y
Basic Information | |
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Species | Vitis vinifera |
Cazyme ID | GSVIVT01022181001 |
Family | AA1 |
Protein Properties | Length: 491 Molecular Weight: 55535.8 Isoelectric Point: 6.7935 |
Chromosome | Chromosome/Scaffold: 7 Start: 17247589 End: 17250725 |
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 | 76 | 348 | 0 |
NVAIHWHGIRQIGTPWFDGTEGVTQCPILPGETFTYEYKVDRPGTYLYHAHYGMQREAGLYGSIRVSVARGKTEPFSYDYDRSIILSDWYHNTTYEQVLG LSSIPFDWIGEPQSLLIQGKGRYNCSLVSSPYVCNATSPQCSPYVLTVVPGKTYRLRVSSLTSLSALSFQIEGHNMTVVEADGHFVEPFVIKNLFIYSGE TYSVLVKADQDPSRNYWVTSSVVSRNNTVTPPGLAIFNYYPNHPNKSPPTVPPAGPLWNDVEPRINQSRAIKA |
Full Sequence |
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Protein Sequence Length: 491 Download |
MRFLALFILL FSVLIFQAAE ARIRRYKWEV KYEYKSPDCF QKMVITINGQ SPGPTILAEE 60 GDTVIVELTN GLLTENVAIH WHGIRQIGTP WFDGTEGVTQ CPILPGETFT YEYKVDRPGT 120 YLYHAHYGMQ REAGLYGSIR VSVARGKTEP FSYDYDRSII LSDWYHNTTY EQVLGLSSIP 180 FDWIGEPQSL LIQGKGRYNC SLVSSPYVCN ATSPQCSPYV LTVVPGKTYR LRVSSLTSLS 240 ALSFQIEGHN MTVVEADGHF VEPFVIKNLF IYSGETYSVL VKADQDPSRN YWVTSSVVSR 300 NNTVTPPGLA IFNYYPNHPN KSPPTVPPAG PLWNDVEPRI NQSRAIKAHH DYVIPPPLTS 360 DRVILMLNTQ NEINGYRKWS PNNSNATETH PWHLHGHDFW VLGYGEGTFN MSSDPRTYNL 420 INPIMKNTAP IHPYGWTALR FRSDNPGVWA FHCHIESHFY MGMGVVFEEG VERVGKLPSS 480 IIDDTNSFRS * 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02191 | PLN02191 | 2.0e-32 | 387 | 461 | 75 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 1.0e-52 | 383 | 482 | 100 | + oxidoreductase | ||
PLN02191 | PLN02191 | 7.0e-135 | 1 | 426 | 435 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 0 | 1 | 383 | 387 | + oxidoreductase | ||
TIGR03388 | ascorbase | 0 | 23 | 482 | 538 | + 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. |
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 | CBI21460.1 | 0 | 1 | 390 | 1 | 390 | unnamed protein product [Vitis vinifera] |
EMBL | CBI21460.1 | 0 | 387 | 482 | 460 | 555 | unnamed protein product [Vitis vinifera] |
EMBL | CBI21465.1 | 0 | 1 | 490 | 1 | 490 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002281314.1 | 0 | 1 | 383 | 1 | 383 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002281314.1 | 0 | 385 | 482 | 458 | 555 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 383 | 1 | 366 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |
PDB | 1asq_B | 3e-38 | 385 | 490 | 440 | 544 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |
PDB | 1asq_A | 0 | 21 | 383 | 1 | 366 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |
PDB | 1asq_A | 3e-38 | 385 | 490 | 440 | 544 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |
PDB | 1asp_B | 0 | 21 | 383 | 1 | 366 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |