STE20_CANAW
ID STE20_CANAW Reviewed; 1224 AA.
AC C4YRB7; C4YRB8; O13431; Q5AGD7; Q92212;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
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; ORFNames=CAWG_04616/04617;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=WO-1;
RX PubMed=8917571; DOI=10.1073/pnas.93.23.13217;
RA Leberer E., Harcus D., Broadbent I.D., Clark K.L., Dignard D.,
RA Ziegelbauer K., Schmidt A., Gow N.A.R., Brown A.J.P., Thomas D.Y.;
RT "Signal transduction through homologs of the Ste20p and Ste7p protein
RT kinases can trigger hyphal formation in the pathogenic fungus Candida
RT albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13217-13222(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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:8917571}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEQ46270.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=EEQ46271.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; L47210; AAB65439.1; -; Genomic_DNA.
DR EMBL; CM000311; EEQ46271.1; ALT_TERM; Genomic_DNA.
DR EMBL; CM000311; EEQ46270.1; ALT_TERM; Genomic_DNA.
DR PIR; T18256; T18256.
DR AlphaFoldDB; C4YRB7; -.
DR SMR; C4YRB7; -.
DR STRING; 5476.C4YRB7; -.
DR EnsemblFungi; EEQ46270; EEQ46270; CAWG_04616.
DR EnsemblFungi; EEQ46271; EEQ46271; CAWG_04617.
DR HOGENOM; CLU_000288_26_0_1; -.
DR Proteomes; UP000001429; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1224
FT /note="Serine/threonine-protein kinase CST20"
FT /id="PRO_0000413041"
FT DOMAIN 469..482
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 947..1199
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..913
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..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1067
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 953..961
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 977
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 95
FT /note="D -> E (in Ref. 1; AAB65439)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="G -> S (in Ref. 1; AAB65439)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="H -> HNNNNNN (in Ref. 1; AAB65439)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="A -> G (in Ref. 1; AAB65439)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="L -> P (in Ref. 1; AAB65439)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1224 AA; 132197 MW; C835CCF4E4A859E0 CRC64;
MSILSENNPT PTSITDPNES SHLHNPELNS GTRVASGPGP GPEVESTPLA PPTEVMNTTS
ANTSSLSLGS PMHEKIKQFD QDEVDTGETN DRTIDSGSGD IDDSQQSHNN NNNESNPESS
EADDEKTQGM PPRMPGTFNV KGLHQGDDSD NEKQYTELTK SINKRTSKDS YSLGTLESPG
TLNALETNNV SPAVIEEEQH TSSLEDLSLS LQHQNENARL SAPRSAPPQV PTSKTSSFHD
MSSVISSSTS VHKIPSNPTS TRGSHLSSYK STLDPGKPAQ AAAPPPPEID IDNLLTKSEL
DSETDTLSSA TNSPNLLRND TLQGIPTRDD ENIDDSPRQL SQNTSATSRN TSGTSTSTVV
KNSRSGTSKS TSTSTAHNQT AAITPIIPSH NKFHQQVINT NATNSSSSLE PLGVGINSNS
SPKSGKKRKS GSKVRGVFSS MFGKNKSTSS SSSSNSGSNS HSQEVNIKIS TPFNAKHLAH
VGIDDNGSYT GLPIEWERLL SASGITKKEQ QQHPQAVMDI VAFYQDTSEN PDDAAFKKFH
FDNNKSSSSG WSNENTPPAT PGGSNSGSGS GGGGAPSSPH RTPPSSIIEK NNVEQKVITP
SQSMPTKTES KQSENQHPHE DNATQYTPRT PTSHVQEGQF IPSRPAPKPP STPLSSMSVS
HKTPSSQSLP RSDSQSDIRS STPKSHQDVS PSKIKIRSIS SKSLKSMRSR KSGDKFTHIA
PAPPPPSLPS IPKSKSHSAS LSSQLRPATN GSTTAPIPAS AAFGGENNAL PKQRINEFKA
HRAPPPPPSA PPAPPVPPAP PANLLSEQTS EIPQQRTAPS QALADVTAPT NIYEIQQTKY
QEAQQKLREK KARELEEIQR LREKNERQNR QQETGQNNAD TASGGSNIAP PVPVPNKKPP
SGSGGGRDAK QAALIAQKKR EEKKRKNLQI IAKLKTICNP GDPNELYVDL VKIGQGASGG
VFLAHDVRDK SNIVAIKQMN LEQQPKKELI INEILVMKGS SHPNIVNFID SYLLKGDLWV
IMEYMEGGSL TDIVTHSVMT EGQIGVVCRE TLKGLKFLHS KGVIHRDIKS DNILLNMDGN
IKITDFGFCA QINEINSKRI TMVGTPYWMA PEIVSRKEYG PKVDVWSLGI MIIEMLEGEP
PYLNETPLRA LYLIATNGTP KLKDPESLSY DIRKFLAWCL QVDFNKRADA DELLHDNFIT
ECDDVSSLSP LVKIARLKKM SESD
