STE20_CANAL
ID STE20_CANAL Reviewed; 1228 AA.
AC P0CY24; A0A1D8PNE1; O13431; Q5AGD7; Q92212;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Serine/threonine-protein kinase CST20;
DE EC=2.7.11.1;
GN Name=CST20; Synonyms=HST20, STE20; OrderedLocusNames=CAALFM_C502340CA;
GN ORFNames=CaO19.11717, CaO19.4242;
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=12453219; DOI=10.1046/j.1365-2958.2002.03249.x;
RA Chen J., Chen J., Lane S., Liu H.;
RT "A conserved mitogen-activated protein kinase pathway is required for
RT mating in Candida albicans.";
RL Mol. Microbiol. 46:1335-1344(2002).
CC -!- FUNCTION: MAP4K component of the MAPK pathway required for the mating
CC pheromone response, and the regulation of cell polarity and cell cycle.
CC Phosphorylates histone H2B to form H2BS10ph (By similarity). Required
CC for hyphal formation and virulence. {ECO:0000250,
CC ECO:0000269|PubMed:12453219}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; CP017627; AOW29660.1; -; Genomic_DNA.
DR RefSeq; XP_720551.1; XM_715458.1.
DR AlphaFoldDB; P0CY24; -.
DR SMR; P0CY24; -.
DR BioGRID; 1220755; 2.
DR STRING; 237561.P0CY24; -.
DR PRIDE; P0CY24; -.
DR GeneID; 3637790; -.
DR KEGG; cal:CAALFM_C502340CA; -.
DR CGD; CAL0000198103; CST20.
DR VEuPathDB; FungiDB:C5_02340C_A; -.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_000288_26_0_1; -.
DR InParanoid; P0CY24; -.
DR OMA; RKFLAWC; -.
DR OrthoDB; 757766at2759; -.
DR PRO; PR:P0CY24; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IGI:CGD.
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:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IGI:CGD.
DR GO; GO:1990277; P:parasexual reproduction with cellular fusion; IMP:CGD.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50108; CRIB; 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1228
FT /note="Serine/threonine-protein kinase CST20"
FT /id="PRO_0000413040"
FT DOMAIN 473..486
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 951..1203
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1071
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 957..965
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 981
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1228 AA; 132773 MW; EFDEE947116E7BBF CRC64;
MSILSENNPT QTSITDPNES SHLHNPELNS GTRVASGPGP GPEVESTPLA PPTEVMNTTS
ANTSSLSLGS PMHEKIKQFD QDEVDTGETN DRTIESGSSD IDDSQQSHNN NNNNNNNESN
PESSEADDEK TQGMPPRMPG TFNVKGLHQG DDSDNEKQYT ELTKSINKRT SKDSYSPGTL
ESPGTLNALE TNNVSPAVIE EEQHTSSLED LSLSLQHQNE NARLSAPRSA PPQVSTSKTS
SFHDMSSVIS SSTSVHKIPS NPTSTRGSHL SSYKSTLDPG KPAQAAAPPP PEIDIDNLLT
KSELDSETDT LSSATNSPNL LRNDTLQGIP TRDDENIDDS PRQLSQNTSA TSRNTSGTST
STVVKNSRSG TSKLTSTSTA HNQTAAITPI IPSHNKFHQQ VINTNSTNSS SSLEPLGVGI
NSNSSPKNGK KRKSGSKVRG VFSSMFGKNK STSSSSSSNS GSNSHSQEVN IKISTPFNAK
HLAHVGIDDN GSYTGLPIEW ERLLSASGIT KKEQQQHPQA VMDIVAFYQD TSENPDDAAF
KKFHFDNNKS SSSGWSNENT PPATPGGSNS GSGGGGGGAP SSPHRTPPSS IIEKNNVEQK
VITPSQSMPT KTESKQSENQ HPHEDNATQY TPRTPTSHVQ EGQFIPSRPA PKPPSTPLSS
MSVSHKTPSS QSLPRSDSQS DIRSSTPKSH QDISPSKIKI RSISSKSLKS MRSRKSGDKF
THIAPAPPPP SLPSIPKSKS HSASLSSQLR PATNGSTTAP IPASAAFGGE NNALPRQRIN
EFKAHRAPPP PPSASPAPPV PPAPPANLLS EQTSEIPQQR TAPSQALADV TAPTNIYEIQ
QTKYQEAQQK LREKKARELE EIQRLREKNE RQNRQQETGQ NNADTASGGS NIAPPVPVPN
KKPPSGSGGG RDAKQAALIA QKKREEKKRK NLQIIAKLKT ICNPGDPNEL YVDLVKIGQG
ASGGVFLAHD VRDKSNIVAI KQMNLEQQPK KELIINEILV MKGSSHPNIV NFIDSYLLKG
DLWVIMEYME GGSLTDIVTH SVMTEGQIGV VCRETLKGLK FLHSKGVIHR DIKSDNILLN
MDGNIKITDF GFCAQINEIN SKRITMVGTP YWMAPEIVSR KEYGPKVDVW SLGIMIIEML
EGEPPYLNET PLRALYLIAT NGTPKLKDPE SLSYDIRKFL AWCLQVDFNK RADADELLHD
NFITECDDVS SLSPLVKIAR LKKMSESD
