Detail Information for IndEnz0015000118
IED ID IndEnz0015000118
Enzyme Type ID laccase000118
Protein Name Transcriptional regulator CRZ1
Gene Name CRZ1 SP1 CNAG_00156
Organism Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Tremellomycetes Tremellales (jelly fungi) Cryptococcaceae Cryptococcus Cryptococcus neoformans species complex Cryptococcus neoformans (Filobasidiella neoformans) Cryptococcus neoformans var. grubii (Filobasidiella neoformans var. grubii) Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Enzyme Sequence MADPASPPSFDAIFAQQPVRRSSSTSTSSFANYTYSALQQHQQFNSDAPLVDEPQSLSEQARKQQRDPSKDGNNKRYLDMMSGLADGYGVINGRRQESLRKESLPFNPQEDSTLIATAPKRGERNGLGRNGYSSPIGDIMFGPEQTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPGAGSAGIDYLPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNGMEDMLTMGDESPFESELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQTRTESFPASRSPSPFAPQQASQTEASNHVVSTPSMGQPTYPRASSSPRTNPNSPFFNKPQSPPALIIPNSPVLPNIVTQSTSNNHSKGLNQPHTRHASNGAGGLFPPSNPALEHLTGMAGISPIAPNADGPMICIQPSTPISGLKEGRGLFDAALRRAGAARGAQRQGPQGQGESQEDRRQDGFNVPSPQSHPLPRTLSSDQVNQGVEMQGMDFAAQMQSYEQQGWANDTLRIAGPSRPRAKSDSIIPSPTADSFDRQAFLAFIGAGNAQPPPPNVEMQPGYVDVSEQWRNTVSAWKAGLGEGELNSQPTLDPRLLPGRESNEAVYQQLLMQQQTGQMPRLDPDQLHQLTQLEGQRARFSLNTNIAPPKYEPGEISPTSMVFYQSMGLYPHAAPELSGTVSAPWSQTAFGQVPGPGPVGHPATAGPAQQHFLTPTLSHATVRRRSFGGGEHPAMGAGTPGYGMEFSSPFAGKSVGQIRGVNMGHRRAARSEDFGRGGTGWGVGAGGSTAEFLQSITGDDGSLLPPSNRGHAMSHSRHSSTSSIRSASPALSISSQGSSFSHHSPRMDMPDSIYPGHPIIAPATPLQVSGLYEEQQTPARVAKMKVTSVATEVASTSRRTNSGIFKCPVPGCGSTFTRHFNLKGHLRSHNDERPFKCLYEGCPKAIVGFARQHDCKRHMLLHEGLRLFECEGCGKKFARLDALTRHHKSEQGQECAITHPLPTNFDGSPMSESQYKTYKGIKSTPEGSGRRLSSTASGSGSGKRRSKKSETSEED
Enzyme Length 1094
Uniprot Accession Number J9VE33
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: DNA-binding transcriptional activator that interacts with calcineurin-dependent response element (CDRE) promoters (PubMed:28376087). Activates expression of genes required to maintain cell wall integrity during stress (PubMed:23251520, PubMed:28376087). Activates expression of genes required for transepithelial migration through the host blood-brain barrier (PubMed:29113016). Required for adaptation to host temperature during infection (PubMed:28376087). {ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:28376087, ECO:0000303|PubMed:28376087, ECO:0000303|PubMed:29113016}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (9); Modified residue (7); Mutagenesis (3); Region (6); Zinc finger (2)
Keywords Activator;Cytoplasm;DNA-binding;Metal-binding;Nucleus;Phosphoprotein;Repeat;Transcription;Transcription regulation;Virulence;Zinc;Zinc-finger
Interact With
Induction INDUCTION: Induced during glucose starvation. {ECO:0000269|PubMed:21487010}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}. Nucleus {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:24520056, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}. Note=Localizes to the nucleus during calcium signaling, cell wall and heat stress (PubMed:21487010, PubMed:23251520, PubMed:24520056, PubMed:27611567, PubMed:28376087, PubMed:28898238, PubMed:31266771). Localizes to the nucleus following dephosphorylation by CNA1 (calcineurin) (PubMed:27611567). Localizes to the nucleus during growth on glucosamine carbon source (PubMed:28898238). Localizes to the cytosol during vegetative growth and osmotic stress (PubMed:23251520, PubMed:28376087, PubMed:28898238). {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:24520056, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}.
Modified Residue MOD_RES 103; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:27611567; MOD_RES 288; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:27611567; MOD_RES 329; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:27611567; MOD_RES 508; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:27611567; MOD_RES 569; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:27611567; MOD_RES 765; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:27611567; MOD_RES 810; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:27611567
Post Translational Modification PTM: Phosphorylated (PubMed:21487010, PubMed:27611567). Dephosphorylated by calcineurin (CNA1) which promotes nuclear localization (PubMed:27611567). {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:27611567}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 117,964
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda