MKCA_DICDI
ID MKCA_DICDI Reviewed; 860 AA.
AC Q54MY9; Q23916;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable serine/threonine-protein kinase mkcA {ECO:0000312|EMBL:EAL64551.1};
DE EC=2.7.11.1;
DE AltName: Full=MAP kinase cascade A;
GN Name=mkcA {ECO:0000312|EMBL:EAL64551.1}; Synonyms=DG1023;
GN ORFNames=DDB_G0285427;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB03507.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8986798; DOI=10.1073/pnas.93.26.15260;
RA Shaulsky G., Escalante R., Loomis W.F.;
RT "Developmental signal transduction pathways uncovered by genetic
RT suppressors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15260-15265(1996).
RN [2] {ECO:0000312|EMBL:EAL64551.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL64551.1};
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 -!- FUNCTION: Coordinates organism morphology with cellular differentiation
CC during development. Negative regulator of sporulation, synchronizing
CC encapsulation with culmination. May have an additional function in
CC prestalk cells. {ECO:0000269|PubMed:8986798}.
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 -!- DEVELOPMENTAL STAGE: Expressed at constant levels during growth and
CC throughout development. Uniformly expressed throughout the prespore and
CC the prestalk regions at the finger stage as well as during culmination.
CC {ECO:0000269|PubMed:8986798}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. {ECO:0000255}.
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DR EMBL; U60169; AAB03507.1; -; Genomic_DNA.
DR EMBL; AAFI02000079; EAL64551.1; -; Genomic_DNA.
DR RefSeq; XP_638154.1; XM_633062.1.
DR AlphaFoldDB; Q54MY9; -.
DR SMR; Q54MY9; -.
DR STRING; 44689.DDB0191179; -.
DR PaxDb; Q54MY9; -.
DR EnsemblProtists; EAL64551; EAL64551; DDB_G0285427.
DR GeneID; 8625202; -.
DR KEGG; ddi:DDB_G0285427; -.
DR dictyBase; DDB_G0285427; mkcA.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_332733_0_0_1; -.
DR InParanoid; Q54MY9; -.
DR OMA; QYPFQES; -.
DR PRO; PR:Q54MY9; -.
DR Proteomes; UP000002195; Chromosome 4.
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; ISS:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0045595; P:regulation of cell differentiation; IGI:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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; Coiled coil; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Sporulation; Transferase.
FT CHAIN 1..860
FT /note="Probable serine/threonine-protein kinase mkcA"
FT /id="PRO_0000379938"
FT DOMAIN 585..836
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 17..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..375
FT /evidence="ECO:0000255"
FT COMPBIAS 264..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 706
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 591..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT BINDING 616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT CONFLICT 506
FT /note="F -> L (in Ref. 1; AAB03507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 860 AA; 97846 MW; D6DF1E42D6AA3759 CRC64;
MDNNSTLNNI TITVASSHNN TTTNSNNNNN NNNGSNSNNN NEQLNTLSNS ITSLKSLNIS
GSGVITNNSE VNTPSEGNIT PLPLLSLSDA LSPLRELYSC LYVGDIRALM SNQYLKFEEN
EKIRILGFPE PHLEIDEKTQ KYFSYQIIEF ESDEDILSIA KSFEQYSQLI LGRTPTQPVV
IQECCFGLVL ASIYFIKYEL FSLPQAHDLI GYNDFFGTSK KHSHFEKVDS CTLINDITSY
YYNNMSSKRK TTIFSNNISF TNLQTTTPPT TTTTTTTTTT TSSSNNSEQI ESTSKNNSSG
ITSPTSIKPK NKVGLLKKLF NKMDKESSNN NNNKEKVEKI KEKKESKKER EAREAKEEKE
REEREKEHQL ALKNIPPAEL YKHHMEQIQK IQKQQIAELN ATSPDGGNDL SNGSNGSKNG
NNNNNNNNSN NNNNNNNSNE PNSQHQNHNP ITNLMDQELI ENYDDGSDRM KNSKTIISPN
FESLPDEYKT MVKTWDIKQE SVDEHFEIIL SLLHFHTKQR FYSSDPTNLP DKPKYYNVGN
VCGNCTPPMI LDPAGSGQMV VAKSFYKRPF DQICKKPTNE MKKLYTFREK VGKGGFGTVY
LVRNNMDKSK SRIAIKKLPH VRKKEKKFNV KEIRVLEFTN HPNIITYYNS HMLHDEVWIA
MEFMEGGTLA EASNQYPFQE SNIAYVAREV LQGLAYLHGI QLVHRDLKSQ NIMMTTSGEI
KLIDFGLCAN LSKGERIRMC GSPIWMPPEM IQQKQHGYTC DIWSTAICLL ELANRNNKLR
KNPIKTMFMV GSEGIKDPFE DPHKWSDEFH DIINKCLQMD PHKRPSAQEL LKHPFIQLAD
NKKKMGKILS SIFLKSIVGI
