Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10016460m |
Family | AA1 |
Protein Properties | Length: 558 Molecular Weight: 61496.7 Isoelectric Point: 9.5798 |
Chromosome | Chromosome/Scaffold: 10 Start: 9516117 End: 9519383 |
Description | Laccase/Diphenol oxidase family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 24 | 543 | 0 |
MVRHYKFNVVMKNTTRLCSSKPIVTVNGRYPGPTIYAREDDTLLIKVVNHVKYNISIHWHGVRQVRTGWADGPAYITQCPIQPGQVYTYNYTLTGQRGTL WWHAHILWLRATVYGAIVILPKRGVPYPFPKPDHEKVIVLGEWWKSDTENVINEAIKSGLAPNVSDAHMINGHPGPVKNCPSQGYKLSVENGKTYLLRLV NAALNEELFFKVAGHIFTVVEVDAVYVKPFKIDTVLIAPGQTTNVLLTASKSAGKYLVTASPFMDAPVAVDNVTATATVHYSGTLSSSPTTLTLPPPQNA TSVANNFTNSLRSLNSKKYPALVPTTIDHHLFFTVGLGLNSCPTCKAGNGSRVVASINNVTFIMPKTALLPAHYFNISGVFTTDFPKNPPHVFNYSGGSV TNMATETGTRLYKLPYNATVQLVLQDTGVIAPENHPIHLHGYNFFEVGRGLGNFDPKKDPNNFNLVDPVERNTVGVPSGGWVVIRFRADNPGVWFMHCHL EVHTTWGLKMAFLVENGKGP |
Full Sequence |
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Protein Sequence Length: 558 Download |
MKSQMVWLLF LVSFLSVFSS SESMVRHYKF NVVMKNTTRL CSSKPIVTVN GRYPGPTIYA 60 REDDTLLIKV VNHVKYNISI HWHGVRQVRT GWADGPAYIT QCPIQPGQVY TYNYTLTGQR 120 GTLWWHAHIL WLRATVYGAI VILPKRGVPY PFPKPDHEKV IVLGEWWKSD TENVINEAIK 180 SGLAPNVSDA HMINGHPGPV KNCPSQGYKL SVENGKTYLL RLVNAALNEE LFFKVAGHIF 240 TVVEVDAVYV KPFKIDTVLI APGQTTNVLL TASKSAGKYL VTASPFMDAP VAVDNVTATA 300 TVHYSGTLSS SPTTLTLPPP QNATSVANNF TNSLRSLNSK KYPALVPTTI DHHLFFTVGL 360 GLNSCPTCKA GNGSRVVASI NNVTFIMPKT ALLPAHYFNI SGVFTTDFPK NPPHVFNYSG 420 GSVTNMATET GTRLYKLPYN ATVQLVLQDT GVIAPENHPI HLHGYNFFEV GRGLGNFDPK 480 KDPNNFNLVD PVERNTVGVP SGGWVVIRFR ADNPGVWFMH CHLEVHTTWG LKMAFLVENG 540 KGPNQSILPP PKDFPKC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02991 | PLN02991 | 7.0e-46 | 22 | 523 | 503 | + oxidoreductase | ||
PLN02835 | PLN02835 | 2.0e-47 | 22 | 519 | 511 | + oxidoreductase | ||
pfam07732 | Cu-oxidase_3 | 5.0e-50 | 31 | 147 | 119 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
TIGR03388 | ascorbase | 3.0e-87 | 25 | 535 | 545 | + 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 | 25 | 557 | 537 | + 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 | NP_565881.1 | 0 | 1 | 557 | 1 | 558 | IRX12 (IRREGULAR XYLEM 12); laccase [Arabidopsis thaliana] |
RefSeq | XP_002322961.1 | 0 | 22 | 557 | 21 | 557 | laccase 1a [Populus trichocarpa] |
RefSeq | XP_002322962.1 | 0 | 7 | 557 | 5 | 557 | laccase 1b [Populus trichocarpa] |
RefSeq | XP_002520425.1 | 0 | 7 | 557 | 6 | 556 | laccase, putative [Ricinus communis] |
RefSeq | XP_002533894.1 | 0 | 1 | 557 | 1 | 556 | 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 | 23 | 535 | 1 | 521 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asq_A | 0 | 23 | 535 | 1 | 521 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asp_B | 0 | 23 | 535 | 1 | 521 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asp_A | 0 | 23 | 535 | 1 | 521 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1aso_B | 0 | 23 | 535 | 1 | 521 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |