Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10013109m |
Family | AA1 |
Protein Properties | Length: 573 Molecular Weight: 63570.2 Isoelectric Point: 9.5847 |
Chromosome | Chromosome/Scaffold: 2 Start: 8210390 End: 8212913 |
Description | laccase 17 |
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 | 24 | 558 | 0 |
TRHYTLDIKMQNVTRLCHTKSIVSVNGQFPGPKLIAREGDQLLIKVVNHVPNNISIHWHGIRQLRSGWADGPAYITQCPIQTGQSYVYNYTIVGQRGTLF YHAHISWLRATVYGPIIILPKRGVPYPFAKPYKEVPMIFGEWFNADPEAIIRQATQTGGGPNVSDAYTINGLPGPLYNCSAKDTFRLRVKPGKTYLLRLI NAALNDELFFSIANHTVTVVEADAIYVKPFETDTILIAPGQTTNVLLKTKPSYPSASFFMTARPYVTGQGTFDNSTVAGILDYEPPKHARTSIKDLPLFT PVLPALNDTNFATKFSNKLRSLNSKKFPAKVPLKVDRKFFFTVGLGTKPCNHKNNQTCQGPTNTTMFAASISNISFTMPTKALLQSHYSGQSHGVYSPNY PWDPIVKFNYTGTPPNNTMVSNGTNLMVLRYNTSVELVMQDTSILGAESHPLHLHGFNFFVVGQGFGNFDPNKDPKNFNLVDPIERNTVGVPSGGWAAIR FLADNPGVWFMHCHLEVHTSWGLRMAWLVLDGDKP |
Full Sequence |
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Protein Sequence Length: 573 Download |
MAFWLLFAVV SCVLLLPEPA FGITRHYTLD IKMQNVTRLC HTKSIVSVNG QFPGPKLIAR 60 EGDQLLIKVV NHVPNNISIH WHGIRQLRSG WADGPAYITQ CPIQTGQSYV YNYTIVGQRG 120 TLFYHAHISW LRATVYGPII ILPKRGVPYP FAKPYKEVPM IFGEWFNADP EAIIRQATQT 180 GGGPNVSDAY TINGLPGPLY NCSAKDTFRL RVKPGKTYLL RLINAALNDE LFFSIANHTV 240 TVVEADAIYV KPFETDTILI APGQTTNVLL KTKPSYPSAS FFMTARPYVT GQGTFDNSTV 300 AGILDYEPPK HARTSIKDLP LFTPVLPALN DTNFATKFSN KLRSLNSKKF PAKVPLKVDR 360 KFFFTVGLGT KPCNHKNNQT CQGPTNTTMF AASISNISFT MPTKALLQSH YSGQSHGVYS 420 PNYPWDPIVK FNYTGTPPNN TMVSNGTNLM VLRYNTSVEL VMQDTSILGA ESHPLHLHGF 480 NFFVVGQGFG NFDPNKDPKN FNLVDPIERN TVGVPSGGWA AIRFLADNPG VWFMHCHLEV 540 HTSWGLRMAW LVLDGDKPNQ KLLPPPADLP KC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 3.0e-52 | 30 | 146 | 119 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 2.0e-65 | 3 | 546 | 575 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 5.0e-80 | 1 | 548 | 578 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-91 | 24 | 546 | 559 | + 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 | 22 | 572 | 552 | + 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 |
EMBL | CBI16199.1 | 0 | 12 | 572 | 2 | 566 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_200810.1 | 0 | 1 | 572 | 1 | 577 | LAC17 (laccase 17); laccase [Arabidopsis thaliana] |
RefSeq | XP_002284473.1 | 0 | 9 | 572 | 16 | 585 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299296.1 | 0 | 5 | 572 | 15 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531824.1 | 0 | 6 | 572 | 17 | 576 | 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 | 25 | 546 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asq_A | 0 | 25 | 546 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asp_B | 0 | 25 | 546 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asp_A | 0 | 25 | 546 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1aso_B | 0 | 25 | 546 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |