Q5AHG6 · SCH9_CANAL

Function

function

Protein kinase that is part of growth control pathway which is at least partially redundant with the cAMP pathway (By similarity).
Plays a role in filamentous growth and virulence. Prevents hypha formation specifically under hypoxia at high CO2 levels. Required for chlamydospore formation, distinctive morphological feature of the fungal pathogen C.albicans that can be induced to form in oxygen-limited environments and has been reported in clinical specimens.

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site398-406ATP (UniProtKB | ChEBI)
Binding site421ATP (UniProtKB | ChEBI)
Active site518Proton acceptor

GO annotations

AspectTerm
Cellular Componentchromatin
Cellular Componentfungal-type vacuole membrane
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processcellular response to starvation
Biological Processchlamydospore formation
Biological Processdevelopment of symbiont in host
Biological Processfilamentous growth
Biological Processfilamentous growth of a population of unicellular organisms
Biological Processfilamentous growth of a population of unicellular organisms in response to chemical stimulus
Biological Processfilamentous growth of a population of unicellular organisms in response to starvation
Biological Processintracellular signal transduction
Biological Processnegative regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus
Biological Processpositive regulation of filamentous growth of a population of unicellular organisms in response to starvation
Biological Processpositive regulation of hydrogen sulfide biosynthetic process
Biological Processpositive regulation of ribosomal protein gene transcription by RNA polymerase II
Biological Processpositive regulation of transcription by RNA polymerase I
Biological Processpositive regulation of transcription by RNA polymerase III
Biological Processregulation of cysteine metabolic process
Biological Processregulation of protein localization
Biological Processregulation of response to osmotic stress
Biological Processregulation of sphingolipid biosynthetic process
Biological Processsymbiont-mediated suppression of host resistance gene-dependent defense response

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase SCH9
  • EC number

Gene names

    • Name
      SCH9
    • ORF names
      CaO19.829, CaO19.8449
    • Ordered locus names
      CAALFM_C203940CA

Organism names

Accessions

  • Primary accession
    Q5AHG6
  • Secondary accessions
    • A0A1D8PGZ3

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Leads to reduced cell size and to sensitivity to rapamycin, caffeine and sodium dodecyl sulfate. Attenuates the virulence of in a mouse model of systemic candidiasis.

Miscellaneous

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004221061-787Serine/threonine-protein kinase SCH9

Keywords

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-82Disordered
Compositional bias13-34Polar residues
Compositional bias44-82Polar residues
Region132-172Disordered
Domain182-354C2
Compositional bias238-267Polar residues
Region238-280Disordered
Domain392-653Protein kinase
Domain654-729AGC-kinase C-terminal

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    787
  • Mass (Da)
    88,746
  • Last updated
    2017-05-10 v2
  • Checksum
    68669E0EC178936C
MVDFAKSLFGFGNYKKESSSQSPTPPPSAHSSQEQHHKSNTEEYPQSHLSQQQHSHRYQPPHMSEQSHQFPQQQQQQQQSGTNKFFPKTLVSAAPTTAVANHSSVYGTTSTTTNNYPEAYLNQTFKNNIYNPQQQQQQQAQQPPPEQQQSSAPYQNSANIQQPYGNQWGSSQDQDANIITIDKTGNKLSPASRDSPIKGKLKVTILEAKDIFATQPYVVCSFESSEFVTNAPDSYGKSPVSSFGHNNNQGHNGPRNMYNSNHGPSPKALPMKNSGNLFGQRPSMYQRQLSTPHLNLPNDSSNPIWNHDTIFDVVGSKSELDISVYDGARDDAFLGHVRISPSTDKNNKNESEWLQLGARITGETVSSGHIKIKWEYTSFDNNIKRSYGPDDFHFLRLLGKGTFGQVFQVRKKDTNRVYAMKILSKKVIVKKKEIAHTIGERNILVRTSAASSPFIVGLKFSFQTPSDLFLVTDFMSGGELFFHLQKEGRFNEDRSKFYTAELILALEHLHDNDIVYRDLKPENILLDANGHIALCDFGLSKADLNMDGTTNTFCGTTEYLAPEVLLDEQGYTKMVDFWSLGVLIFEMTCGWSPFHAENTQQMYKNIAFGKVRFPKDVLSPEGRSFVKGLLNRNPKHRLGATDDARELKAHPFFADIDWDLLRAKNIPPPFKPHIVSETDISNFDTEFTSENTSALKRQMEMATTPLSPGIQANFKGFTYVDDSTMDDHFARSYRANAFRPPGSFIPGDPNLPPDEEVLAEQIEEEDEMEVDEDQHMDDEFVNGRFDL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias13-34Polar residues
Compositional bias44-82Polar residues
Compositional bias238-267Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP017624
EMBL· GenBank· DDBJ
AOW27421.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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