A2QS62 · A2QS62_ASPNC
- ProteinContig An08c0220, genomic contig
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids594 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 125 | Cu2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 127 | Cu2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 169 | Cu2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 171 | Cu2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 187 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 197 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 253 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 270 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 345 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 347 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 351 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 383 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 385 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 431 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 433 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 465 | Cu2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 468 | Cu2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 470 | Cu2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 494 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 532 | Cu2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 533 | Cu2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 534 | Cu2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 538 | Cu2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 538 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 572 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: E |
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 | |
---|---|---|
Molecular Function | copper ion binding | |
Molecular Function | hydroquinone:oxygen oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA2QS62
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MTIFLLLLGLLAPLVLC | ||||||
Chain | PRO_5042449746 | 18-594 | ||||
Sequence: SPIRHVTPHLSHSTPIPRDMQGNSSQSPNTPWQGYDINTNYYETIPQTNVVREYWFDIVNTTAALDGVERPVLLVNGQFPGPTIEANWGDTVKVHVTNRMENNGTAIHFHGIRQLYNNQMDGVAALTQCPVPPNSSYTYVWRAEEYGSSWYHSHFSLQAWEGVFGGILIHGPSTAEYDHDLGMVFLNDWSHQTVDEMYQSVLESQNPPHFQTGLINGSNIWVTADNQTVGRRFQTEFVPGQRYRLRLVNAAMHTHFRFSIDNHDLTVIASDFVPIVPFTTNNVPIGMGQRYDIIVTANQAPDNYWIRAIPQSFCSDNANSDNIKGVLHYEGAADNSDPTSTKWDYGDDIQCLDFSLDELVPWLALDADIGGAQMAESDVDFTPFGDVPLYLWTMGGNALNISWKDPTLQQTFEDPDKMDWKASQGVIEAAIPNKWTVLVVQTDLPVPHPIHLHGHDFYLLAQGFGQFNPQNVTLKTHNPPRRDTALMTAATPENGGGGYMVIGFPADNPGVWLIHCHIGFHATEGFAQQIVERQSEFNTFFSEDLLENTCDAWDEYAKVNPYGHQYRALAGPYESGI | ||||||
Glycosylation | 77 | N-acetyl-D-glucosamine 1 | ||||
Sequence: N | ||||||
Glycosylation | 100 | N-acetyl-D-glucosamine 2 | ||||
Sequence: T | ||||||
Glycosylation | 118 | N-acetyl-D-glucosamine 1 | ||||
Sequence: E | ||||||
Glycosylation | 119 | N-acetyl-D-glucosamine 1 | ||||
Sequence: N | ||||||
Disulfide bond | 146↔567 | |||||
Sequence: CPVPPNSSYTYVWRAEEYGSSWYHSHFSLQAWEGVFGGILIHGPSTAEYDHDLGMVFLNDWSHQTVDEMYQSVLESQNPPHFQTGLINGSNIWVTADNQTVGRRFQTEFVPGQRYRLRLVNAAMHTHFRFSIDNHDLTVIASDFVPIVPFTTNNVPIGMGQRYDIIVTANQAPDNYWIRAIPQSFCSDNANSDNIKGVLHYEGAADNSDPTSTKWDYGDDIQCLDFSLDELVPWLALDADIGGAQMAESDVDFTPFGDVPLYLWTMGGNALNISWKDPTLQQTFEDPDKMDWKASQGVIEAAIPNKWTVLVVQTDLPVPHPIHLHGHDFYLLAQGFGQFNPQNVTLKTHNPPRRDTALMTAATPENGGGGYMVIGFPADNPGVWLIHCHIGFHATEGFAQQIVERQSEFNTFFSEDLLENTC | ||||||
Glycosylation | 200 | N-acetyl-D-glucosamine 2 | ||||
Sequence: M | ||||||
Glycosylation | 233 | N-acetyl-D-glucosamine 2 | ||||
Sequence: N | ||||||
Glycosylation | 233 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 331↔368 | |||||
Sequence: CSDNANSDNIKGVLHYEGAADNSDPTSTKWDYGDDIQC | ||||||
Glycosylation | 417 | N-acetyl-D-glucosamine 4 | ||||
Sequence: N | ||||||
Glycosylation | 417 | N-acetyl-D-glucosamine 5 | ||||
Sequence: N | ||||||
Glycosylation | 584 | N-acetyl-D-glucosamine 5 | ||||
Sequence: R |
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 28-47 | Disordered | ||||
Sequence: SHSTPIPRDMQGNSSQSPNT | ||||||
Compositional bias | 31-47 | Polar residues | ||||
Sequence: TPIPRDMQGNSSQSPNT | ||||||
Domain | 78-189 | Plastocyanin-like | ||||
Sequence: TTAALDGVERPVLLVNGQFPGPTIEANWGDTVKVHVTNRMENNGTAIHFHGIRQLYNNQMDGVAALTQCPVPPNSSYTYVWRAEEYGSSWYHSHFSLQAWEGVFGGILIHGP | ||||||
Domain | 200-349 | Plastocyanin-like | ||||
Sequence: MVFLNDWSHQTVDEMYQSVLESQNPPHFQTGLINGSNIWVTADNQTVGRRFQTEFVPGQRYRLRLVNAAMHTHFRFSIDNHDLTVIASDFVPIVPFTTNNVPIGMGQRYDIIVTANQAPDNYWIRAIPQSFCSDNANSDNIKGVLHYEGA | ||||||
Domain | 419-551 | Plastocyanin-like | ||||
Sequence: SWKDPTLQQTFEDPDKMDWKASQGVIEAAIPNKWTVLVVQTDLPVPHPIHLHGHDFYLLAQGFGQFNPQNVTLKTHNPPRRDTALMTAATPENGGGGYMVIGFPADNPGVWLIHCHIGFHATEGFAQQIVERQ |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length594
- Mass (Da)66,587
- Last updated2007-03-06 v1
- Checksum3394B395BF5EA250
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 31-47 | Polar residues | ||||
Sequence: TPIPRDMQGNSSQSPNT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM270177 EMBL· GenBank· DDBJ | CAK40046.1 EMBL· GenBank· DDBJ | Genomic DNA |