ID   CBK1_PNECA              Reviewed;         507 AA.
AC   Q6TGC6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Serine/threonine-protein kinase CBK1;
DE            EC=2.7.11.1;
GN   Name=CBK1;
OS   Pneumocystis carinii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX   NCBI_TaxID=4754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15271923; DOI=10.1128/iai.72.8.4628-4636.2004;
RA   Kottom T.J., Limper A.H.;
RT   "Pneumocystis carinii cell wall biosynthesis kinase gene CBK1 is an
RT   environmentally responsive gene that complements cell wall defects of cbk-
RT   deficient yeast.";
RL   Infect. Immun. 72:4628-4636(2004).
CC   -!- FUNCTION: Protein kinase that seems to play a role in signaling
CC       pathways necessary for cell growth and mating.
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. COT1 subfamily. {ECO:0000305}.
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DR   EMBL; AY422071; AAR00227.1; -; mRNA.
DR   AlphaFoldDB; Q6TGC6; -.
DR   SMR; Q6TGC6; -.
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   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..507
FT                   /note="Serine/threonine-protein kinase CBK1"
FT                   /id="PRO_0000085695"
FT   DOMAIN          126..431
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          432..505
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        249
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         132..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         155
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   507 AA;  58561 MW;  CC0252F0E40266EE CRC64;
     MQKVSGSGKK TTAFQQRKSD SVYNNNEMNK GTSSISYDPV YFVRDASSFT KTTHERAASV
     KLKLEHLYKV TVEQTVERNQ RRMDFEAKLA QDRGSEERKK RQLNSLGQKE SQFLRLRRTK
     LSLNDFHTVK VIGKGAFGEV RLVQKIDTGK IYAMKTLLKS EMFKKDQLAH VKAERDVLAE
     SDSPWVVSLY YSFQDSQYLY LIMEFLPGGD LMTMLIKYDT FSEDVTRFYI AECILAIEAV
     HKLGFIHRDI KPDNILIDKT GHIKLSDFGL SMGFHKTHDN AYYQRLFESK INTSTSSTQN
     SLMVDTISLT MSSKDKIATW KKNRRIMAYS TVGTPDYIAP EIFTQHGYGQ ECDWWSLGAI
     MFECLIGWPP FCSENAHETY RKIINWRENL YFPEDLHLSA EAEDLIRKLL TSADQRLGRY
     GANDIKLHPF FRGVNWDTIR EINAPFIPQL KSITDTSYFE EIDTIPNITM NSPPVLQNKI
     PSDVDQNLAF VGYTYKRFDM MTQKGIL