MKCB_DICDI
ID MKCB_DICDI Reviewed; 714 AA.
AC Q9NGW9; Q54FP0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable serine/threonine-protein kinase mkcB {ECO:0000312|EMBL:AAF65408.1};
DE EC=2.7.11.1;
DE AltName: Full=MAP kinase cascade B {ECO:0000312|dictyBase:DDB_G0290723};
GN Name=mkcB {ECO:0000312|EMBL:AAF65408.1};
GN Synonyms=DG1101 {ECO:0000312|dictyBase:DDB_G0290723};
GN ORFNames=DDB_G0290723;
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:AAF65408.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=NC-4 {ECO:0000312|EMBL:AAF65408.1};
RX PubMed=11553701; DOI=10.1091/mbc.12.9.2590;
RA Iranfar N., Fuller D., Sasik R., Hwa T., Laub M., Loomis W.F.;
RT "Expression patterns of cell-type-specific genes in Dictyostelium.";
RL Mol. Biol. Cell 12:2590-2600(2001).
RN [2] {ECO:0000312|EMBL:EAL62067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL62067.1};
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 -!- TISSUE SPECIFICITY: Expressed at equal levels in prestalk and prespore
CC cells. {ECO:0000269|PubMed:11553701}.
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; AF238312; AAF65408.1; -; Genomic_DNA.
DR EMBL; AAFI02000169; EAL62067.1; -; Genomic_DNA.
DR RefSeq; XP_635572.1; XM_630480.1.
DR AlphaFoldDB; Q9NGW9; -.
DR SMR; Q9NGW9; -.
DR STRING; 44689.DDB0191334; -.
DR PaxDb; Q9NGW9; -.
DR EnsemblProtists; EAL62067; EAL62067; DDB_G0290723.
DR GeneID; 8627796; -.
DR KEGG; ddi:DDB_G0290723; -.
DR dictyBase; DDB_G0290723; mkcB.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_387062_0_0_1; -.
DR InParanoid; Q9NGW9; -.
DR OMA; HTCHIDK; -.
DR PRO; PR:Q9NGW9; -.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..714
FT /note="Probable serine/threonine-protein kinase mkcB"
FT /id="PRO_0000381740"
FT DOMAIN 438..687
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 558
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 444..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 714 AA; 78925 MW; B4AA7C50D11C181F CRC64;
MKSILKKAKH FFHTNETVNG ENGGEKTAKE SESQQHHQQQ QQHDENGANP PDQGVDEASN
VSQSQPTTSA LQTSTSLQPS SSLHQIPQSQ SSLELTTNPT QQLPTTPTKQ LPTPPPPQQP
HSQQQQQQQQ QSQSQLNNND ISISTNTNNT TNNTNNNNNI DSTLTTPVPS SENLATLSTS
TTSEQQPNSQ PTPNNTNTTT SPPPSSASTS NLSTSTTTTT TTTTTTTAAA NENTNTTQEQ
TVSPNKPPQP PNALSQSTTS SSTSSTSLLS STFSKFKIKL GSGSTKNKDS SSAPGTPHIN
NNNNTVSSSN KNRSTLVITP GSVNNNNNNQ NNHKNNNTTP DHPPEEQKPV EKEVITIATL
ADFPEDCQKL IRISGIPEEK LIKNIQILAY VLHFRTGRFF KLVDEPPREP RKKFVSERFN
DGEKLLEPVE PALLKKMYKD SDQVGKGGFG TVYFAKSTKE KRLVAIKKMP HVTKRQQQQN
FREAAILAKC DHPNIVKLHT CHIDKDSNLW IVMEFMEGGT FEEAAKAWKF NENNLAYVAK
ELLKGLQYLH ENHMVHRDLK SANIMMSVEG KVKLIDFGLC EDVATSTPMH MVGSPFWMAP
EMIQQKYHST PVDIWSFAIS LLEMANQRPP MMESAVKAMF TVATDGATGF DDPALWSDCF
KDFLSLCLKQ DPAERATAEE LLKHPFIKKA DSRDNMENIL KKIFLTNSLM NSGF
