| Basic Information | |
|---|---|
| Species | Medicago truncatula |
| Cazyme ID | Medtr1g101020.1 |
| Family | CE13 |
| Protein Properties | Length: 538 Molecular Weight: 60660.6 Isoelectric Point: 8.3293 |
| Chromosome | Chromosome/Scaffold: 1 Start: 29576809 End: 29586980 |
| Description | Pectinacetylesterase family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CE13 | 161 | 513 | 0 |
| LYVNMTLVNNARETGAFCLDGSLPAYHLDRGFGAGEDNWLLQFEGGGWCNDLKSCLERAKTRRGSTNYMTKYETFNGILSNNATVNPDFYNWNRVKLRYC DGASFTGNRVFNNGTTKLYFKGQNIWEAIIADILPKGLGKARKALLSGCSAGGLATFHHCDNFTKYLPTNASVKCLSDAGFFLDGRDVSLNHTMRYFFKS VVTLQGSVQNLNKNCTSAMSSYPDLCFFPQYVLKYISTPYFILNSAYDVFQFHNILVPPSADPHGHWNHCKKDPAACTPTEINTLQGFRLSMIAASKPIY FYSNRGGIFINSCFAHCQSESQDTWSGADSPRIINTTIAEAVGDWYFCRNKSK | |||
| Full Sequence |
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| Protein Sequence Length: 538 Download |
| MDNQFTFMRT LPSPFLIHLH RTTNPNFIRR FNWSFVSISK PMFNLYSSSF TSSQSAAEED 60 HNDGNNDTNG TSSFRNFKLN QSTFLASLMP KTEIGVDRFL HSYPHYDGRG VLIAIFELES 120 SGKTMIHNSF SVTMNFAVAF ALFYLITVES WRVHSQEPKK LYVNMTLVNN ARETGAFCLD 180 GSLPAYHLDR GFGAGEDNWL LQFEGGGWCN DLKSCLERAK TRRGSTNYMT KYETFNGILS 240 NNATVNPDFY NWNRVKLRYC DGASFTGNRV FNNGTTKLYF KGQNIWEAII ADILPKGLGK 300 ARKALLSGCS AGGLATFHHC DNFTKYLPTN ASVKCLSDAG FFLDGRDVSL NHTMRYFFKS 360 VVTLQGSVQN LNKNCTSAMS SYPDLCFFPQ YVLKYISTPY FILNSAYDVF QFHNILVPPS 420 ADPHGHWNHC KKDPAACTPT EINTLQGFRL SMIAASKPIY FYSNRGGIFI NSCFAHCQSE 480 SQDTWSGADS PRIINTTIAE AVGDWYFCRN KSKAIDWPYP CDTTCRNLIP VLHNLIP* 540 |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| cd04857 | Peptidases_S8_Tripeptidyl_Aminopeptidase_II | 4.0e-9 | 88 | 117 | 30 | + Peptidase S8 family domain in Tripeptidyl aminopeptidases_II. Tripeptidyl aminopeptidases II are member of the peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Tripeptidyl aminopeptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl aminopeptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing. |
| pfam03283 | PAE | 1.0e-179 | 160 | 515 | 356 | + Pectinacetylesterase. |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN83189.1 | 0 | 151 | 531 | 16 | 374 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002271673.1 | 0 | 150 | 531 | 15 | 393 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002318215.1 | 0 | 134 | 529 | 1 | 391 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002322478.1 | 0 | 160 | 529 | 24 | 392 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002513692.1 | 0 | 137 | 530 | 5 | 395 | pectin acetylesterase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3lxu_X | 0.0008 | 86 | 117 | 13 | 44 | X Chain X, Crystal Structure Of Tripeptidyl Peptidase 2 (Tpp Ii) |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| CA918471 | 253 | 210 | 462 | 0 |
| BG648785 | 245 | 223 | 467 | 0 |
| EL451663 | 322 | 206 | 527 | 0 |
| FY469003 | 238 | 276 | 513 | 0 |
| DT754656 | 275 | 181 | 455 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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