y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30004.m000428 |
Family | AA1 |
Protein Properties | Length: 578 Molecular Weight: 64575.4 Isoelectric Point: 9.8752 |
Chromosome | Chromosome/Scaffold: 30004 Start: 416095 End: 418478 |
Description | laccase 17 |
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 | 32 | 565 | 0 |
ITRHYKFDIMEQNVTRLCHTKTMVTVNGQFPGPRIVAKEGDRLLIQVTNHVKHNISIHWHGIRQLRSGWADGPAYITQCPIQTGQSYVYNYTIVGQRGTL WWHAHISWLRTTVYGPIIIHSKSSIHHPFVKPNKEVPIIFGEWFNADPDAVIKEALKTGGGPNVSDAYTINGFPGPLSNCSTKDTYRLHVKPGKTYMLRL INAALNDELFFSIANHTLTVVEVDAVYVKPFHTKILVIAPGQTTNVLLQTKPHYPEATFFMTARPYATGQGTFDNSSVAAILQYKATSKSNRSNKKIPLF KPSLPALNDSSFVMKYTNKLRSLASEEFPANVPQRIDRRFFFTIGLGTKPCPRNETCQGPNGAKFAASANNVSFTMPTKALLQSHFLGQAKGVYTLDFPR TVLFRFNYTGNPPNNTMVSTGTKVVKLHFNTSIELIMQDTSILGVESHPLHLHGFNFFVVGQGFGNFDPKKDPSKFNLVDPVERNTVGVPSGGWVAIRFL ADNPGVWFMHCHLEVHTSWGLKMAWVVNDGKHPN |
Full Sequence |
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Protein Sequence Length: 578 Download |
MGVSLLPSAP FMGHFLLVFI TLCLYYELTV AITRHYKFDI MEQNVTRLCH TKTMVTVNGQ 60 FPGPRIVAKE GDRLLIQVTN HVKHNISIHW HGIRQLRSGW ADGPAYITQC PIQTGQSYVY 120 NYTIVGQRGT LWWHAHISWL RTTVYGPIII HSKSSIHHPF VKPNKEVPII FGEWFNADPD 180 AVIKEALKTG GGPNVSDAYT INGFPGPLSN CSTKDTYRLH VKPGKTYMLR LINAALNDEL 240 FFSIANHTLT VVEVDAVYVK PFHTKILVIA PGQTTNVLLQ TKPHYPEATF FMTARPYATG 300 QGTFDNSSVA AILQYKATSK SNRSNKKIPL FKPSLPALND SSFVMKYTNK LRSLASEEFP 360 ANVPQRIDRR FFFTIGLGTK PCPRNETCQG PNGAKFAASA NNVSFTMPTK ALLQSHFLGQ 420 AKGVYTLDFP RTVLFRFNYT GNPPNNTMVS TGTKVVKLHF NTSIELIMQD TSILGVESHP 480 LHLHGFNFFV VGQGFGNFDP KKDPSKFNLV DPVERNTVGV PSGGWVAIRF LADNPGVWFM 540 HCHLEVHTSW GLKMAWVVND GKHPNQKLLP PPADLPNC 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 1.0e-48 | 42 | 147 | 108 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 4.0e-58 | 12 | 568 | 585 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 1.0e-74 | 16 | 552 | 568 | + oxidoreductase | ||
TIGR03388 | ascorbase | 9.0e-84 | 33 | 552 | 554 | + 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 | 31 | 578 | 549 | + 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 |
RefSeq | XP_002299296.1 | 0 | 1 | 578 | 1 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002300066.1 | 0 | 1 | 578 | 1 | 580 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002329138.1 | 0 | 1 | 578 | 1 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520231.1 | 0 | 1 | 578 | 1 | 580 | laccase, putative [Ricinus communis] |
RefSeq | XP_002520232.1 | 0 | 1 | 578 | 1 | 578 | 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 | 34 | 552 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asq_A | 0 | 34 | 552 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asp_B | 0 | 34 | 552 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asp_A | 0 | 34 | 552 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1aso_B | 0 | 34 | 552 | 4 | 517 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |