Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi2g54680.1 |
Family | AA1 |
Protein Properties | Length: 578 Molecular Weight: 63160.9 Isoelectric Point: 8.946 |
Chromosome | Chromosome/Scaffold: 2 Start: 53524201 End: 53527247 |
Description | laccase 17 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 30 | 564 | 0 |
TRHYDFDVQMAKVTRLCGSKSIVTVNGQFPGPELVAREGDRVHVRVTNHVSHNMSLHWHGIRQMQTGWADGPAYITQCPIQMGQTYVYKFTITGQRGTLW WHAHISWHRATVYGAIVILPKLGVPYPFAAPHKEVPVIFGEWWAADTEVVMSQALKVGGAPNISDAFTINGLPGPLYNCSAQDTFKLKVTPGKTYLLRLI NAALNDELFFSVANHTLTVVEVDAVYVKPFTVKTIVISPGQTTNVLLTAKPVNPKANFYMSAAPYSVIRPGTFDNTTVAGILEYHEDPSSSSSFDKNLPL FKPMLPRFNDTKFVTNFTTKLRSLATTKYPAAVPQTVDKRFFFTIGLGTLPCPKNMTCQGPNGTQFAAAVNNVSLVLPTKALLQSHFTGLTTGVYASDFP AMPLSPFNYTGTPPNNTNVATGTKLLALPFNTSVELVMQDTSVLGIESHPLHLHGFNYFVVGQGFGNYDSAKDPAKFNLVDPVERNTVGVPAGGWVAIRF LADNPGVWFMHCHLEVHTTWGLRMAWLVHDGSKPN |
Full Sequence |
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Protein Sequence Length: 578 Download |
MAMAISSGLP ACSVVMATLM VLIIQAQGIT RHYDFDVQMA KVTRLCGSKS IVTVNGQFPG 60 PELVAREGDR VHVRVTNHVS HNMSLHWHGI RQMQTGWADG PAYITQCPIQ MGQTYVYKFT 120 ITGQRGTLWW HAHISWHRAT VYGAIVILPK LGVPYPFAAP HKEVPVIFGE WWAADTEVVM 180 SQALKVGGAP NISDAFTING LPGPLYNCSA QDTFKLKVTP GKTYLLRLIN AALNDELFFS 240 VANHTLTVVE VDAVYVKPFT VKTIVISPGQ TTNVLLTAKP VNPKANFYMS AAPYSVIRPG 300 TFDNTTVAGI LEYHEDPSSS SSFDKNLPLF KPMLPRFNDT KFVTNFTTKL RSLATTKYPA 360 AVPQTVDKRF FFTIGLGTLP CPKNMTCQGP NGTQFAAAVN NVSLVLPTKA LLQSHFTGLT 420 TGVYASDFPA MPLSPFNYTG TPPNNTNVAT GTKLLALPFN TSVELVMQDT SVLGIESHPL 480 HLHGFNYFVV GQGFGNYDSA KDPAKFNLVD PVERNTVGVP AGGWVAIRFL ADNPGVWFMH 540 CHLEVHTTWG LRMAWLVHDG SKPNQKLLPP PSDMPKC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 1.0e-53 | 36 | 150 | 117 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 9.0e-77 | 15 | 551 | 566 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-86 | 12 | 553 | 574 | + oxidoreductase | ||
TIGR03388 | ascorbase | 3.0e-101 | 30 | 546 | 549 | + 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 | 28 | 577 | 551 | + 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 |
GenBank | AAL73968.1 | 0 | 1 | 577 | 1 | 578 | AF465468_1 laccase LAC5-6 [Lolium perenne] |
GenBank | EAZ14115.1 | 0 | 25 | 577 | 23 | 577 | hypothetical protein OsJ_04039 [Oryza sativa Japonica Group] |
GenBank | EEC71777.1 | 0 | 25 | 577 | 23 | 577 | hypothetical protein OsI_04389 [Oryza sativa Indica Group] |
RefSeq | NP_001044772.1 | 0 | 25 | 577 | 25 | 579 | Os01g0842400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001105875.1 | 0 | 3 | 577 | 1 | 587 | putative laccase [Zea mays] |
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 | 31 | 551 | 4 | 517 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
PDB | 1asq_A | 0 | 31 | 551 | 4 | 517 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
PDB | 1asp_B | 0 | 31 | 551 | 4 | 517 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
PDB | 1asp_A | 0 | 31 | 551 | 4 | 517 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
PDB | 1aso_B | 0 | 31 | 551 | 4 | 517 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |