| Basic Information | |
|---|---|
| Species | Brachypodium distachyon |
| Cazyme ID | Bradi1g45890.1 |
| Family | CE10 |
| Protein Properties | Length: 717 Molecular Weight: 79122.7 Isoelectric Point: 5.1721 |
| Chromosome | Chromosome/Scaffold: 1 Start: 44183156 End: 44193172 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 461 | 689 | 3e-27 |
| AYFYPPLNPMFQGLPDERPPLLVKTHGGPTAEAQGILDLSVQYWTSRGWAFLDVNYGGSTGYGREYRERLLEKWGIVDVDDCCSCARFLVENGKVDDQRL CITGRSAGGYTTLASLAFRDTFKAGASLYGVGDLSLLRAETHKFESHYMDSLVGNERAYYERSPINFVNKFTCPVILFQGLDDKVVPPDQARAIYKALKE KGLPVALVEYEGEQHGFRKAENIKFTLEQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 717 Download |
| MATLLASIFL LPATCSASAP GLLLRGAIPR FRRALASPPR MSSSSASPAP AAAAAGEKPA 60 AAPYGSWRSP ITADVVSGAG KRLGGIALAG DGRLLWIEGR PEEKGRMVIV KEDDNPVDVI 120 PQEFAARTVA QEYGGGAFAV QDNVVVFSNY KDQRLYKQVT GTGSLPVPLT PDYGAPDVSY 180 ADGVFDPHFN RYVTVMEDRR KSSLNPTTTI ASINLSGGDV HEPKVLISGN DFYAFPRIDQ 240 NKMRMAWIEW GHPNMPWDKS ELWVGYFSEN GDLTKRVCVA GGNPMLVESP TEPKWSPKGQ 300 LFFISDRGSG FWNIYKWVEH TNEVVPVYTL DAEFTRPLWV FGISCYDFLG KSNHIILTYR 360 QLGRSYLGVL ECESGSVSLL DIPFSDLSDV VTGNDYFYIE GASASIPMSI AKVTLDESKA 420 KVVSFSIVWS SSPDVVQYKP FFSTPEFIEF PTSTPGQNAY AYFYPPLNPM FQGLPDERPP 480 LLVKTHGGPT AEAQGILDLS VQYWTSRGWA FLDVNYGGST GYGREYRERL LEKWGIVDVD 540 DCCSCARFLV ENGKVDDQRL CITGRSAGGY TTLASLAFRD TFKAGASLYG VGDLSLLRAE 600 THKFESHYMD SLVGNERAYY ERSPINFVNK FTCPVILFQG LDDKVVPPDQ ARAIYKALKE 660 KGLPVALVEY EGEQHGFRKA ENIKFTLEQQ MLFFARLVGK FEVADDITPI KIENFD* 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0657 | Aes | 3.0e-8 | 539 | 677 | 163 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 3.0e-8 | 539 | 677 | 162 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| COG0412 | COG0412 | 7.0e-11 | 444 | 677 | 244 | + Dienelactone hydrolase and related enzymes [Secondary metabolites biosynthesis, transport, and catabolism] | ||
| pfam00326 | Peptidase_S9 | 3.0e-45 | 497 | 700 | 209 | + Prolyl oligopeptidase family. | ||
| COG1506 | DAP2 | 8.0e-64 | 222 | 701 | 489 | + Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0006508 | proteolysis |
| GO:0008152 | metabolic process |
| GO:0008236 | serine-type peptidase activity |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEC80224.1 | 0 | 52 | 716 | 20 | 683 | hypothetical protein OsI_22153 [Oryza sativa Indica Group] |
| RefSeq | NP_001057137.1 | 0 | 52 | 716 | 20 | 683 | Os06g0215300 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001152650.1 | 0 | 57 | 716 | 15 | 674 | acylaminoacyl-peptidase1 [Zea mays] |
| RefSeq | XP_002284264.1 | 0 | 51 | 716 | 2 | 675 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002438048.1 | 0 | 1 | 716 | 1 | 721 | hypothetical protein SORBIDRAFT_10g007270 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3azo_B | 0 | 62 | 704 | 5 | 653 | A Chain A, Crystal Structure Of Puromycin Hydrolase |
| PDB | 3azo_A | 0 | 62 | 704 | 5 | 653 | A Chain A, Crystal Structure Of Puromycin Hydrolase |
| PDB | 3azq_B | 0 | 60 | 704 | 3 | 653 | A Chain A, Crystal Structure Of Puromycin Hydrolase |
| PDB | 3azq_A | 0 | 60 | 704 | 3 | 653 | A Chain A, Crystal Structure Of Puromycin Hydrolase |
| PDB | 3azp_B | 0 | 60 | 704 | 3 | 653 | A Chain A, Crystal Structure Of Puromycin Hydrolase S511a Mutant |
