Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.009G260800.1 |
Family | AA1 |
Protein Properties | Length: 564 Molecular Weight: 63110.6 Isoelectric Point: 6.6352 |
Chromosome | Chromosome/Scaffold: 09 Start: 21501577 End: 21504203 |
Description | laccase 14 |
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 | 21 | 543 | 0 |
ADVHHYEFFVRESNFKKMCNTSTLLVVNNSYPGPEIRVHRGDTVFVNVHNRGKYGFTIHWHGVKQPRNPWFDGPEFITQCPIRPRTNFTYKIILSEEIGT LWWHAHSDWTRGSVHGAIVILPAENETYPFPTPDGEQTIILESWYNGNFKKIIDKALAAGTPPPQPDAYAINGHLGDTYGCPTDTIFRMEVDYEKTYLLR IINAAMNEQQFFTIMNHTLTVVAVDASYVRRFKSDYILISPGQTMDVLVSANQNAGQYYMATRPFSDSDVPPVDFITTGIFQYTNFVGGSNASLITLPAM NNTDAMLNFISRIRNTNVTQNPPINVPADTDINRRVFITLAVNDLPCKNSKCVVSDGFAASLNNVSFVYPHIDVLQAYYRNIRGVFAENFPFLPPEFYDF TGNLTGVVSAVEVGTRAICVNYGDAVEIVLQSTQMGAGGSHPIHLHGYSFYWVGAGFGNFNGETDPSTYNLVDPPLMNTIDVPGTGWVAIRFFANNPGVW YMHCHFERHTSWGMSTVLIVRNG |
Full Sequence |
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Protein Sequence Length: 564 Download |
MGLVTWSVGV LFLSTLLLCS ADVHHYEFFV RESNFKKMCN TSTLLVVNNS YPGPEIRVHR 60 GDTVFVNVHN RGKYGFTIHW HGVKQPRNPW FDGPEFITQC PIRPRTNFTY KIILSEEIGT 120 LWWHAHSDWT RGSVHGAIVI LPAENETYPF PTPDGEQTII LESWYNGNFK KIIDKALAAG 180 TPPPQPDAYA INGHLGDTYG CPTDTIFRME VDYEKTYLLR IINAAMNEQQ FFTIMNHTLT 240 VVAVDASYVR RFKSDYILIS PGQTMDVLVS ANQNAGQYYM ATRPFSDSDV PPVDFITTGI 300 FQYTNFVGGS NASLITLPAM NNTDAMLNFI SRIRNTNVTQ NPPINVPADT DINRRVFITL 360 AVNDLPCKNS KCVVSDGFAA SLNNVSFVYP HIDVLQAYYR NIRGVFAENF PFLPPEFYDF 420 TGNLTGVVSA VEVGTRAICV NYGDAVEIVL QSTQMGAGGS HPIHLHGYSF YWVGAGFGNF 480 NGETDPSTYN LVDPPLMNTI DVPGTGWVAI RFFANNPGVW YMHCHFERHT SWGMSTVLIV 540 RNGSTIETSI RPRPSTMPRC HRT* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
PLN02168 | PLN02168 | 6.0e-46 | 8 | 520 | 527 | + copper ion binding / pectinesterase |
PLN02191 | PLN02191 | 1.0e-56 | 1 | 539 | 587 | + L-ascorbate oxidase |
PLN02604 | PLN02604 | 5.0e-71 | 18 | 537 | 558 | + oxidoreductase |
TIGR03388 | ascorbase | 2.0e-73 | 23 | 537 | 556 | + 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 | 21 | 560 | 542 | + 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 |
GenBank | AAR83118.1 | 0 | 2 | 560 | 6 | 563 | secretory laccase [Gossypium arboreum] |
GenBank | ACI46953.1 | 0 | 3 | 560 | 8 | 566 | putative lacasse/diphenol oxidase [Castanea mollissima] |
GenBank | ADB97327.1 | 0 | 1 | 563 | 1 | 567 | laccase [Litchi chinensis] |
RefSeq | XP_002325572.1 | 0 | 16 | 560 | 8 | 551 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002325575.1 | 0 | 16 | 560 | 8 | 551 | multicopper oxidase [Populus trichocarpa] |
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 | 538 | 1 | 521 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
PDB | 1asq_A | 0 | 21 | 538 | 1 | 521 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
PDB | 1asp_B | 0 | 21 | 538 | 1 | 521 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
PDB | 1asp_A | 0 | 21 | 538 | 1 | 521 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |
PDB | 1aso_B | 0 | 21 | 538 | 1 | 521 | A Chain A, Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 In Complex With Gluco-Phenylimidazole |