y
Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra027207 |
Family | GH17 |
Protein Properties | Length: 529 Molecular Weight: 59232.9 Isoelectric Point: 10.0588 |
Chromosome | Chromosome/Scaffold: 05 Start: 19708530 End: 19713484 |
Description | Glycosyl hydrolase superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH17 | 235 | 490 | 0 |
EGIEIIVGLGNEFLKDISVGEDRAMNWVKENVEPFIRSGTKISGIAVGNDILGGTTVELWEVLLPAAKNVYSALRRLGLHTRVEVSSLHSEAVFANSYPP SACTFRDDVVPFMKPLLAFFWQIGSPFYINAYPFLAYKSDPSHIDLNYALFEHSDGIYDAKTKLRYDNMFDAMVDASYAALEKAGFPKVPVKNARTYNRN LRKRLNKRKGTPYRPDMVARAYVFALFNENQKPGPTSERNFGLFKPDGSIAYDIGF |
Full Sequence |
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Protein Sequence Length: 529 Download |
MATALFNTTR SSNLYHHHSV LPPFSQRFHL HRQNFFFLAT PRCLRRLAVV GGPPSPPSPD 60 PPPPENTTQL EGVVGAVTRV EDRVKIFLAV LIWMSLFFWV TVVDGMGFSE FSFASVFKGS 120 QQQKMGTEDE IVSVELPAPS SWKKLFFPNK VKKTEIVFVS PTGEEINNRK QLEQYLKSHP 180 GSPAIAEFDW TTSGTPRRRS ARISEKTKST PSPDKEPPKK RGRTKSSGSK KDTDEGIEII 240 VGLGNEFLKD ISVGEDRAMN WVKENVEPFI RSGTKISGIA VGNDILGGTT VELWEVLLPA 300 AKNVYSALRR LGLHTRVEVS SLHSEAVFAN SYPPSACTFR DDVVPFMKPL LAFFWQIGSP 360 FYINAYPFLA YKSDPSHIDL NYALFEHSDG IYDAKTKLRY DNMFDAMVDA SYAALEKAGF 420 PKVPVKNART YNRNLRKRLN KRKGTPYRPD MVARAYVFAL FNENQKPGPT SERNFGLFKP 480 DGSIAYDIGF TGLKYSSATR PRFGTSLNAL VSTCVFMFLV LHRLLPMS* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00122 | MBD | 2.0e-6 | 134 | 190 | 61 | + MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of proteins that share the methyl-CpG-binding domain (MBD). The MBD consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1. The MBDs present in putative chromatin remodelling subunit, BAZ2A, and putative histone methyltransferase, CLLD8, represent two phylogenetically distinct groups within the MBD protein family. | ||
pfam01429 | MBD | 9.0e-8 | 129 | 198 | 75 | + Methyl-CpG binding domain. The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase. | ||
cd01396 | MeCP2_MBD | 3.0e-10 | 137 | 199 | 72 | + MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a protein family that share the methyl-CpG-binding domain (MBD). The MBD, consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1. | ||
pfam00332 | Glyco_hydro_17 | 3.0e-63 | 236 | 490 | 272 | + Glycosyl hydrolases family 17. |
Gene Ontology | |
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GO Term | Description |
GO:0003677 | DNA binding |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005634 | nucleus |
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 | BAB02311.1 | 0 | 236 | 514 | 81 | 380 | beta-1,3-glucanase-like protein [Arabidopsis thaliana] |
EMBL | CBI36326.1 | 0 | 236 | 528 | 86 | 396 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_188201.1 | 0 | 236 | 514 | 89 | 388 | glycosyl hydrolase family 17 protein [Arabidopsis thaliana] |
RefSeq | XP_002299750.1 | 0 | 236 | 499 | 63 | 345 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002327527.1 | 0 | 236 | 499 | 54 | 336 | predicted protein [Populus trichocarpa] |
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 | 1ghs_B | 0 | 234 | 490 | 45 | 306 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1ghs_A | 0 | 234 | 490 | 45 | 306 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 2cyg_A | 4.2039e-45 | 234 | 490 | 45 | 312 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 3f55_D | 9.94922e-44 | 237 | 491 | 49 | 316 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 3f55_C | 9.94922e-44 | 237 | 491 | 49 | 316 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |