MRKB_DICDI
ID MRKB_DICDI Reviewed; 715 AA.
AC Q54MV2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable serine/threonine-protein kinase MARK-B;
DE EC=2.7.11.1;
GN Name=mrkB; ORFNames=DDB_G0285643;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000079; EAL64659.1; -; Genomic_DNA.
DR RefSeq; XP_638191.1; XM_633099.1.
DR AlphaFoldDB; Q54MV2; -.
DR SMR; Q54MV2; -.
DR STRING; 44689.DDB0216238; -.
DR PaxDb; Q54MV2; -.
DR EnsemblProtists; EAL64659; EAL64659; DDB_G0285643.
DR GeneID; 8625237; -.
DR KEGG; ddi:DDB_G0285643; -.
DR dictyBase; DDB_G0285643; mrkB.
DR eggNOG; KOG0583; Eukaryota.
DR eggNOG; KOG0586; Eukaryota.
DR HOGENOM; CLU_386591_0_0_1; -.
DR InParanoid; Q54MV2; -.
DR OMA; INRMIVA; -.
DR Reactome; R-DDI-1632852; Macroautophagy.
DR Reactome; R-DDI-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-DDI-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DDI-200425; Carnitine metabolism.
DR Reactome; R-DDI-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-DDI-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DDI-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DDI-8953750; Transcriptional Regulation by E2F6.
DR PRO; PR:Q54MV2; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005524; F:ATP 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
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; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 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; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..715
FT /note="Probable serine/threonine-protein kinase MARK-B"
FT /id="PRO_0000338410"
FT DOMAIN 65..320
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 666..715
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 24..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 71..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 715 AA; 79988 MW; 3433A4A96CCED882 CRC64;
MATAVSSYND IQLETIQEVS CSTSCSSNST TSSSSNSPKQ NKVSPGYRNK PQQQQHKKGH
KMGNYLLGKT IGSGTSSKVK IGTNILTGKQ YAIKITKPKR IKERKEIERE ISILKRLKHD
NIIQLHDAIY EDDVGRICLI LELVSGGELF DYIVARGRLS EKEGRKFFRQ MLCGLIYCHS
NMVCHRDLKL ENLLVDEDGN LKISDFGYSN IIKPGNLLST FCGSPVYAPP EILLEKRYNG
NEVDIWSMGV ILYAMVTGQL PWTLTDGVQV EGMDRLLRGE FKYPSHVILS DDVKDLINRM
IVAEPVERAT LDEIKTHVWV NKGYDMEPDQ EYNKKVSDRL EKEQQQQTPQ HQQTQQQLQP
QSQLQQHSPR SPKPLFVDTI IGSNRPLNQS SPNLTIPQNK QYVSSNSNIN ININNNNNNN
SNVINNSIKP IQFNSSSCLD EKKINCSAPT SPHSISPQFI SPSPSTSTTP PLSPLSVSGQ
RSPPTFSSNP NIGHIPNNNH NSLSSSQNNI NTSGKNQYHH HHHHQNHHST SLFHNIFKKR
QSVTSVSANS SPVIVSSNGG LNNNNHNNIL HVSSSNINVD GASASAPQFS SSSSKRRFSL
EDIVKAITIR SGKGKNPKIR SMKGPFNSGT TTMLNPIQLI EHIEENLNST QISYRRNFYV
FDCKTLCPRN ETINFEIEVC KVNGMDMYGI KFKRLSGDAW SYSSSCIKIV ESLKL
