MKCC_DICDI
ID MKCC_DICDI Reviewed; 891 AA.
AC Q54JQ1;
DT 01-SEP-2009, 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 mkcC {ECO:0000312|EMBL:EAL63573.1};
DE EC=2.7.11.1;
DE AltName: Full=MAP kinase cascade C {ECO:0000312|dictyBase:DDB_G0287853};
GN Name=mkcC {ECO:0000312|EMBL:EAL63573.1}; ORFNames=DDB_G0287853;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL63573.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL63573.1};
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 Evidence={ECO:0000250|UniProtKB:Q869N2};
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; Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000104; EAL63573.1; -; Genomic_DNA.
DR RefSeq; XP_637101.1; XM_632009.1.
DR AlphaFoldDB; Q54JQ1; -.
DR SMR; Q54JQ1; -.
DR STRING; 44689.DDB0229967; -.
DR PaxDb; Q54JQ1; -.
DR PRIDE; Q54JQ1; -.
DR EnsemblProtists; EAL63573; EAL63573; DDB_G0287853.
DR GeneID; 8626355; -.
DR KEGG; ddi:DDB_G0287853; -.
DR dictyBase; DDB_G0287853; mkcC.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_324262_0_0_1; -.
DR InParanoid; Q54JQ1; -.
DR OMA; CIAYVAK; -.
DR PRO; PR:Q54JQ1; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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: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 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..891
FT /note="Probable serine/threonine-protein kinase mkcC"
FT /id="PRO_0000381741"
FT DOMAIN 616..864
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..588
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 41..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 735
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 622..630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 891 AA; 96978 MW; 992E96F004755B66 CRC64;
MDVEFTPSDT NKFEANITKQ HQVIELNNQE EQQQPEQQEQ PEQQEELKDN NEKIKTSEDS
TTTTTTTATI TTTGENSISI TVTEANNNTN QLNKSTSSSS SLNNNKNEDN KSVTASIAPS
SPVIESSAIE SAIDSPYISS ASVFSNATNN NNNTTTTNVV VPPPQLLESS TENITSAAEI
TPVTTTTTEE TINIPKESIE VQKQLAETTT TAAITTTNST QVTSTTVTNP DKLKCKMHRS
NFIMTQIGGK KFTEMTLEQL LDEDDPQTGM GFKNPGPQGF LEYVGDTAPP PTPPPISTSN
TTGKNTGKNS TTGKSEGKKA TSNSSNVPPS PVLASSASPS PKLKSSSSSI RNSGAISGTS
ENGGGGNGSG TISKNTAPTT GNSTTTTTTT TSTTTSSSKD RKSVVQKQST LGRLQKNEEE
RRKRKEQKRS RAREKPILIA GIEDLPAECL KMVKKSKIPE DKLIQHLNIL LPILRFRTGY
NLRHVPIVSS NNSTNSLGSS INKNNSNNTT TTTTTTNTNN KSPEVSTNSL DVNIINQNQN
QTNSVQNNQI NTSSNVITTN VIPTTTASQS SQAPYHPSHN GNEEDDYDDG SRLENAILPK
GTVDLIETDR DVKKLYKNLK QIGSGGFGSV FLAKSTVDKC EIAIKKIAHV SAKAQRTNLN
EIGFLNFCKH PNIVSYLRSH LVDDTIWIAM EYMQGGTLTE ASQGHTFNES CIAYVAKGML
EGLMYLHAHN IVHRDIKSGN IMMTIDGKIK IVDFGLCVDA NERKLVHMAG SPFWMSPEMI
RGESYGCPTD IWSFAICLLE LANGEPPHRK SSLTAMFTTA TEGCAGLDKP ERWTEHFTHF
LNLCLEMDPS KRSTAEQLLK HPWINLSENP ETMKKILAQI FIANVMNHLD N
