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Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma01g37930.1 |
Family | AA1 |
Protein Properties | Length: 565 Molecular Weight: 62548.8 Isoelectric Point: 8.8822 |
Chromosome | Chromosome/Scaffold: 01 Start: 50166502 End: 50169549 |
Description | laccase 11 |
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 | 557 | 0 |
AATKKYQFDIQVKNVSRLCHAKPIVTVNGRFPGPTIYVREGDRVLVNVTNHAKYNMTIHWHGIKQYRNGWADGPAYITQCPIQTGNSYTYDFNVTGQRGT LWWHAHIFWLRATVYGAIVIMPKPGTPFPFPQPAREFEILLGEWWHKDVEEIETQGNQMGLPPNMSDAHTINGKPGPLFPCSEKHTFAMEVEQGKTYLLR IINAALDDELFFAIGGHNLTVVEVDAVYTKPFTTQTILIAPGQTTNVLVKANQVAGRYFMATRTFMDAPIPVDSKAATAIFQYKGIPNTVLPSLPSLPAA NDTRFALSYNKKLRSLNTPQYPANVPLKVDRNLFYTIGLAKNSCPTCVNGTRLLASLNNVSFVMPQTALLQAHYFNIKGVYRTDFPDKPLTAFNYTGAPL TANLGTSVGTRISKVPFNSTVELVLQDTNLLTVESHPFHLHGYNFFVVGTGIGNFDPAKDPAKYNLVDPIERNTVGVPTGGWTAIRFRADNPGVWFMHCH LELHTGWGLKTAFLVEDGPGQDQSVVPP |
Full Sequence |
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Protein Sequence Length: 565 Download |
MAAGMGFRSH KSLLTILFGF LGLFSFTVEA ATKKYQFDIQ VKNVSRLCHA KPIVTVNGRF 60 PGPTIYVREG DRVLVNVTNH AKYNMTIHWH GIKQYRNGWA DGPAYITQCP IQTGNSYTYD 120 FNVTGQRGTL WWHAHIFWLR ATVYGAIVIM PKPGTPFPFP QPAREFEILL GEWWHKDVEE 180 IETQGNQMGL PPNMSDAHTI NGKPGPLFPC SEKHTFAMEV EQGKTYLLRI INAALDDELF 240 FAIGGHNLTV VEVDAVYTKP FTTQTILIAP GQTTNVLVKA NQVAGRYFMA TRTFMDAPIP 300 VDSKAATAIF QYKGIPNTVL PSLPSLPAAN DTRFALSYNK KLRSLNTPQY PANVPLKVDR 360 NLFYTIGLAK NSCPTCVNGT RLLASLNNVS FVMPQTALLQ AHYFNIKGVY RTDFPDKPLT 420 AFNYTGAPLT ANLGTSVGTR ISKVPFNSTV ELVLQDTNLL TVESHPFHLH GYNFFVVGTG 480 IGNFDPAKDP AKYNLVDPIE RNTVGVPTGG WTAIRFRADN PGVWFMHCHL ELHTGWGLKT 540 AFLVEDGPGQ DQSVVPPPKD LPAC* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 3.0e-58 | 39 | 546 | 555 | + L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized. | ||
PLN02191 | PLN02191 | 3.0e-81 | 30 | 542 | 551 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 1.0e-94 | 28 | 542 | 552 | + oxidoreductase | ||
TIGR03388 | ascorbase | 3.0e-105 | 32 | 538 | 540 | + 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 | 564 | 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 | |
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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 | CBI17500.1 | 0 | 29 | 564 | 7 | 542 | unnamed protein product [Vitis vinifera] |
EMBL | CBI32739.1 | 0 | 29 | 564 | 27 | 562 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266464.1 | 0 | 29 | 564 | 28 | 563 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002310245.1 | 0 | 33 | 564 | 31 | 562 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512915.1 | 0 | 16 | 564 | 10 | 558 | 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 | 30 | 542 | 1 | 521 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
PDB | 1asq_A | 0 | 30 | 542 | 1 | 521 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
PDB | 1asp_B | 0 | 30 | 542 | 1 | 521 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
PDB | 1asp_A | 0 | 30 | 542 | 1 | 521 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
PDB | 1aso_B | 0 | 30 | 542 | 1 | 521 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |