STE20_CANAX
ID STE20_CANAX Reviewed; 1230 AA.
AC P0CY23; 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 31.
DE RecName: Full=Serine/threonine-protein kinase CST20;
DE EC=2.7.11.1;
GN Name=CST20; Synonyms=HST20, STE20;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=1066;
RX PubMed=8917572; DOI=10.1073/pnas.93.23.13223;
RA Koehler J.R., Fink G.R.;
RT "Candida albicans strains heterozygous and homozygous for mutations in
RT mitogen-activated protein kinase signaling components have defects in
RT hyphal development.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13223-13228(1996).
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:8917572}.
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; U73457; AAB38875.1; -; Genomic_DNA.
DR PIR; T18259; T18259.
DR AlphaFoldDB; P0CY23; -.
DR SMR; P0CY23; -.
DR VEuPathDB; FungiDB:C5_02340C_A; -.
DR VEuPathDB; FungiDB:CAWG_04616; -.
DR VEuPathDB; FungiDB:CAWG_04617; -.
DR BRENDA; 2.7.11.1; 1096.
DR PHI-base; PHI:461; -.
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..1230
FT /note="Serine/threonine-protein kinase CST20"
FT /id="PRO_0000086685"
FT DOMAIN 475..488
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 953..1205
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..919
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..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1073
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 959..967
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 983
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1230 AA; 132862 MW; 2B2AC4C133B9FE81 CRC64;
MSILSENNPT PTSITDPNKS SHLHNPELNS GTRVASGPGP GPEAESTPLA PPTEVMNTTS
ANTSSLSLGS PMHEKIKQFD QDEVDTGETN DRTIESGSGD IDDSQQSHNN NNNNNNNNNE
SNPESSEGDD EKTQGMPPRM PGTFNVKGLH QGDDSDNEKQ YTELTKSINK RTSKDSYSPG
TLESPGTLNA LETNNVSPAV IEEEQHTSSL EDLSLSLQHQ NENARLSAPR SAPPQVPTSK
TSSFHDMSSV ISSSTSVHKI PSNPTSTRGS HLSSYKSTLD PGKPAQAAAP PPPEIDIDNL
LTKSELDSET DTLSSATNSP NLLRNDTLQG IPTRDDENID DSPRQLSQNT SATSRNTSGT
STSTVVKNSR SGTSKSTSTS TAHNQTAAIT PIIPSHNKFH QQVINTNATN SLSSLEPLGV
GINSNSSPKS GKKRKSGSKV RGVFSSMFGK NKSTSSSSSS NSGSNSHSQE VNIKISTPFN
AKHLAHVGID DNGSYTGLPI EWERLLSASG ITKKEQQQHP QAVMDIVAFY QDTSENPDDA
AFKKFHFDNN KSSSSGWSNE NTPPATPGGS NSGSGSGGGG APSSPHRTPP SSIIEKNNVE
QKVITPSQSM PTKTESKQSE NQHPHEDNAT QYTPRTPTSH VQEGQFIPSR PAPKPPSTPL
SSMSVSHKTP SSQSLPRSDS QSDIRSSTPK SHQDVSPSKI KIRSISSKSL KSMRSRKSGD
KFTHIAPAPP PPSLPSIPKS KSHSASLSSQ LRPATNGSTT APIPASAAFG GENNALPKQR
INEFKAHRAP PPPPSAPPAP PVPPAPPANL LSEQTSEIPQ QRTAPSQALA DVTAPTNIYE
IQQTKYQEAQ QKLREKKARE LEEIQRLREK NERQNRQQET GQNNADTASG GSNIAPPVPV
PNKKPPSGSG GGRDAKQAAL IAQKKREEKK RKNLQIIAKL KTICNPGDPN ELYVDLVKIG
QGASGGVFLA HDVRDKSNIV AIKQMNLEQQ PKKELIINEI LVMKGSSHPN IVNFIDSYLL
KGDLWVIMEY MEGGSLTDIV THSVMTEGQI GVVCRETLKG LKFLHSKGVI HRDIKSDNIL
LNMDGNIKIT DFGFCAQINE INSKRITMVG TPYWMAPEIV SRKEYGPKVD VWSLGIMIIE
MLEGEPPYLN ETPLRALYLI ATNGTPKLKD PESLSYDIRK FLAWCLQVDF NKRADADELL
HDNFITECDD VSSLSPLVKI ARLKKMSESD
