SCH9_CANAL
ID SCH9_CANAL Reviewed; 787 AA.
AC Q5AHG6; A0A1D8PGZ3;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Serine/threonine-protein kinase SCH9;
DE EC=2.7.11.1;
GN Name=SCH9; OrderedLocusNames=CAALFM_C203940CA;
GN ORFNames=CaO19.829, CaO19.8449;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=14663094; DOI=10.1099/mic.0.26640-0;
RA Nobile C.J., Bruno V.M., Richard M.L., Davis D.A., Mitchell A.P.;
RT "Genetic control of chlamydospore formation in Candida albicans.";
RL Microbiology 149:3629-3637(2003).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20345900; DOI=10.1111/j.1567-1364.2010.00617.x;
RA Liu W., Zhao J., Li X., Li Y., Jiang L.;
RT "The protein kinase CaSch9p is required for the cell growth, filamentation
RT and virulence in the human fungal pathogen Candida albicans.";
RL FEMS Yeast Res. 10:462-470(2010).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21335533; DOI=10.1128/ec.00289-10;
RA Stichternoth C., Fraund A., Setiadi E., Giasson L., Vecchiarelli A.,
RA Ernst J.F.;
RT "Sch9 kinase integrates hypoxia and CO2 sensing to suppress hyphal
RT morphogenesis in Candida albicans.";
RL Eukaryot. Cell 10:502-511(2011).
CC -!- FUNCTION: Protein kinase that is part of growth control pathway which
CC is at least partially redundant with the cAMP pathway (By similarity).
CC Plays a role in filamentous growth and virulence. Prevents hypha
CC formation specifically under hypoxia at high CO(2) levels. Required for
CC chlamydospore formation, distinctive morphological feature of the
CC fungal pathogen C.albicans that can be induced to form in oxygen-
CC limited environments and has been reported in clinical specimens.
CC {ECO:0000250, ECO:0000269|PubMed:14663094, ECO:0000269|PubMed:20345900,
CC ECO:0000269|PubMed:21335533}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- DISRUPTION PHENOTYPE: Leads to reduced cell size and to sensitivity to
CC rapamycin, caffeine and sodium dodecyl sulfate. Attenuates the
CC virulence of in a mouse model of systemic candidiasis.
CC {ECO:0000269|PubMed:20345900, ECO:0000269|PubMed:21335533}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; CP017624; AOW27421.1; -; Genomic_DNA.
DR RefSeq; XP_720953.2; XM_715860.2.
DR AlphaFoldDB; Q5AHG6; -.
DR SMR; Q5AHG6; -.
DR STRING; 237561.Q5AHG6; -.
DR PRIDE; Q5AHG6; -.
DR GeneID; 3637421; -.
DR KEGG; cal:CAALFM_C203940CA; -.
DR CGD; CAL0000175489; SCH9.
DR VEuPathDB; FungiDB:C2_03940C_A; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_52_2_1; -.
DR InParanoid; Q5AHG6; -.
DR OrthoDB; 614710at2759; -.
DR PHI-base; PHI:2557; -.
DR PRO; PR:Q5AHG6; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
DR GO; GO:0044114; P:development of symbiont in host; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1900438; P:negative regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Virulence.
FT CHAIN 1..787
FT /note="Serine/threonine-protein kinase SCH9"
FT /id="PRO_0000422106"
FT DOMAIN 182..354
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 392..653
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 654..729
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 518
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 398..406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 787 AA; 88746 MW; 68669E0EC178936C CRC64;
MVDFAKSLFG FGNYKKESSS QSPTPPPSAH SSQEQHHKSN TEEYPQSHLS QQQHSHRYQP
PHMSEQSHQF PQQQQQQQQS GTNKFFPKTL VSAAPTTAVA NHSSVYGTTS TTTNNYPEAY
LNQTFKNNIY NPQQQQQQQA QQPPPEQQQS SAPYQNSANI QQPYGNQWGS SQDQDANIIT
IDKTGNKLSP ASRDSPIKGK LKVTILEAKD IFATQPYVVC SFESSEFVTN APDSYGKSPV
SSFGHNNNQG HNGPRNMYNS NHGPSPKALP MKNSGNLFGQ RPSMYQRQLS TPHLNLPNDS
SNPIWNHDTI FDVVGSKSEL DISVYDGARD DAFLGHVRIS PSTDKNNKNE SEWLQLGARI
TGETVSSGHI KIKWEYTSFD NNIKRSYGPD DFHFLRLLGK GTFGQVFQVR KKDTNRVYAM
KILSKKVIVK KKEIAHTIGE RNILVRTSAA SSPFIVGLKF SFQTPSDLFL VTDFMSGGEL
FFHLQKEGRF NEDRSKFYTA ELILALEHLH DNDIVYRDLK PENILLDANG HIALCDFGLS
KADLNMDGTT NTFCGTTEYL APEVLLDEQG YTKMVDFWSL GVLIFEMTCG WSPFHAENTQ
QMYKNIAFGK VRFPKDVLSP EGRSFVKGLL NRNPKHRLGA TDDARELKAH PFFADIDWDL
LRAKNIPPPF KPHIVSETDI SNFDTEFTSE NTSALKRQME MATTPLSPGI QANFKGFTYV
DDSTMDDHFA RSYRANAFRP PGSFIPGDPN LPPDEEVLAE QIEEEDEMEV DEDQHMDDEF
VNGRFDL
