MKCF_DICDI
ID MKCF_DICDI Reviewed; 677 AA.
AC Q55CE0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable serine/threonine-protein kinase mkcF {ECO:0000312|EMBL:EAL72401.1};
DE EC=2.7.11.1;
DE AltName: Full=MAP kinase cascade F {ECO:0000312|dictyBase:DDB_G0270102};
GN Name=mkcF {ECO:0000312|EMBL:EAL72401.1}; ORFNames=DDB_G0270102;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL72401.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL72401.1};
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. Ser/Thr protein
CC kinase family. STE20 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000005; EAL72401.1; -; Genomic_DNA.
DR RefSeq; XP_646541.1; XM_641449.1.
DR AlphaFoldDB; Q55CE0; -.
DR SMR; Q55CE0; -.
DR STRING; 44689.DDB0229970; -.
DR PaxDb; Q55CE0; -.
DR EnsemblProtists; EAL72401; EAL72401; DDB_G0270102.
DR GeneID; 8617507; -.
DR KEGG; ddi:DDB_G0270102; -.
DR dictyBase; DDB_G0270102; mkcF.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_406240_0_0_1; -.
DR InParanoid; Q55CE0; -.
DR OMA; MLWQCFE; -.
DR PhylomeDB; Q55CE0; -.
DR PRO; PR:Q55CE0; -.
DR Proteomes; UP000002195; Chromosome 1.
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:0022607; P:cellular component assembly; IEA:UniProt.
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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; SH3 domain;
KW Transferase.
FT CHAIN 1..677
FT /note="Probable serine/threonine-protein kinase mkcF"
FT /id="PRO_0000381744"
FT DOMAIN 1..58
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 401..646
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 72..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 519
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 407..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 677 AA; 75623 MW; 04E043C278AF1633 CRC64;
MLYLVATGDY KGPSENHLSF TKGQRIEFLE RTENGFIKGK LDGKVGIFPS SLITIETRPL
SIIQNQPIKY STETKDDTGS ISSSTSTSTS SLTTPRAESS KDASGEQQPS TSTINGQSSS
TSPILQSNGT TNTTTSSTSN NNIGDNISEK SFGDYDDTTS NHSKSASRLS VASFSTTTTA
TTTTTTTTTA TSSKDKDKKD KKEKKEKKDK KSKDDDKSEK EGLYRKSKGS SSSSSSSSSS
TKRRYANRKA CEPWVVKKYE DIPEEVKSDM LKEDIPIKDI QDHFKLFLRI LKFITRQKIT
LLIPIDPTIP TKEMNLLDLS DAESVAKSTT MFTREEIRTS AFDNVDAFVD APIMDDNEKA
AKTTEIKLER KRILTGISTE FLGQASTTIR VIPSSDIKKR IKFTHMVGRG QYGKVYDALY
DKKRVCVKVV NYSTPKEQHN VLQEIGFLTQ CDHPNILKYN CSVLYGSDLF IVSEFIQGGT
LEQASASSHV FKETQVGFIG LELLKAISYL HEKKLIHRDI KAANVMVSTD GEVKLIDFGL
CASVEKGGSQ HMVGSPYYMS PEMIRGEECS YPSDIWSFGI CILELLFKKP PHRDSRMKAM
FYNAINGIDF PKIRCSIDLK DMLWQCFESN PEKRSTVDKL MRHPFFKRCE SKSQMKSVFT
DMFSTSSKNS ISTTGFF
