y
Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10434158g0010 |
Family | CBM43 |
Protein Properties | Length: 392 Molecular Weight: 43864.8 Isoelectric Point: 9.4408 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM43 | 296 | 378 | 4.3e-28 |
WCVVDAKADVSALPSAIKSACSQGYNTCAAIQPGKPCYQPNTVIDHASYAFNSYWQKSKNFYIGCDFNKTARLVTKDPSHGTC | |||
GH17 | 166 | 271 | 4.4e-33 |
KQLDAAVAAMSKLGYEDIRLAIAETGWPNAGDLSQLGANIFNAAHYNRRVIKRMLADPPLGTPRRPKQFIPTYIFSLFNENQKPGPGTERHWGFVYPNGA TMYEID | |||
GH17 | 39 | 166 | 9.3e-37 |
IGIAYGPLGDNLPSVQEAMQLIQRMKIDRVKIYSTDPRILKALAHTGIKVSVMVRTEDIASVSASQSFADEWVNKNIVYFYPATKINIILVGNEVLTDYS NKQTWYQLVPAMQRIWRALLRYNLTNIK |
Full Sequence |
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Protein Sequence Length: 392 Download |
MLHPTGTIRT MPIPGRKVFC LLLAILGVII HAYAEKYSIG IAYGPLGDNL PSVQEAMQLI 60 QRMKIDRVKI YSTDPRILKA LAHTGIKVSV MVRTEDIASV SASQSFADEW VNKNIVYFYP 120 ATKINIILVG NEVLTDYSNK QTWYQLVPAM QRIWRALLRY NLTNIKQLDA AVAAMSKLGY 180 EDIRLAIAET GWPNAGDLSQ LGANIFNAAH YNRRVIKRML ADPPLGTPRR PKQFIPTYIF 240 SLFNENQKPG PGTERHWGFV YPNGATMYEI DLTGKLQDSQ YKPLPPPPPP YKGKLWCVVD 300 AKADVSALPS AIKSACSQGY NTCAAIQPGK PCYQPNTVID HASYAFNSYW QKSKNFYIGC 360 DFNKTARLVT KDPSHGTCTY PFEECVQKSV LC 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07983 | X8 | 5.0e-15 | 295 | 366 | 77 | + X8 domain. The X8 domain domain contains at least 6 conserved cysteine residues that presumably form three disulphide bridges. The domain is found in an Olive pollen allergen as well as at the C-terminus of several families of glycosyl hydrolases. This domain may be involved in carbohydrate binding. This domain is characteristic of GPI-anchored domains. | ||
pfam00332 | Glyco_hydro_17 | 4.0e-27 | 39 | 166 | 129 | + Glycosyl hydrolases family 17. | ||
pfam00332 | Glyco_hydro_17 | 8.0e-30 | 168 | 271 | 104 | + Glycosyl hydrolases family 17. | ||
smart00768 | X8 | 2.0e-33 | 295 | 380 | 86 | + Possibly involved in carbohydrate binding. The X8 domain, which may be involved in carbohydrate binding, is found in an Olive pollen antigen as well as at the C terminus of family 17 glycosyl hydrolases. It contains 6 conserved cysteine residues which presumably form three disulfide bridges. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI39470.1 | 3e-30 | 39 | 166 | 29 | 156 | unnamed protein product [Vitis vinifera] |
EMBL | CBI39470.1 | 0 | 166 | 381 | 246 | 463 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002298669.1 | 0 | 166 | 381 | 241 | 458 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002534357.1 | 0.0000000000005 | 91 | 166 | 1 | 75 | Glucan endo-1,3-beta-glucosidase precursor, putative [Ricinus communis] |
RefSeq | XP_002534357.1 | 0 | 105 | 381 | 128 | 383 | Glucan endo-1,3-beta-glucosidase precursor, 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 | 2jon_A | 1e-16 | 286 | 381 | 3 | 97 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 2cyg_A | 6e-16 | 39 | 172 | 1 | 131 | 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 | 2cyg_A | 0.00000000000002 | 168 | 272 | 215 | 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 | 1ghr_A | 0.000000000000007 | 168 | 272 | 211 | 306 | 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 | 1ghr_A | 0.000000002 | 39 | 166 | 1 | 122 | 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 |