y
Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000192322 |
Family | AA1 |
Protein Properties | Length: 517 Molecular Weight: 57389.7 Isoelectric Point: 6.861 |
Chromosome | Chromosome/Scaffold: 010516417 Start: 6822 End: 9328 |
Description | laccase 7 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 23 | 258 | 0 |
AIVEHSFNVNNMTVXRLCRNQSITVVNGSYPGPTIYARDXDTLIVHVLNQSPYNITIHWHGIFQLLSAWADGPAYVTQCPIRPGQSFTYKFNITGQEGTL WWHAHVSWLRATVHGALIIHPKVGRSFPFLKPAKEVPILLGEWYNGNVVDIEEEGLATGIAPNGSNAYTINGLXGDLYDCSQNQTYQLXVVRGKTYLLRL INVALNNQLFFKIANHNMTVVAIDATYTTPYVTDVV | |||
AA1 | 262 | 504 | 0 |
SXTPIMPSMPNPRNTPLAHXFLTNLTXLAGGPQWVPVPLKVDERMFVTISVNLEXCPENATCQGPLFNRLSASMNNESFVLPSNTSMMEAQFNNMSGVYT RDFPDEPPIKFDYTDTNVSFDLSLIYAPKSTKVKTLKFNSTVEVVLQNTAFLAIENHPMHLHGFNFHVLAQGFGNYDPINDPKKFNFINPQIRNTIGVPV GGWAVIRFQANNPGIWYMHCHLDVHVPWGLGMAFEVENGPTPE |
Full Sequence |
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Protein Sequence Length: 517 Download |
MARLAFVLVC AVALLASSVA SGAIVEHSFN VNNMTVXRLC RNQSITVVNG SYPGPTIYAR 60 DXDTLIVHVL NQSPYNITIH WHGIFQLLSA WADGPAYVTQ CPIRPGQSFT YKFNITGQEG 120 TLWWHAHVSW LRATVHGALI IHPKVGRSFP FLKPAKEVPI LLGEWYNGNV VDIEEEGLAT 180 GIAPNGSNAY TINGLXGDLY DCSQNQTYQL XVVRGKTYLL RLINVALNNQ LFFKIANHNM 240 TVVAIDATYT TPYVTDVVGS RSXTPIMPSM PNPRNTPLAH XFLTNLTXLA GGPQWVPVPL 300 KVDERMFVTI SVNLEXCPEN ATCQGPLFNR LSASMNNESF VLPSNTSMME AQFNNMSGVY 360 TRDFPDEPPI KFDYTDTNVS FDLSLIYAPK STKVKTLKFN STVEVVLQNT AFLAIENHPM 420 HLHGFNFHVL AQGFGNYDPI NDPKKFNFIN PQIRNTIGVP VGGWAVIRFQ ANNPGIWYMH 480 CHLDVHVPWG LGMAFEVENG PTPESTLPPP PLDLPKC 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 4.0e-48 | 30 | 144 | 117 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 2.0e-54 | 40 | 495 | 521 | + L-ascorbate oxidase | ||
TIGR03388 | ascorbase | 1.0e-71 | 24 | 496 | 542 | + 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. | ||
PLN02604 | PLN02604 | 6.0e-72 | 40 | 496 | 520 | + oxidoreductase | ||
TIGR03389 | laccase | 0 | 27 | 500 | 522 | + 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 | CBI30455.1 | 0 | 1 | 517 | 1 | 542 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002276415.1 | 0 | 1 | 517 | 1 | 565 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002308196.1 | 0 | 1 | 517 | 1 | 562 | laccase 110a [Populus trichocarpa] |
RefSeq | XP_002333273.1 | 0 | 1 | 517 | 1 | 568 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527888.1 | 0 | 29 | 517 | 2 | 540 | 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 | 24 | 495 | 3 | 521 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
PDB | 1asq_A | 0 | 24 | 495 | 3 | 521 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
PDB | 1asp_B | 0 | 24 | 495 | 3 | 521 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
PDB | 1asp_A | 0 | 24 | 495 | 3 | 521 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
PDB | 1aso_B | 0 | 24 | 495 | 3 | 521 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |