ID   CLA4_CANAX              Reviewed;         971 AA.
AC   O14427;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Serine/threonine-protein kinase CLA4;
DE            EC=2.7.11.1;
GN   Name=CLA4;
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].
RX   PubMed=9259554; DOI=10.1016/s0960-9822(06)00252-1;
RA   Leberer E., Ziegelbauer K., Schmidt A., Harcus D., Dignard D., Ash J.,
RA   Johnson L., Thomas D.Y.;
RT   "Virulence and hyphal formation of Candida albicans require the Ste20p-like
RT   protein kinase CaCla4p.";
RL   Curr. Biol. 7:539-546(1997).
CC   -!- FUNCTION: Essential for virulence and morphological switching (hyphal
CC       formation) of C.albicans.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U87996; AAB68613.1; -; Genomic_DNA.
DR   AlphaFoldDB; O14427; -.
DR   SMR; O14427; -.
DR   VEuPathDB; FungiDB:C1_10210C_A; -.
DR   VEuPathDB; FungiDB:CAWG_00412; -.
DR   BRENDA; 2.7.11.1; 1096.
DR   PHI-base; PHI:85; -.
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; 2.30.29.30; -; 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; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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; Serine/threonine-protein kinase;
KW   Transferase; Virulence.
FT   CHAIN           1..971
FT                   /note="Serine/threonine-protein kinase CLA4"
FT                   /id="PRO_0000085864"
FT   DOMAIN          67..178
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          231..244
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          680..935
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        803
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         686..694
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         710
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   971 AA;  106890 MW;  AD6F0DBBC6CF624B CRC64;
     MTSIYTSDLK NHRRAPPPPN GAAGSGSGSG SGSGSGSGSL ANIVTSSNSL GVTANQTKPI
     QLNINSSKRQ SGWVHVKDDG IFTSFRWNKR FMVINDKTLN FYKQEPYSSD GNSNSNTPDL
     SFPLYLINNI NLKPNSGYSK TSQSFEIVPK NNNKSILISV KTNNDYLDWL DAFTTKCPLV
     QIGENNSGVS SSHPHLQIQH LTNGSLNGNS SSSPTSGLLS SSVLTGGNSG VSGPINFTHK
     VHVGFDPASG NFTGLPDTWK SLLQHSKITN EDWKKDPVAV IEVLEFYSDI NGGNSAAGTP
     IGSPMINSKT NNNNNDPNNY SSTKNNVQEA NLQEWVKPPA KSTVSQFKPS RAAPKPPTPY
     HLTQLNGSSH QHTSSSGSLP SSGNNNNNNS TNNNNTKNVS PLNNLMNKSE LIPARRAPPP
     PTSGTSSDTY SNKNHQDRSG YEQQRQQRTD SSQQQQQQKQ HQYQQKSQQQ QQQPQQPLSS
     HQGGTSHIPK QVPPTLPSSG PPTQAASGKS MPSKIHPDLK IQQGTNNYIK SSGTDANQVD
     GDAKQFIKPF NLQSKKSQQQ LASKQPSPPS SQQQQQKPMT SHGLMGTSHS VTKPLNPVND
     PIKPLNLKSS KSKEALNETS GVSKTPSPTD KSNKPTAPAS GPAVTKTAKQ LKKERERLND
     LQIIAKLKTV VNNQDPKPLF RIVEKAGQGA SGNVYLAEMI KDNNRKIAIK QMDLDAQPRK
     ELIINEILVM KDSQHKNIVN FLDSYLIGDN ELWVIMEYMQ GGSLTEIIEN NDFKLNEKQI
     ATICFETLKG LQHLHKKHII HRDIKSDNVL LDAYGNVKIT DFGFCAKLTD QRNKRATMVG
     TPYWMAPEVV KQKEYDEKVD VWSLGIMTIE MIEGEPPYLN EEPLKALYLI ATNGTPKLKK
     PELLSNSIKK FLSICLCVDV RYRASTDELL EHSFIQHKSG KIEELAPLLE WKKQQQKHQQ
     HKQETSDTGF A