| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_004756m |
| Family | AA1 |
| Protein Properties | Length: 560 Molecular Weight: 62188.8 Isoelectric Point: 9.2876 |
| Chromosome | Chromosome/Scaffold: 09231 Start: 204210 End: 206461 |
| Description | laccase 11 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA1 | 25 | 545 | 0 |
| AAVKRYQFDIQVRKVSRLCHAKPIVTVNGRFPGPTIYVREGDRVLVNVTNYAQYNMSIHWHGLKQFRNGWADGPAYVTQCPIKTGQSYTYDFNVKGQRGT LWWHAHIFWLRATVYGAIVIMPKLGNPVPFPRPQMEEVIILGEWWNYDVEEIVKQGNKLGLPPYASDAHTINGKPGPLFPCSEKHTFAMEVEQGKTYLLR IINAALNDELFFAIAGHKMTVVEIDAVYTKPFTTEAILIAPGQTTNVVVQATQSPGRYFMAARPFMDAPLSIDNKTATAILRYKCIPNTVFPLLPQLPAP NDTAFALSYNSKLRSLNTRQFPANVPLKVDRHLFYTIGLGMNPCSSCLNGTQLTASLNNITFVMPQVGLLQAHYFNINGVFTTDFPDNPPTPFNYTGAPL TANLGTTLGTRLSKIAYNSTVQLVLQGTNLLIVESHPFHLHGYNFFVVGTGIGNFDPKKDPAKFNLVDPPERNTVAVPTGGWTAIRFRADNPGVWFMHCH LELHTGWGLKTALVVENGKGS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 560 Download |
| MALSKRVCVL FLFFIGLISR PPVEAAVKRY QFDIQVRKVS RLCHAKPIVT VNGRFPGPTI 60 YVREGDRVLV NVTNYAQYNM SIHWHGLKQF RNGWADGPAY VTQCPIKTGQ SYTYDFNVKG 120 QRGTLWWHAH IFWLRATVYG AIVIMPKLGN PVPFPRPQME EVIILGEWWN YDVEEIVKQG 180 NKLGLPPYAS DAHTINGKPG PLFPCSEKHT FAMEVEQGKT YLLRIINAAL NDELFFAIAG 240 HKMTVVEIDA VYTKPFTTEA ILIAPGQTTN VVVQATQSPG RYFMAARPFM DAPLSIDNKT 300 ATAILRYKCI PNTVFPLLPQ LPAPNDTAFA LSYNSKLRSL NTRQFPANVP LKVDRHLFYT 360 IGLGMNPCSS CLNGTQLTAS LNNITFVMPQ VGLLQAHYFN INGVFTTDFP DNPPTPFNYT 420 GAPLTANLGT TLGTRLSKIA YNSTVQLVLQ GTNLLIVESH PFHLHGYNFF VVGTGIGNFD 480 PKKDPAKFNL VDPPERNTVA VPTGGWTAIR FRADNPGVWF MHCHLELHTG WGLKTALVVE 540 NGKGSDQSVL PPPKDLPSC* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02191 | PLN02191 | 9.0e-72 | 7 | 533 | 567 | + L-ascorbate oxidase | ||
| PLN02604 | PLN02604 | 3.0e-89 | 6 | 542 | 573 | + oxidoreductase | ||
| TIGR03388 | ascorbase | 5.0e-95 | 27 | 533 | 552 | + 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 | 25 | 559 | 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. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0016491 | oxidoreductase activity |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI32739.1 | 0 | 22 | 559 | 25 | 562 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002305436.1 | 0 | 29 | 559 | 10 | 540 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002313847.1 | 0 | 2 | 559 | 4 | 561 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002512915.1 | 0 | 1 | 559 | 1 | 558 | laccase, putative [Ricinus communis] |
| RefSeq | XP_002519529.1 | 0 | 10 | 559 | 11 | 559 | laccase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1asq_B | 0 | 25 | 540 | 1 | 526 | 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 | 1asq_A | 0 | 25 | 540 | 1 | 526 | 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 | 1asp_B | 0 | 25 | 540 | 1 | 526 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
