MRKA_DICDI
ID MRKA_DICDI Reviewed; 1060 AA.
AC Q54DF2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable serine/threonine-protein kinase MARK-A;
DE EC=2.7.11.1;
GN Name=mrkA; ORFNames=DDB_G0292304;
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; AAFI02000189; EAL61276.1; -; Genomic_DNA.
DR RefSeq; XP_629689.1; XM_629687.1.
DR AlphaFoldDB; Q54DF2; -.
DR SMR; Q54DF2; -.
DR STRING; 44689.DDB0216369; -.
DR PaxDb; Q54DF2; -.
DR PRIDE; Q54DF2; -.
DR EnsemblProtists; EAL61276; EAL61276; DDB_G0292304.
DR GeneID; 8628605; -.
DR KEGG; ddi:DDB_G0292304; -.
DR dictyBase; DDB_G0292304; mrkA.
DR eggNOG; KOG0586; Eukaryota.
DR HOGENOM; CLU_289424_0_0_1; -.
DR InParanoid; Q54DF2; -.
DR OMA; DWVIFED; -.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:Q54DF2; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; IPR015940; UBA.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 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; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1060
FT /note="Probable serine/threonine-protein kinase MARK-A"
FT /id="PRO_0000338409"
FT DOMAIN 109..361
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 488..528
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1008..1057
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 115..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1060 AA; 119681 MW; 0199D58D6B60C4CC CRC64;
METLKEEEQF RNFDTPLLNT PHHLKEETQI QQKEREQQQQ QQQQLQQQLQ LQNERENRNH
NITEELNKIP SSNNSSNSSS PNPLSISVSS SLGSASSIHL TPQGTIGNYL VIKTIGRGQF
GKVKLGYHKK IPNEKVAIKI INKGKLDPET LKMVQREVRI MKLLHHPNII RLYEVIETSR
ALYLIMEYAG EGEVMDFMIA HGVLTESQAR TFFTQIVSAI NYCHSKRAVH RDLKPENLLL
DCNRQIKIID FGLSNVFTPG SYLKTFCGSP TYASPELILR KEYNGPSVDV WSMGVVLFVL
VTGYLPFDGD NYVELFQKIL AGNYTIPSYL THECKSLISR MLVVDPDKRA TMEEIINHPW
LSSTKQIILS TTMTDSLKNL NSCLEQQINV ENLLNQSLNN SNNNNINNIN NINNTMATMN
NSNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNTTTTTN ATTTTPITSP
IQNRNNEELD QEIIEELVGL GFEREELCNS IRQNKYNDAA STYFLLQGKK LRESQQNQTD
NAKKLEKFYS EPLTIPAHVG ENSPLIKYKR HHKRSNTVDS PKSTNTPQYR SSNTQQNNHH
HQQQQQQQQQ QQQQHHHHTQ QQNQQQSQQQ YNNNNHNKPP TPTIVTTQAS TTVNNHISIN
NNNNNNNNNN NNNNSSTPGS NTVSSTQSSS INSSVNPSPL CLSNAVPVSL REKLREKEAT
TTNTTTTTTT TTTTTTNTSS NNSSNQSISS ISPPTSTSPN LQPFSLASTA NNNNNNNNSN
NNSNNNNNNN NNNNNSLNSH IQRRATASSL QQQQQMQQAS NTRRLRSNSS SVADQSQRQE
SRKLEDDWVI FEDYSNDGHR DGQPKNYHLQ PSSLSSHKKQ KSPVHSFLSS FKNILKRSDD
KSFNSSSSNN NTNNNNTTTS VSTNNTPRTL EVDHQNSNNN NQQATSSSPN VTSPSSPSQQ
QQQEPRIVRF VFGVNTTTMK DAPELMQQVL KVVDTFCIPH TKKAPFLIEC ETEGVRFSIE
ICRLPRLSVN GLKFKRIGGS SWRYKSICKD LLSQMKLNSH
