Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.002G031600.1 |
Family | AA1 |
Protein Properties | Length: 565 Molecular Weight: 62532.3 Isoelectric Point: 7.68 |
Chromosome | Chromosome/Scaffold: 02 Start: 3250393 End: 3253687 |
Description | laccase 11 |
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 | 30 | 551 | 0 |
AATKKYQFDIQVKNVSRLCHAKPIVTVNGRFPGPTIYVREGDRVQVNVTNHAKYNMSIHWHGIKQYRNGWADGPAYITQCPIQTGSSYTYDFNVTGQRGT LWWHAHILWLRATVYGAIVIMPKPGTPFPFPQPAREFEILLGEWWHNDVEAVETQGNQMGLPPNMSDAHTINGKPGPLFPCSEKHTYAMEVEQGKSYLLR IINAALDDELFFAIAGHNMTVVEVDAVYTKPFTTQTIIIAPGQTTNVLVKANQVAGRYFMATRTFMDAPIPVDNKSATAIFQYKGIPNTVLPFPPSLPAA NDTPFALSYNNKIRSLNSPQYPANVPLEVDRNLFYTIGLAQNSCPTCVNGTRLLASLNNVSFVMPQTALLQAHYFNIKGVYRTDFPDKPSTTFNYTGAPL TANLGTSTGTRISKVPFNSTVELVLQDTNLLTVESHPFHLHGYNFFVVGTGIGNFDPSKDPAKYNLVDPIERNTVGVPTGGWTAIRFRADNPGVWFMHCH LELHTGWGLKTAFLVEDGPGQE |
Full Sequence |
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Protein Sequence Length: 565 Download |
MAAGMDFSSH RSLLIIIFGF LGLFSFTVEA ATKKYQFDIQ VKNVSRLCHA KPIVTVNGRF 60 PGPTIYVREG DRVQVNVTNH AKYNMSIHWH GIKQYRNGWA DGPAYITQCP IQTGSSYTYD 120 FNVTGQRGTL WWHAHILWLR ATVYGAIVIM PKPGTPFPFP QPAREFEILL GEWWHNDVEA 180 VETQGNQMGL PPNMSDAHTI NGKPGPLFPC SEKHTYAMEV EQGKSYLLRI INAALDDELF 240 FAIAGHNMTV VEVDAVYTKP FTTQTIIIAP GQTTNVLVKA NQVAGRYFMA TRTFMDAPIP 300 VDNKSATAIF QYKGIPNTVL PFPPSLPAAN DTPFALSYNN KIRSLNSPQY PANVPLEVDR 360 NLFYTIGLAQ NSCPTCVNGT RLLASLNNVS FVMPQTALLQ AHYFNIKGVY RTDFPDKPST 420 TFNYTGAPLT ANLGTSTGTR ISKVPFNSTV ELVLQDTNLL TVESHPFHLH GYNFFVVGTG 480 IGNFDPSKDP AKYNLVDPIE RNTVGVPTGG WTAIRFRADN PGVWFMHCHL ELHTGWGLKT 540 AFLVEDGPGQ EQSVVPPPKD LPTC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 3.0e-55 | 39 | 546 | 556 | + 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 | 2.0e-79 | 27 | 542 | 550 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 7.0e-95 | 28 | 542 | 549 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-103 | 32 | 538 | 541 | + 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] |
RefSeq | XP_002266464.1 | 0 | 29 | 564 | 28 | 563 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002275392.1 | 0 | 12 | 564 | 5 | 557 | 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 | 545 | 1 | 526 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 1asq_A | 0 | 30 | 545 | 1 | 526 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 1asp_B | 0 | 30 | 545 | 1 | 526 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 1asp_A | 0 | 30 | 545 | 1 | 526 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 1aso_B | 0 | 30 | 545 | 1 | 526 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |