y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_004439m |
Family | AA1 |
Protein Properties | Length: 577 Molecular Weight: 63554.9 Isoelectric Point: 9.6078 |
Chromosome | Chromosome/Scaffold: 07991 Start: 542961 End: 545385 |
Description | laccase 2 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 32 | 562 | 0 |
TRHYKFNIVSINVTRLCRTKSMVTVNGQFPGPPVVAREGDHLLVKVVNHVSSNITIHWHGIRQLRNGWADGPSYITQCPIQTNDTYVYNFTITGQRGTLL WHAHFRELRATVHGALVILPPHNSSYPFPKPYKEVTILLGEWYNTDPEAIINQALQTGAAPNVSDAYTINGLPGPLYNCSAKDTYRLKVKPGKTYLLRVI NAAVDDDLFFTIANHSVIVVEADATYVKPFETELLLISPGQTTNVLLKTKPIAPNAKFFILARPYSTSLGAIDNTTVAGILEYKTSSNSSKSKRLPVVRP PLPPINATSVAANYSSRFRRLVNAHFPANVPQKVDKNFYFTVGLGTSPCPKNQTCQGPNGTKFAASINNNSLVLPSTAILQSYYFKKSNGVYTSNFPRFP PKPFNYTGTPPNITFVAKGTKVAVLPFNASVEVVLQDTSILGIERHPLHLHGYNFYVVGQGFGNFDSKNDPKNYNLVDPVELNTVGVPSGGWVAIRFFAD NPGVWFMHCHFDVHLNWGLAMAWIVLDGKHP |
Full Sequence |
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Protein Sequence Length: 577 Download |
MDTSSYVLLP AFLVAALFFF CAVPQVANAG ITRHYKFNIV SINVTRLCRT KSMVTVNGQF 60 PGPPVVAREG DHLLVKVVNH VSSNITIHWH GIRQLRNGWA DGPSYITQCP IQTNDTYVYN 120 FTITGQRGTL LWHAHFRELR ATVHGALVIL PPHNSSYPFP KPYKEVTILL GEWYNTDPEA 180 IINQALQTGA APNVSDAYTI NGLPGPLYNC SAKDTYRLKV KPGKTYLLRV INAAVDDDLF 240 FTIANHSVIV VEADATYVKP FETELLLISP GQTTNVLLKT KPIAPNAKFF ILARPYSTSL 300 GAIDNTTVAG ILEYKTSSNS SKSKRLPVVR PPLPPINATS VAANYSSRFR RLVNAHFPAN 360 VPQKVDKNFY FTVGLGTSPC PKNQTCQGPN GTKFAASINN NSLVLPSTAI LQSYYFKKSN 420 GVYTSNFPRF PPKPFNYTGT PPNITFVAKG TKVAVLPFNA SVEVVLQDTS ILGIERHPLH 480 LHGYNFYVVG QGFGNFDSKN DPKNYNLVDP VELNTVGVPS GGWVAIRFFA DNPGVWFMHC 540 HFDVHLNWGL AMAWIVLDGK HPNEKVLPPP SDLPKC* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 7.0e-48 | 38 | 152 | 117 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 2.0e-68 | 48 | 564 | 551 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 5.0e-76 | 25 | 550 | 562 | + oxidoreductase | ||
TIGR03388 | ascorbase | 4.0e-88 | 32 | 550 | 547 | + 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 | 30 | 576 | 548 | + 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 | XP_002299296.1 | 0 | 5 | 576 | 4 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002308164.1 | 0 | 9 | 576 | 13 | 580 | laccase 110b [Populus trichocarpa] |
RefSeq | XP_002313424.1 | 0 | 12 | 576 | 18 | 576 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002329138.1 | 0 | 4 | 576 | 3 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520541.1 | 0 | 22 | 576 | 24 | 579 | 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 | 33 | 552 | 4 | 519 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asq_A | 0 | 33 | 552 | 4 | 519 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asp_B | 0 | 33 | 552 | 4 | 519 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asp_A | 0 | 33 | 552 | 4 | 519 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1aso_B | 0 | 33 | 552 | 4 | 519 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |