Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.T079500.1 |
Family | AA1 |
Protein Properties | Length: 583 Molecular Weight: 65597.4 Isoelectric Point: 7.6842 |
Chromosome | Chromosome/Scaffold: 87 Start: 39187 End: 41651 |
Description | Cupredoxin superfamily protein |
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 | 35 | 558 | 0 |
ARIRHYKFELKYEYKSPDCYKKLVITINGRTPGPTIFAQQNDTVIVEVKNSLLTENTAIHWHGIRQIGTPWFDGTEGVTQCPILPGDTFVYKFVVDRPGT YLYHAHYGMQREAGIYGSIRVALPDGESEPFAYDYDRSIILTDWYHKSTYEQATGLSSIPFQWVGEPQSLLIQGKGRFDCSAANPPLKADVCNNTSPECS LYSTTVVPGKTYRLRISSLTALSALSFQIEGHSLTVVEADGHYVEPFVVKNLFIYSGETYSVLVKTDQDPSRNYWATTNVVSRNATTPPGLAIFNYYPNH PRRSPPTIPPSGPMWNDIEPRFNQSVAIKARKGHIYSPPATSDRVIVFLNTQNRVNGNVRWSVNNVSFNIPHTPYLIALKENLLHTFSQTPPPEGYDFKN YDIFARQNNTNATTSDAIYRLQLNSTVDIILQNANTMNPNNSETHPWHLHGHDFWVLGYGKGKFDPINDPKNYNLVDPIMKNTVPVHPLGWTALRFKADN PGAWAFHCHIESHFFMGMGVVFEE |
Full Sequence |
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Protein Sequence Length: 583 Download |
MSGYQLSESK SIAMMKFLAL CFFVISLINI PIAEARIRHY KFELKYEYKS PDCYKKLVIT 60 INGRTPGPTI FAQQNDTVIV EVKNSLLTEN TAIHWHGIRQ IGTPWFDGTE GVTQCPILPG 120 DTFVYKFVVD RPGTYLYHAH YGMQREAGIY GSIRVALPDG ESEPFAYDYD RSIILTDWYH 180 KSTYEQATGL SSIPFQWVGE PQSLLIQGKG RFDCSAANPP LKADVCNNTS PECSLYSTTV 240 VPGKTYRLRI SSLTALSALS FQIEGHSLTV VEADGHYVEP FVVKNLFIYS GETYSVLVKT 300 DQDPSRNYWA TTNVVSRNAT TPPGLAIFNY YPNHPRRSPP TIPPSGPMWN DIEPRFNQSV 360 AIKARKGHIY SPPATSDRVI VFLNTQNRVN GNVRWSVNNV SFNIPHTPYL IALKENLLHT 420 FSQTPPPEGY DFKNYDIFAR QNNTNATTSD AIYRLQLNST VDIILQNANT MNPNNSETHP 480 WHLHGHDFWV LGYGKGKFDP INDPKNYNLV DPIMKNTVPV HPLGWTALRF KADNPGAWAF 540 HCHIESHFFM GMGVVFEEGI ERVGKLPSSI MGCGETKHLL KP* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
TIGR03390 | ascorbOXfungal | 1.0e-83 | 53 | 559 | 540 | + 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. |
TIGR03389 | laccase | 3.0e-110 | 35 | 571 | 561 | + 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. |
PLN02604 | PLN02604 | 0 | 14 | 578 | 566 | + oxidoreductase |
TIGR03388 | ascorbase | 0 | 37 | 576 | 543 | + 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. |
PLN02191 | PLN02191 | 0 | 33 | 580 | 552 | + L-ascorbate oxidase |
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 | AAY47050.1 | 0 | 33 | 582 | 31 | 578 | ascorbate oxidase [Solanum lycopersicum] |
RefSeq | XP_002281435.1 | 0 | 15 | 579 | 1 | 563 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002306323.1 | 0 | 15 | 582 | 1 | 570 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002309992.1 | 0 | 14 | 582 | 1 | 542 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002528975.1 | 0 | 5 | 582 | 3 | 576 | l-ascorbate oxidase, 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 | 35 | 580 | 1 | 545 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asq_A | 0 | 35 | 580 | 1 | 545 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asp_B | 0 | 35 | 580 | 1 | 545 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asp_A | 0 | 35 | 580 | 1 | 545 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1aso_B | 0 | 35 | 580 | 1 | 545 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |