| Basic Information | |
|---|---|
| Species | Prunus persica |
| Cazyme ID | ppa003514m |
| Family | GH37 |
| Protein Properties | Length: 569 Molecular Weight: 64514.1 Isoelectric Point: 6.3367 |
| Chromosome | Chromosome/Scaffold: 5 Start: 12372493 End: 12375922 |
| Description | trehalase 1 |
| 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 |
| GH37 | 45 | 557 | 0 |
| DPKFYVDLSLKFELSKTQTAFDQLPKSANGSASVKDLKEFIAEYFEDAGEDMVLAEPEDFVPEPEGFLPKVKNPEVRAWALEVHLLWKNLSRKVSDGVHK RPEFHTLLPLPQQCVIPGSRFREVYYWDSYWVIRGLLASKMYDTAKAIVSNLIYLIEEYGYVLNGARAYYTNRSQPPLLSAMVFEVYKRTGDVEFARKSL PALIKEHEFWNSGIHKVTVQDSQAQKHTLSRYYAMWNKPRPESSTIDKEFASNISNVYEKQHFYREVASAAESGWDFSTRWMRNHSDFTTLATTSILPVD LNAFILRMEHDIALLAKVTGDHNIAERFLKASEARHEAIKTVFWNAEKGQWLDYWLGNSTCNAEAQTWEACNQNQNVFASNFVPLWIEPFFSDASLVEKV TRSLQSSGLLCDAGIATSLTKSGEQWDFPNGWAPIQHMIVEGLARSGLKEAKLVAEDIAVRWIRTNYVAYKKTGTMHEKYDVEKCGAFGGGGEYIPQTGF GWSNGVVLAFLEE | |||
| Full Sequence |
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| Protein Sequence Length: 569 Download |
| MTFTTKASSA CTSEPGPVKP TIPLVAFFDR LQETALATFG KTKFDPKFYV DLSLKFELSK 60 TQTAFDQLPK SANGSASVKD LKEFIAEYFE DAGEDMVLAE PEDFVPEPEG FLPKVKNPEV 120 RAWALEVHLL WKNLSRKVSD GVHKRPEFHT LLPLPQQCVI PGSRFREVYY WDSYWVIRGL 180 LASKMYDTAK AIVSNLIYLI EEYGYVLNGA RAYYTNRSQP PLLSAMVFEV YKRTGDVEFA 240 RKSLPALIKE HEFWNSGIHK VTVQDSQAQK HTLSRYYAMW NKPRPESSTI DKEFASNISN 300 VYEKQHFYRE VASAAESGWD FSTRWMRNHS DFTTLATTSI LPVDLNAFIL RMEHDIALLA 360 KVTGDHNIAE RFLKASEARH EAIKTVFWNA EKGQWLDYWL GNSTCNAEAQ TWEACNQNQN 420 VFASNFVPLW IEPFFSDASL VEKVTRSLQS SGLLCDAGIA TSLTKSGEQW DFPNGWAPIQ 480 HMIVEGLARS GLKEAKLVAE DIAVRWIRTN YVAYKKTGTM HEKYDVEKCG AFGGGGEYIP 540 QTGFGWSNGV VLAFLEEFGW PQDRRINC* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK13271 | treA | 1.0e-91 | 1 | 556 | 572 | + trehalase; Provisional | ||
| PRK13270 | treF | 2.0e-92 | 80 | 561 | 493 | + trehalase; Provisional | ||
| COG1626 | TreA | 2.0e-104 | 125 | 564 | 456 | + Neutral trehalase [Carbohydrate transport and metabolism] | ||
| PLN02567 | PLN02567 | 0 | 18 | 568 | 554 | + alpha,alpha-trehalase | ||
| pfam01204 | Trehalase | 0 | 44 | 559 | 523 | + Trehalase. Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004555 | alpha,alpha-trehalase activity |
| GO:0005991 | trehalose 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 |
| EMBL | CBI34549.1 | 0 | 4 | 568 | 3 | 543 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002263698.1 | 0 | 4 | 568 | 3 | 564 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002303674.1 | 0 | 1 | 568 | 1 | 568 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002303675.1 | 0 | 1 | 568 | 1 | 568 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002518875.1 | 0 | 4 | 568 | 3 | 567 | alpha,alpha-trehalase, 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 | 2wyn_D | 0 | 17 | 556 | 7 | 500 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 2wyn_C | 0 | 17 | 556 | 7 | 500 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 2wyn_B | 0 | 17 | 556 | 7 | 500 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 2wyn_A | 0 | 17 | 556 | 7 | 500 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 2jjb_D | 0 | 17 | 556 | 7 | 500 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| FQ480353 | 289 | 267 | 554 | 0 |
| FQ452601 | 289 | 267 | 554 | 0 |
| FQ416049 | 286 | 267 | 551 | 0 |
| DT571282 | 288 | 9 | 296 | 0 |
| FQ459065 | 272 | 267 | 537 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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