A0A0B4F5S2 · MLAC1_METBS
- ProteinLaccase 1
- GeneMlac1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids613 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Laccase; part of the Pks1 gene cluster that mediates the biosynthesis of an anthraquinone derivative pigment that contributes to conidial pigmentation that provides protection from UV radiation, heat and cold stress (PubMed:29958281).
The polyketide synthase Pks1 produces 1-acetyl-2,4,6,8-tetrahydroxy-9,10-anthraquinone though condensation of acetyl-CoA with malonyl-CoA (Probable). The dehydratase EthD and the laccase Mlac1 further convert the anthraquinone derivative into the final conidial pigment (Probable)
The polyketide synthase Pks1 produces 1-acetyl-2,4,6,8-tetrahydroxy-9,10-anthraquinone though condensation of acetyl-CoA with malonyl-CoA (Probable). The dehydratase EthD and the laccase Mlac1 further convert the anthraquinone derivative into the final conidial pigment (Probable)
Cofactor
Note: Binds 4 Cu cations per monomer.
Pathway
Pigment biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 78 | Cu cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 80 | Cu cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 122 | Cu cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 124 | Cu cation 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 506 | Cu cation 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 509 | Cu cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 509 | Cu cation 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 511 | Cu cation 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 580 | Cu cation 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 581 | Cu cation 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 582 | Cu cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 586 | Cu cation 4 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Molecular Function | copper ion binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLaccase 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Metarhizium
Accessions
- Primary accessionA0A0B4F5S2
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MSRFARLLLIVALFFTNAWA | ||||||
Chain | PRO_5002086819 | 21-613 | Laccase 1 | |||
Sequence: KTVKETLRITWKEGAPNGQARELIYTNGQFPSPTLVWDEDDDIEVTVYNEMAKNVTVHWHGLDQKDTPWSDGTPGLSQRPIQPGNKFVYRFKASPPGNHWYHSHEKMSLVDGLYGAIHIRPKGDRTGLWSQISQDKDDIKAMENAAYDPEYLVVSDWSQYTSEEYWKISTDSGLLVFCLDSILVNGKGEVYCPGQKFLQAELAPGLVEDAFPPGTEVSDKGCFPADLDQVQGGPWNITKRPDLIPPRVQEGCVASRHENATIVVDPSKNNGWVSMHFVAAATIAQITFSVDSHEFWLYEIDGNYVNPRKFVSAVMSAGETFSVMIKLDQEPGKYTMRIPNSGASQVLGGFAEMVYKGCEREEKAGKAYLSYGGNPTSPDVEKNSFFPWQLDTDHMSPWPPNKPRPGNADEEHLLVLGRVGAPYNYTMNTKYLYPVDFQNDDPLLFYPNATRDTENDGLVLRTKNGSWVDLILQVSTLPGDTSSFEHFMHKHGSKTWRIGFGTGVWNYTSVEEAIQERPQDFNLETPGLRDTWITAFSIGGEAYWSVFRYFVDNPGPWLFHCHIELHLMGGMGIAILDGVDAWPEHIPEEYQVC | ||||||
Glycosylation | 74 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 279 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 444 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 468 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 484 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 526 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-142 | Plastocyanin-like 1 | ||||
Sequence: ITWKEGAPNGQARELIYTNGQFPSPTLVWDEDDDIEVTVYNEMAKNVTVHWHGLDQKDTPWSDGTPGLSQRPIQPGNKFVYRFKASPPGNHWYHSHEKMSLVDGLYGAIHIRPK | ||||||
Domain | 171-359 | Plastocyanin-like 2 | ||||
Sequence: YLVVSDWSQYTSEEYWKISTDSGLLVFCLDSILVNGKGEVYCPGQKFLQAELAPGLVEDAFPPGTEVSDKGCFPADLDQVQGGPWNITKRPDLIPPRVQEGCVASRHENATIVVDPSKNNGWVSMHFVAAATIAQITFSVDSHEFWLYEIDGNYVNPRKFVSAVMSAGETFSVMIKLDQEPGKYTMRIP | ||||||
Domain | 468-598 | Plastocyanin-like 3 | ||||
Sequence: NATRDTENDGLVLRTKNGSWVDLILQVSTLPGDTSSFEHFMHKHGSKTWRIGFGTGVWNYTSVEEAIQERPQDFNLETPGLRDTWITAFSIGGEAYWSVFRYFVDNPGPWLFHCHIELHLMGGMGIAILDG |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length613
- Mass (Da)69,094
- Last updated2015-03-04 v1
- Checksum5EF56B8ECA1422C1
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AZNG01000033 EMBL· GenBank· DDBJ | KID61216.1 EMBL· GenBank· DDBJ | Genomic DNA |