Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10016445m |
Family | AA1 |
Protein Properties | Length: 571 Molecular Weight: 64094.1 Isoelectric Point: 9.7756 |
Chromosome | Chromosome/Scaffold: 10 Start: 5728328 End: 5730707 |
Description | laccase 3 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 26 | 553 | 0 |
ELHVREFVIQPKPVKRLCRTHQSITVNGQFPGPNLEVRNGDSLAITVINRARYNISIHWHGIRQLRNPWADGPEYITQCPIRPGQSYTYRFTIEGQEGTL WWHAHSKWLRATVYGALIIYPRLGSPYPFSMPKRDIPILLGEWWDRNPMDVLRLAQFTGAAPNVSDAYTINGQPGDLYRCSRAETTRFPIFPGETVQLRV INAALNQELFFSVANHQLTVVETDSAYTKPFTTSVIMIGPGQTTNVLLTANQRPGRYYMAARAYNSANAPFDNTTTTAILEYVNAPTRRGRGRGQIAPVF PVLPGFNDTATATAFTNRLRYWKRAPVPLQVDDNLFLTVGLGLINCTNPNSPRCQGPNGTRFAASINNQSFVLPRRNSIMQAYYQGMPGIFTTDFPPFPP VQFDYTGNVSRGLWQPVKGTKVYKLKYKANVQIVFQDTSIVTPENHPMHLHGYQFYVVGSGFGNFNPRTDPARFNLFDPPERNTIGTPPGGWVAIRFVAD NPGAWFMHCHIDSHLGWGLAMVFLVENG |
Full Sequence |
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Protein Sequence Length: 571 Download |
MESLSRFFFV SLIALLAYFA LFASAELHVR EFVIQPKPVK RLCRTHQSIT VNGQFPGPNL 60 EVRNGDSLAI TVINRARYNI SIHWHGIRQL RNPWADGPEY ITQCPIRPGQ SYTYRFTIEG 120 QEGTLWWHAH SKWLRATVYG ALIIYPRLGS PYPFSMPKRD IPILLGEWWD RNPMDVLRLA 180 QFTGAAPNVS DAYTINGQPG DLYRCSRAET TRFPIFPGET VQLRVINAAL NQELFFSVAN 240 HQLTVVETDS AYTKPFTTSV IMIGPGQTTN VLLTANQRPG RYYMAARAYN SANAPFDNTT 300 TTAILEYVNA PTRRGRGRGQ IAPVFPVLPG FNDTATATAF TNRLRYWKRA PVPLQVDDNL 360 FLTVGLGLIN CTNPNSPRCQ GPNGTRFAAS INNQSFVLPR RNSIMQAYYQ GMPGIFTTDF 420 PPFPPVQFDY TGNVSRGLWQ PVKGTKVYKL KYKANVQIVF QDTSIVTPEN HPMHLHGYQF 480 YVVGSGFGNF NPRTDPARFN LFDPPERNTI GTPPGGWVAI RFVADNPGAW FMHCHIDSHL 540 GWGLAMVFLV ENGRGQLQSV QAPPLDLPRC * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 6.0e-53 | 33 | 147 | 117 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 8.0e-72 | 43 | 548 | 531 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 5.0e-74 | 49 | 548 | 540 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-90 | 43 | 548 | 545 | + 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 | 32 | 570 | 543 | + 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 | |
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GO Term | Description |
GO:0005507 | copper ion binding |
GO:0016491 | oxidoreductase activity |
GO:0055114 | oxidation-reduction 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 |
RefSeq | NP_180580.1 | 0 | 1 | 570 | 1 | 570 | LAC3 (laccase 3); laccase [Arabidopsis thaliana] |
RefSeq | NP_196330.3 | 0 | 1 | 570 | 1 | 569 | LAC13 (laccase 13); laccase [Arabidopsis thaliana] |
RefSeq | XP_002319955.1 | 0 | 1 | 570 | 8 | 576 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002326089.1 | 0 | 1 | 570 | 8 | 576 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002516345.1 | 0 | 2 | 570 | 9 | 577 | laccase, 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 | 1asq_B | 0 | 43 | 548 | 19 | 521 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |
PDB | 1asq_A | 0 | 43 | 548 | 19 | 521 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |
PDB | 1asp_B | 0 | 43 | 548 | 19 | 521 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |
PDB | 1asp_A | 0 | 43 | 548 | 19 | 521 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |
PDB | 1aso_B | 0 | 43 | 548 | 19 | 521 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |