ID   PKD1_DICDI              Reviewed;         714 AA.
AC   P34100; Q550C5; Q86AR2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Developmentally-regulated protein kinase 1;
DE            EC=2.7.11.1;
GN   Name=pkaD; Synonyms=PK1; ORFNames=DDB_G0277145;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 299-714, AND DEVELOPMENTAL STAGE.
RX   PubMed=1864510; DOI=10.1016/0378-1119(91)90538-m;
RA   Buerki E., Anjard C., Scholder J.-C., Reymond C.D.;
RT   "Isolation of two genes encoding putative protein kinases regulated during
RT   Dictyostelium discoideum development.";
RL   Gene 102:57-65(1991).
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   -!- DEVELOPMENTAL STAGE: Expressed in vegetatively growing cells and during
CC       development. {ECO:0000269|PubMed:1864510}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other members of the AGC Ser/Thr protein kinase
CC       family, lacks the AGC-kinase C-terminal domain at the C-terminus.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000019; EAL68758.1; -; Genomic_DNA.
DR   EMBL; M38794; AAA33239.1; -; mRNA.
DR   PIR; PQ0207; PQ0207.
DR   RefSeq; XP_642691.1; XM_637599.1.
DR   AlphaFoldDB; P34100; -.
DR   SMR; P34100; -.
DR   STRING; 44689.DDB0185224; -.
DR   PaxDb; P34100; -.
DR   EnsemblProtists; EAL68758; EAL68758; DDB_G0277145.
DR   GeneID; 8620880; -.
DR   KEGG; ddi:DDB_G0277145; -.
DR   dictyBase; DDB_G0277145; pkaD.
DR   eggNOG; KOG0616; Eukaryota.
DR   HOGENOM; CLU_387059_0_0_1; -.
DR   InParanoid; P34100; -.
DR   OMA; IMLNISH; -.
DR   PRO; PR:P34100; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd05123; STKc_AGC; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045270; STKc_AGC.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..714
FT                   /note="Developmentally-regulated protein kinase 1"
FT                   /id="PRO_0000086551"
FT   DOMAIN          334..589
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          88..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        457
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         340..348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         488
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        299..325
FT                   /note="IICSSPIVNIPPPFYLDGSIDPVENID -> LFHKAKFQECHKNLISIVHYV
FT                   AFKVLT (in Ref. 3; AAA33239)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   714 AA;  81674 MW;  2C8F7A359D95ED1F CRC64;
     MSAILNNYQY IPNNSLNSNN SNNGNNSTIL SLCDNATQLM DIIMREFNEP IFDYNQNSSE
     INKSLVKTIK SLLETLTKNL NNINNNINNN ISNNNNNNNN NNNNNNNNNN NNNNINNNNN
     FNTPQIIIND NYKLYTPPPA PMLKGLSCEV PFETMEYMQP LDLSNNNISL NNSCNMINND
     NNNNNNNNNN NNNNNNNNNN QQQQFYNAPS SNSTPSHSSP SSPTTSSIPF HPNFTLSQDN
     FNQQLQNNNN SNNNSNNNNN NNIINNNFLQ NSQQTNQSLQ FSTTQPNLNN FYDIPKQPII
     CSSPIVNIPP PFYLDGSIDP VENIDWKRTK ISDFNFYGSL GSGSFGTAKL CRHRGSGLFF
     CSKTLRRETI VHEKHKEHVN NEINIMLNIS HPYIVKTYST FNTPTKIHFI MEYAGKKDLF
     HHLRANKCFT EQTTKLIVAE IVLAIEYLHA ENIIYRDLKP ENILIDEKGH IKLTDFGFSK
     KTVGGKNTSS VCGTFDYMAP EILNSSNGHG KPVDWWALGV VVYELVTGKL PFSNSKESLL
     NRKADFQLIF QNSYLSDEIK DFIFQLLSVD PSKRLGTFDS CSIRNHKWFS DINWLHLESK
     YQIDGPLSTL NSFINCDFNI NLLKKSKSYT EQQQQQQQLP QQQQQQQQNN QLFNQTLQQQ
     NFNFHPIQPQ QQQQQQFFNF QFNNNNFNNN NNNNNNFNEA CTSNTCGGTT ASIF