MKCE_DICDI
ID MKCE_DICDI Reviewed; 715 AA.
AC Q54TN4;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable serine/threonine-protein kinase mkcE {ECO:0000312|EMBL:EAL66586.1};
DE EC=2.7.11.1;
DE AltName: Full=MAP kinase cascade E {ECO:0000312|dictyBase:DDB_G0281649};
GN Name=mkcE {ECO:0000312|EMBL:EAL66586.1}; ORFNames=DDB_G0281649;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL66586.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL66586.1};
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; AAFI02000042; EAL66586.1; -; Genomic_DNA.
DR RefSeq; XP_640557.1; XM_635465.1.
DR AlphaFoldDB; Q54TN4; -.
DR SMR; Q54TN4; -.
DR STRING; 44689.DDB0230009; -.
DR PaxDb; Q54TN4; -.
DR EnsemblProtists; EAL66586; EAL66586; DDB_G0281649.
DR GeneID; 8623167; -.
DR KEGG; ddi:DDB_G0281649; -.
DR dictyBase; DDB_G0281649; mkcE.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_386588_0_0_1; -.
DR InParanoid; Q54TN4; -.
DR OMA; KNDEEIW; -.
DR PRO; PR:Q54TN4; -.
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: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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..715
FT /note="Probable serine/threonine-protein kinase mkcE"
FT /id="PRO_0000381743"
FT DOMAIN 427..683
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 207..241
FT /evidence="ECO:0000255"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 550
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 433..441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 715 AA; 79470 MW; F8FA4548C2DFC9C6 CRC64;
MQKIVSFLKK KKEPNSWSNF DRSDDKSKSL SKKGSLYANG NYDGGGSGSG SGGSSSNSSG
SSRKINTGGN NRNGGGMVHS PSNSSISSTS SNNSNSTTAS SSSKLKGNKN RNSSGKQKNS
SSQHQQYGNT YYLDDECDSD DFIPGEVRSI SKTIDFSKSE RKWLTSLNIP QELLDGNINV
LLNVLNFLSK KEGILYIQTP TNIINNTGKK NFQQQQLQQL QQQQQQQQLQ QQQHQQHNHQ
IYGNGNNNNL NVNVNVNGNN NNSNNNNGNY TSYVNSRSNS IASNNSSITP STSCSNLNND
NNNNNNNNCT DNNSNNNNNN NNNNSTTTTT TITNTNVNMI GASNINSSKS NLNSLLLSGG
SNGNGGVDNL SSTTTSLSQN PPIQPMRRSD YNRIFIEPGK FYIFPESESF ALARLVVEEE
DPSKLFRIGE NAEVKGAFGT VYQVFYVNGQ YNNVDVALKK MDHKSEKKRR NNLNEISILR
YLKHPNIVTY INSYEKNDEE IWMVMEYMDG GTIRDAISNF TFTEKYVAYI TKEILHSLEY
LASLNIAHRD LKSSNIMINS KAEVKLIDFG FSIDLTHLKQ DINMCGSPFY MSPEQIQDKA
HGLAVDIWSL GIVVAEMVRG RVPHHKSKIK AMFLAGTVGV KFSKEKKYSC HWSPELFDFL
NVCLQMDPTK RPTPTQLLQH PFIATAATKA ETLDLLPLLF MSKTLSKLSR GRDNQ
