P14217 · ARS_CHLRE
- ProteinArylsulfatase
- GeneAS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids647 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- an aryl sulfate + H2O = a phenol + sulfate + H+
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 35 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 36 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 73 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 73 | Ca2+ (UniProtKB | ChEBI); via 3-oxoalanine | ||||
Sequence: C | ||||||
Binding site | 323 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 324 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | arylsulfatase activity | |
Molecular Function | metal ion binding | |
Biological Process | phenol-containing compound metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArylsulfatase
- EC number
- Short namesAS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Chlorophyta > core chlorophytes > Chlorophyceae > CS clade > Chlamydomonadales > Chlamydomonadaceae > Chlamydomonas
Accessions
- Primary accessionP14217
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MGALAVFAVACLAAVASVAHA | ||||||
Chain | PRO_0000033444 | 22-647 | Arylsulfatase | |||
Sequence: ADTKKPNFVVIFTDDQDAIQNSTHPHYMPSLHKYIRYPGVELSQYFVTTPVCCPSRTNLXRGQFAHNTNFTSVLPPYGGWAKWKGLGIDQSYLPLWLKDQGYNTYYVGKFLVDYSVSNYQQVPRAGTISMPXVTPYTFDYNTRLQRNGATPNIYPGEYSTDVIRDKGVAQIKSAVAAGKPFYAQISPIAPHTSTQISTNPATGVTRSYFFPPIPAPPHWQLFSDANLPGGSXNKNLYEVDVSDKPAWIRALPLAQQNNRTYQEEIYRLRLRSLGPDELIEQVVKTLDEAGVLDNTYIIYSADNGYHVGAHRFGAGKTTGYEEDLRVPFLIRGPGIKASKSDKPQNSKVGLHVDFAPTILSLAGASHLLGDKGLDGTPLGLYANDDGTLPSDYPRPEQHRQQFQGEFWGGWSDELLQNLRSQPNNTWKVVRTYDESSKQGWKLIAQCTNERELYDLRKDPGELYNIYDKAKPAVRSRLEGLLAVLAVCKGESCSNPWKILHPDGTVKNFTQALNSKYDRIYNAIRPFTYKRCLPYLDWDNEDSQFKTQIRGANPAAGVGHHRLLTAASERAIATRRRAQAAVSAELADGPAVFQAKVEEKSVPVPQDILKADVEKWFAFNNAEYYLA | ||||||
Glycosylation | 42 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 73 | 3-oxoalanine (Cys) | ||||
Sequence: C | ||||||
Glycosylation | 90 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 279 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 444 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 528 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By sulfur deprivation.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length647
- Mass (Da)72,106
- Last updated1996-10-01 v2
- Checksum7404EA1BF233F0B1
Sequence caution
Keywords
- Technical term