Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_118833g0010 |
Family | AA1 |
Protein Properties | Length: 619 Molecular Weight: 68661.2 Isoelectric Point: 10.066 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 66 | 607 | 0 |
TTRHYSFHVKLKNVTRLCHTKPLITVNGKSPGPKIVVREGDRVIIRVHNHVKDNVSIHWHGVRQLRSGWADGPAYITQCPIQTGKTYTYNFTVTGQRGTL WWHAHISWLRASVYGAFIIYPKRGVPYPFPKPYKEVPMILGEWWNADTEKVVNQSMITGGGPNVSDCYSINGHPGPLYNCTAFNDTFILNVDPGKTYLLR IINAALNDEMFISIANHTMTVVEVDAVYTKHVTTNTIMIAPGQTTNVLLTASASDYKGKKFFILASPYATGQGTFDNTTLAGILSYSKHVHFNTSHLNSS SNFTNAILPKLPVFNDTAFATNFTLKLKSLANAQYPALVPQTVDRKFYFIVSLGLNPCPKGQKCQGVNGTKFTASINNISFVMPSVALLQSHYTGKMKGV YKTNFPDNPLFPFNYTGNPPKNVTTPNGTRVKVLPFNTTVQVVLQDTSIAGAESHPLHLHGFNFFIVGQGFGNYNETKDSPKFNLIDPVERNTAGVPSGG WVALRFRADNPGVWFMHCHLEVHTSWGLKMAWVVKNGKGPSQ |
Full Sequence |
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Protein Sequence Length: 619 Download |
MHSITIFRSI VSAVVSHLRS VTDRTLIPIS LTQIMMMAMA RAEYGTKLII QLLFVLLLVQ 60 FVSGKTTRHY SFHVKLKNVT RLCHTKPLIT VNGKSPGPKI VVREGDRVII RVHNHVKDNV 120 SIHWHGVRQL RSGWADGPAY ITQCPIQTGK TYTYNFTVTG QRGTLWWHAH ISWLRASVYG 180 AFIIYPKRGV PYPFPKPYKE VPMILGEWWN ADTEKVVNQS MITGGGPNVS DCYSINGHPG 240 PLYNCTAFND TFILNVDPGK TYLLRIINAA LNDEMFISIA NHTMTVVEVD AVYTKHVTTN 300 TIMIAPGQTT NVLLTASASD YKGKKFFILA SPYATGQGTF DNTTLAGILS YSKHVHFNTS 360 HLNSSSNFTN AILPKLPVFN DTAFATNFTL KLKSLANAQY PALVPQTVDR KFYFIVSLGL 420 NPCPKGQKCQ GVNGTKFTAS INNISFVMPS VALLQSHYTG KMKGVYKTNF PDNPLFPFNY 480 TGNPPKNVTT PNGTRVKVLP FNTTVQVVLQ DTSIAGAESH PLHLHGFNFF IVGQGFGNYN 540 ETKDSPKFNL IDPVERNTAG VPSGGWVALR FRADNPGVWF MHCHLEVHTS WGLKMAWVVK 600 NGKGPSQSLP PPPPDLPHC |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 1.0e-54 | 70 | 601 | 577 | + L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized. | ||
PLN02191 | PLN02191 | 7.0e-68 | 68 | 598 | 557 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 9.0e-79 | 67 | 593 | 549 | + oxidoreductase | ||
TIGR03388 | ascorbase | 1.0e-92 | 67 | 593 | 565 | + L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. | ||
TIGR03389 | laccase | 0 | 67 | 604 | 539 | + laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAK37823.1 | 0 | 35 | 604 | 1 | 571 | laccase [Pinus taeda] |
GenBank | AAK37827.1 | 0 | 65 | 608 | 43 | 580 | AF132123_1 laccase [Pinus taeda] |
GenBank | AAK37828.1 | 0 | 48 | 604 | 13 | 563 | AF132124_1 laccase [Pinus taeda] |
RefSeq | XP_002299296.1 | 0 | 56 | 619 | 14 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531824.1 | 0 | 45 | 619 | 14 | 576 | laccase, 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 | 1asq_B | 0 | 68 | 609 | 4 | 536 | 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 | 1asq_A | 0 | 68 | 609 | 4 | 536 | 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 | 1asp_B | 0 | 68 | 609 | 4 | 536 | 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 | 1asp_A | 0 | 68 | 609 | 4 | 536 | 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 | 1aso_B | 0 | 68 | 609 | 4 | 536 | 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 |