| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s196_77V6.1 |
| Family | GH37 |
| Protein Properties | Length: 606 Molecular Weight: 68205.4 Isoelectric Point: 5.3104 |
| Chromosome | Chromosome/Scaffold: 196 Start: 549555 End: 554210 |
| Description | trehalase 1 |
| 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 |
| GH37 | 75 | 590 | 0 |
| DPKLYVDLPLKSTLKETVEAFRSLPRAPITGSVDRDTLKTFLKDYFGETGSDLVPYTPEDHLANPPDFLPRVQNTDARKWGLKVHSLWPSLTRLVCPTVE REPDRHTLLPLKHPFIVPGERFREVYYWDSYWVIRGLLASKMKKTAAGMIDNFLAVVQAYGFLPNGARTYYENRSQPPFLSRMVRAIFSATDDLKLATRA LPLLLVEHDFWVTGSHVVTIRDSQGRDHRLSRYSAHWDQPRPECSTIDKCIAGGFSKLKQQQLYHDIATAAESGWDFSSRWMEDQEQLSSMKTSSIIPVD LNAFLLQMELDIAYLAKALNNTSVAKRFTRAVDARKRAFEAILWNENKSQWLDYWLPLQKPVKGVKKIYMWDSDRANQNVYASNFVPLWCGLLSAGDAKI DKVVEALSSSGLILPGGIATSLIKTGQQWDFPNAWAPLQHMLIEGLILSGSPKARELAESITRSWLRSNYLAFQRFGHMVEKYDARYCGEVGGGGEYITQ TGFGWTNGVVLTLLND | |||
| Full Sequence |
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| Protein Sequence Length: 606 Download |
| MSVDDEECVE SGAVVKKVNS GVKEHGFIVD MVEEFGEDGG YGEGVYDDGA GELLCFLMDL 60 QSTAMDSFGG DAEFDPKLYV DLPLKSTLKE TVEAFRSLPR APITGSVDRD TLKTFLKDYF 120 GETGSDLVPY TPEDHLANPP DFLPRVQNTD ARKWGLKVHS LWPSLTRLVC PTVEREPDRH 180 TLLPLKHPFI VPGERFREVY YWDSYWVIRG LLASKMKKTA AGMIDNFLAV VQAYGFLPNG 240 ARTYYENRSQ PPFLSRMVRA IFSATDDLKL ATRALPLLLV EHDFWVTGSH VVTIRDSQGR 300 DHRLSRYSAH WDQPRPECST IDKCIAGGFS KLKQQQLYHD IATAAESGWD FSSRWMEDQE 360 QLSSMKTSSI IPVDLNAFLL QMELDIAYLA KALNNTSVAK RFTRAVDARK RAFEAILWNE 420 NKSQWLDYWL PLQKPVKGVK KIYMWDSDRA NQNVYASNFV PLWCGLLSAG DAKIDKVVEA 480 LSSSGLILPG GIATSLIKTG QQWDFPNAWA PLQHMLIEGL ILSGSPKARE LAESITRSWL 540 RSNYLAFQRF GHMVEKYDAR YCGEVGGGGE YITQTGFGWT NGVVLTLLND YGWPEDLPLD 600 FDYKS* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK13272 | treA | 3.0e-91 | 147 | 592 | 458 | + trehalase; Provisional | ||
| PRK13271 | treA | 3.0e-93 | 161 | 600 | 446 | + trehalase; Provisional | ||
| COG1626 | TreA | 2.0e-99 | 161 | 595 | 447 | + Neutral trehalase [Carbohydrate transport and metabolism] | ||
| PLN02567 | PLN02567 | 0 | 53 | 601 | 550 | + alpha,alpha-trehalase | ||
| pfam01204 | Trehalase | 0 | 74 | 592 | 528 | + 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ABO61746.1 | 0 | 42 | 599 | 11 | 568 | trehalase [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001769611.1 | 0 | 42 | 599 | 5 | 554 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001771381.1 | 0 | 65 | 605 | 1 | 541 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001775598.1 | 0 | 53 | 599 | 4 | 542 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001775772.1 | 0 | 31 | 605 | 1 | 571 | predicted protein [Physcomitrella patens subsp. patens] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2wyn_D | 0 | 158 | 600 | 89 | 510 | A Chain A, Structure Of E. Coli Beta-Glucuronidase Bound With A Novel, Potent Inhibitor 1-((6,7-Dimethyl-2-Oxo-1,2-Dihydroquinolin-3-Yl)methyl)-1- (2-Hydroxyethyl)-3-(3-Methoxyphenyl)thiourea |
| PDB | 2wyn_C | 0 | 158 | 600 | 89 | 510 | A Chain A, Structure Of E. Coli Beta-Glucuronidase Bound With A Novel, Potent Inhibitor 1-((6,7-Dimethyl-2-Oxo-1,2-Dihydroquinolin-3-Yl)methyl)-1- (2-Hydroxyethyl)-3-(3-Methoxyphenyl)thiourea |
| PDB | 2wyn_B | 0 | 158 | 600 | 89 | 510 | A Chain A, Structure Of E. Coli Beta-Glucuronidase Bound With A Novel, Potent Inhibitor 1-((6,7-Dimethyl-2-Oxo-1,2-Dihydroquinolin-3-Yl)methyl)-1- (2-Hydroxyethyl)-3-(3-Methoxyphenyl)thiourea |
| PDB | 2wyn_A | 0 | 158 | 600 | 89 | 510 | A Chain A, Structure Of E. Coli Beta-Glucuronidase Bound With A Novel, Potent Inhibitor 1-((6,7-Dimethyl-2-Oxo-1,2-Dihydroquinolin-3-Yl)methyl)-1- (2-Hydroxyethyl)-3-(3-Methoxyphenyl)thiourea |
| PDB | 2jjb_D | 0 | 158 | 600 | 89 | 510 | A Chain A, Structure Of E. Coli Beta-Glucuronidase Bound With A Novel, Potent Inhibitor 1-((6,7-Dimethyl-2-Oxo-1,2-Dihydroquinolin-3-Yl)methyl)-1- (2-Hydroxyethyl)-3-(3-Methoxyphenyl)thiourea |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| trehalose degradation II (trehalase) | TREHALA-RXN | EC-3.2.1.28 | α,α-trehalase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| EX329585 | 306 | 288 | 587 | 0 |
| CV735561 | 294 | 152 | 445 | 0 |
| FQ480353 | 291 | 298 | 587 | 0 |
| FQ452601 | 291 | 298 | 587 | 0 |
| FQ416049 | 288 | 298 | 584 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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