAQNRIP 360 DLLHAPVLSY GIAINCRLIT SVSVSSFWWG LVEKSWGILR NFSGPLPLYT NFDQGRGYHI 420 SVDGNSVSDA TWCNISCQGF QPLLELADPT NSIQVTIDLK EASFSGGGNI TFKGSLEKQT 480 YFERKILQGE FLLGEDPIHF IYSVKCNGNS SLGLKLVFTS NNDEKNYVLL TSGEVNDLSS 540 KFNKVITTRE HKGFSHGWVI NESAIAMNEY TLNEIHAVCY RSNSSLSDCT DCTVASPSDY 600 YALLGHVTIK NSDYKSDFPV SSSWLVDGKY IKWTSGSNGS KTLNIKISWT LKDGKNYLSL 660 KYNIYLVKLS KQAGGNPGTT LELVKEYLGV AQVNCFYVSD LEVPSDTSSL KFIIQVCSVD 720 GTIQALDESP YYQLEVEGP* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam01079 | Hint | 0.007 | 497 | 580 | 91 | + Hint module. This is an alignment of the Hint module in the Hedgehog proteins. It does not include any Inteins which also possess the Hint module. |
cd00598 | GH18_chitinase-like | 2.0e-7 | 109 | 264 | 175 | + 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 | 3.0e-35 | 120 | 525 | 426 | + Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism] |
pfam03644 | Glyco_hydro_85 | 2.0e-117 | 109 | 422 | 319 | + Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates. |
cd06547 | GH85_ENGase | 2.0e-130 | 104 | 451 | 353 | + 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 | |
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GO Term | Description |
GO:0005737 | cytoplasm |
GO:0033925 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002273683.1 | 0 | 42 | 738 | 8 | 689 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315137.1 | 0 | 57 | 738 | 26 | 698 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315138.1 | 0 | 39 | 738 | 7 | 695 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520781.1 | 0 | 43 | 738 | 11 | 692 | endo beta n-acetylglucosaminidase, putative [Ricinus communis] |
RefSeq | XP_002520784.1 | 0 | 34 | 738 | 1 | 686 | endo beta n-acetylglucosaminidase, putative [Ricinus communis] |
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 | 3fha_D | 1e-29 | 82 | 516 | 28 | 464 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fha_C | 1e-29 | 82 | 516 | 28 | 464 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fha_B | 1e-29 | 82 | 516 | 28 | 464 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fha_A | 1e-29 | 82 | 516 | 28 | 464 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fhq_F | 2e-29 | 82 | 516 | 28 | 464 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GW895450 | 279 | 9 | 283 | 0 |
GR107739 | 245 | 103 | 347 | 0 |
EL437937 | 286 | 128 | 413 | 0 |
AJ502367 | 226 | 1 | 226 | 0 |
JG621224 | 306 | 153 | 457 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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