ID   KPSH1_PINFU             Reviewed;         415 AA.
AC   Q4KTY1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Serine/threonine-protein kinase H1 homolog;
DE            EC=2.7.11.1;
GN   Name=PSKH1;
OS   Pinctada fucata (Akoya pearl oyster) (Pinctada imbricata fucata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=50426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Dai Y., Xie L., Xiong X., Chen L., Fan W., Zhang R.;
RT   "Characterization of a novel protein serine kinase from Pinctada fucata.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AY818357; AAX19940.1; -; mRNA.
DR   AlphaFoldDB; Q4KTY1; -.
DR   SMR; Q4KTY1; -.
DR   PRIDE; Q4KTY1; -.
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; 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; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..415
FT                   /note="Serine/threonine-protein kinase H1 homolog"
FT                   /id="PRO_0000086170"
FT   DOMAIN          80..334
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         86..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   415 AA;  47155 MW;  8897AFA6C9B800DA CRC64;
     MGCMSSKLVP EGPSGNQAVV EVFNNERNKE YNRQNPHQNR GPRDPTKDPK NAGPPPEGQR
     SNRKVKKYRD KFDPRVTAKY DIKALIGRGN FSKVVRVEHR VTKQPYAIKM IDRVQGKEVF
     ESEVAVLRRV KHSYIIQLIE VFETKDKVYM VMELATGGEL FDRIIAKGSF TERDATRVLN
     MVLDGVKYLH GLGITHRDLK PENLLYYHPG HDSKIMITDF GLSSTRKGPE NFMRTTCGTP
     EYIAPEIIAR KPYMCQVDMW AVGVITYILL SGTMPFDDEN KTRLYRLILK AKYSYAGEHW
     KDVSAQAKDF IDKLLVVSPG DRLSAADALK HQWLISNAAS SSNKNLHRTI SQNLIHRQST
     RANSTKSAKS TRSTKSNKSN RSGRSLRSEH RRVMPDEIDE LHRDPDVQAD LASLG