ID   MRKC_DICDI              Reviewed;         773 AA.
AC   Q54TA3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable serine/threonine-protein kinase MARK-C;
DE            EC=2.7.11.1;
GN   Name=mrkC; ORFNames=DDB_G0281895;
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=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).
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. SNF1 subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000043; EAL66507.1; -; Genomic_DNA.
DR   RefSeq; XP_640486.1; XM_635394.1.
DR   AlphaFoldDB; Q54TA3; -.
DR   SMR; Q54TA3; -.
DR   STRING; 44689.DDB0216323; -.
DR   PaxDb; Q54TA3; -.
DR   EnsemblProtists; EAL66507; EAL66507; DDB_G0281895.
DR   GeneID; 8623300; -.
DR   KEGG; ddi:DDB_G0281895; -.
DR   dictyBase; DDB_G0281895; mrkC.
DR   eggNOG; KOG0586; Eukaryota.
DR   HOGENOM; CLU_361869_0_0_1; -.
DR   InParanoid; Q54TA3; -.
DR   OMA; TWKYKDI; -.
DR   PRO; PR:Q54TA3; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR001772; KA1_dom.
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; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; SSF103243; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50032; KA1; 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; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..773
FT                   /note="Probable serine/threonine-protein kinase MARK-C"
FT                   /id="PRO_0000338411"
FT   DOMAIN          46..300
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          724..773
FT                   /note="KA1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          362..390
FT                   /evidence="ECO:0000255"
FT   COILED          445..474
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         52..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   773 AA;  87926 MW;  1729BF18BCC5BA34 CRC64;
     MESNKSSSHG DVSTSPSFLN NHHQFNNGGD IIPKKKKNRI MHVGSYEVGK TLGNGTFGKV
     KLGTNICTKE NVAIKFIKNN KLSGKQKETC FREIDIMKLL DHPNIVKLLD VVDKREEEGT
     TYLIVEYVSG GELFDYIVAR EYIKEKEARK FFRQMISAIE YCHANLIVHR DLKPENLLLD
     SNGDIKISDF GLSNNIQPGK LLESFCGSPL YAAPEILKAE KYLGPPVDIW SLGVIMYAVL
     CGNLPWEGDS QAEISFNSVH GNYEDPTHLS AEAVHILRRM IVPNPKDRAT IQELKNHPWT
     NIDYQEIPKS HLPPRDAVHE IKEDIFAHLI SLGFPNTKET RDIILKNENC GIVNVYHLLL
     DRYASKEVEN LKSKLELLSK RKKSFSDKRN PSTNSLASIP EDSNDLSSNN NNNQQQQNSP
     PSKTNSSSTS SSNRESNNNS PSQGSIKEIS LDELDNHIEQ LDNDIENSDN NKSSSLTRRS
     SDPNKDIENS LKAQGLFSSY SAPGVPNSDH NYDFETYQQQ QQYQQQLHQQ QLQLQQQYQS
     QIQSDISFPH DDVEIESYSI QQQQLQQQQQ QQQEQHKEDN NKPNTNLRRN SIAVSTFMED
     EPNEMPINNL YKMNEQIQQQ PIIGGSGNVM RSQFNQTLPT IDQQPVIEAP KTRRMSLDSR
     MLNGDQQSLV EKNQHMASPR TSKGIFKSST TTTKSPEKTI IELKRSLEES GLFTKKKGPY
     LFLCFDEDNS VKFQIEIVKI CNLDLTGIQL KRLSGDTWKY KDICTELVES MKL