Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.T079700.1 |
Family | AA1 |
Protein Properties | Length: 569 Molecular Weight: 64122.9 Isoelectric Point: 8.2033 |
Chromosome | Chromosome/Scaffold: 87 Start: 50641 End: 52823 |
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 | 300 | 544 | 4.2039e-45 |
VVSRNATTPPGLAIFNYYPNHPRRSPPTIPPSGPMWNDIAPRFNQSVAIKARRGHIYPPPATSDRVIVLLNTQNTVNGNVRWSVNKVSFNIPHTPYLIAL KENLLHTFSQTPPPEGYDFKNYDIFARQNNTNATTSDAIYRLQLNSTVDIILQNANTMNPNNSETHPWHLHGHDFWVLGYGKGKFDPINDPKNYNLVDPI MKNTVPVHPFGWTALRFKADNPGVWAFHCHIESHFFMGMGVVFEE | |||
AA1 | 75 | 347 | 0 |
ENTAIHWHGIRQIGTPWFDGTEGVTQCPILPGDTFVYKFVVDRPGTYLYHAHYGMQREAGIYGSIRVALPDGESEPFAYDYDRSIILTDWYHKSTYEQAA GLSSIPFQWVGEPQSLLIQGKGRFDCSAANPPLKADVCNNTNPECSLYSTTVVPGKTYRLRISSLSALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFI YSGETYSVLVKTDQDPSRNYWATTNVVSRNATTPPGLAIFNYYPNHPRRSPPTIPPSGPMWNDIAPRFNQSVA |
Full Sequence |
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Protein Sequence Length: 569 Download |
MKFFALCFFV ISLINIPIAD ARIRHYKWEL KYEYKSPDCY KKLVITINGR TPGPTILAKQ 60 NDTVIVEVKN SLLTENTAIH WHGIRQIGTP WFDGTEGVTQ CPILPGDTFV YKFVVDRPGT 120 YLYHAHYGMQ REAGIYGSIR VALPDGESEP FAYDYDRSII LTDWYHKSTY EQAAGLSSIP 180 FQWVGEPQSL LIQGKGRFDC SAANPPLKAD VCNNTNPECS LYSTTVVPGK TYRLRISSLS 240 ALSALSFQIE GHNMTVVEAD GHYVEPFVVK NLFIYSGETY SVLVKTDQDP SRNYWATTNV 300 VSRNATTPPG LAIFNYYPNH PRRSPPTIPP SGPMWNDIAP RFNQSVAIKA RRGHIYPPPA 360 TSDRVIVLLN TQNTVNGNVR WSVNKVSFNI PHTPYLIALK ENLLHTFSQT PPPEGYDFKN 420 YDIFARQNNT NATTSDAIYR LQLNSTVDII LQNANTMNPN NSETHPWHLH GHDFWVLGYG 480 KGKFDPINDP KNYNLVDPIM KNTVPVHPFG WTALRFKADN PGVWAFHCHI ESHFFMGMGV 540 VFEEGIERVG KLPSSIMGCG ETKRLLKP* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 1.0e-80 | 39 | 545 | 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 | 5.0e-108 | 21 | 557 | 563 | + 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 | 1 | 564 | 565 | + oxidoreductase | ||
TIGR03388 | ascorbase | 0 | 23 | 562 | 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 | 19 | 566 | 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 | 19 | 568 | 31 | 578 | ascorbate oxidase [Solanum lycopersicum] |
RefSeq | XP_002281435.1 | 0 | 1 | 565 | 1 | 563 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002306323.1 | 0 | 1 | 568 | 1 | 570 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002309992.1 | 0 | 1 | 568 | 2 | 542 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002528975.1 | 0 | 2 | 568 | 13 | 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 | 21 | 566 | 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 | 21 | 566 | 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 | 21 | 566 | 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 | 21 | 566 | 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 | 21 | 566 | 1 | 545 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |